|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-200 |
1.73e-116 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 329.46 E-value: 1.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLG 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTADENLAFYHP---QTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTAL 157
Cdd:PRK13538 81 HQPGIKTELTALENLRFYQRlhgPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 158 DAAGVATLTRRLEAHAARGGAVIVTTHQPLAF-NVAHRTLTLTP 200
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDLPVaSDKVRKLRLGQ 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
1.41e-93 |
|
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: 271.66 E-value: 1.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTADENLAFYH----PQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTA 156
Cdd:COG4133 82 HADGLKPELTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 157 LDAAGVATLTRRLEAHAARGGAVIVTTHQPLAFNvAHRTLTLTP 200
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELA-AARVLDLGD 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-187 |
7.10e-81 |
|
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: 239.18 E-value: 7.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGH 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAALTADENLAFYHP--QTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*...
gi 1354918145 160 AGVATLTRRLEAHAARGGAVIVTTHQPL 187
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-187 |
8.06e-81 |
|
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: 239.32 E-value: 8.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGH 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAALTADENLAFYHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG 161
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*.
gi 1354918145 162 VATLTRRLEAHAARGGAVIVTTHQPL 187
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQDL 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-203 |
6.09e-62 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 191.24 E-value: 6.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEP--LAHQRSAFHqellW 78
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDidDPDVAEACH----Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 79 LGHLPGIKAALTADENLAF---YHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEFwaaFLGGEELDIA-AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1354918145 156 ALDAAGVATLTRRLEAHAARGGAVIVTTHQPLAFNVAhRTLTLTPEPA 203
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPGA-RELDLGPFAA 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
3.20e-52 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 166.66 E-value: 3.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTADENLAF-YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:PRK13540 81 HRSGINPYLTLRENCLYdIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|...
gi 1354918145 160 AGVATLTRRLEAHAARGGAVIVTTHQPLAFNVA 192
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-202 |
2.17e-46 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 151.93 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHqeLLWLG 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF--MAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTADENLAF---YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTAL 157
Cdd:PRK13543 89 HLPGLKADLSTLENLHFlcgLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1354918145 158 DAAGVATLTRRLEAHAARGGAVIVTTHQPL-AFNVAHRTLTLTPEP 202
Cdd:PRK13543 169 DLEGITLVNRMISAHLRGGGAALVTTHGAYaAPPVRTRMLTLEAAA 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-186 |
2.55e-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: 147.70 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTADENLAFY---HPQTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:COG4555 81 DERGLYDRLTVRENIRYFaelYGLFDEELKKRIeelIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 155 TALDAAGVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIM 192
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-184 |
6.93e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.37 E-value: 6.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH---------QRSA 71
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRarrrigyvpQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 FH-------QELLWLGHLPGIkaaltadeNLAFYHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSE 144
Cdd:COG1121 86 VDwdfpitvRDVVLMGRYGRR--------GLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1354918145 145 ASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTH 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-184 |
8.75e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.58 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAALTADENLAFY- 98
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEPALYPDLTVRENLRFFa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 99 ----HPQTRRETRW-QALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHA 173
Cdd:COG1131 99 rlygLPRKEARERIdELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELA 178
|
170
....*....|.
gi 1354918145 174 ARGGAVIVTTH 184
Cdd:COG1131 179 AEGKTVLLSTH 189
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-194 |
5.74e-36 |
|
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: 126.31 E-value: 5.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRS-AFHQELLWL 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHLPGIKAALTADENLAFY-HPQTRRETRW---------QALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWV 149
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGrYPHLGLFGRPsaedreaveEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1354918145 150 LDEPLTALDAA---GVATLTRRLeaHAARGGAVIVTTHQP-LAFNVAHR 194
Cdd:COG1120 161 LDEPTSHLDLAhqlEVLELLRRL--ARERGRTVVMVLHDLnLAARYADR 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-198 |
6.22e-36 |
|
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: 123.51 E-value: 6.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 3 EARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqrsafhqellwlghl 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 pgikaaltadenlafyhpqtrRETRWQALAAIGLggyedlpVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGV 162
Cdd:cd00267 65 ---------------------KLPLEELRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 163 ATLTRRLEAHAARGGAVIVTTHQP-LAFNVAHRTLTL 198
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPeLAELAADRVIVL 153
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-198 |
6.24e-35 |
|
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: 123.21 E-value: 6.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLA-CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-AHQRSAFHQellwl 79
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 ghlpgiKAAL------------TADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLW 141
Cdd:COG1122 76 ------KVGLvfqnpddqlfapTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1354918145 142 LSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP-LAFNVAHRTLTL 198
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLdLVAELADRVIVL 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-198 |
1.48e-34 |
|
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: 121.42 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-------QRSAF------HQeLL 77
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslkelrRKVGLvfqnpdDQ-FF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 78 wlghlpgikaALTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLD 151
Cdd:cd03225 90 ----------GPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1354918145 152 EPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP-LAFNVAHRTLTL 198
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLdLLLELADRVIVL 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-184 |
1.09e-33 |
|
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: 118.27 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAALTADENLafyh 99
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYENLTVRENL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 100 pqtrretrwqalaaiglggyedlpveQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAV 179
Cdd:cd03230 95 --------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI 148
|
....*
gi 1354918145 180 IVTTH 184
Cdd:cd03230 149 LLSSH 153
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-155 |
2.17e-33 |
|
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: 116.59 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQ-RSAFHQELLWLGHLPGIKAALTADENL 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 96 AF----YHPQTRRETRW--QALAAIGLGGYEDLPVE----QLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:pfam00005 81 RLglllKGLSKREKDARaeEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-184 |
5.40e-33 |
|
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: 117.63 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 3 EARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSafhqellWLGHL 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-------RIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 PGIKAA-----LTADENLA--------FYHPQTRRETR--WQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASL 147
Cdd:cd03235 74 PQRRSIdrdfpISVRDVVLmglyghkgLFRRLSKADKAkvDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 148 WVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-198 |
1.65e-32 |
|
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: 115.23 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 3 EARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRsafHQEL-LWLGH 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELaRKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPgikaaltadenlafyhpqtrretrwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG 161
Cdd:cd03214 78 VP-------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 1354918145 162 VATLTRRLEAHAA-RGGAVIVTTHQP-LAFNVAHRTLTL 198
Cdd:cd03214 133 QIELLELLRRLAReRGKTVVMVLHDLnLAARYADRVILL 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-198 |
6.04e-32 |
|
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: 121.02 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLR-DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFHQELLWL 79
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHLPGIKAAlTADENLAFYHPQTRRETRWQALAAIGL--------GGYeDLPVE----QLSAGQQRRVALARLWLSEASL 147
Cdd:COG4988 417 PQNPYLFAG-TIRENLRLGRPDASDEELEAALEAAGLdefvaalpDGL-DTPLGeggrGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1354918145 148 WVLDEPLTALDAAGVATLTRRLEAhAARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALLAQADRILVL 544
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-198 |
2.41e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.60 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QRSAF 72
Cdd:COG1136 4 LLELRNLTkSYGTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 73 HQE----------LLwlghlpgikAALTADENLAF---YHPQTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVA 136
Cdd:COG1136 84 RRRhigfvfqffnLL---------PELTALENVALpllLAGVSRKERRERArelLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 137 LARLWLSEASLWVLDEPLTALD---AAGVATLTRRLeaHAARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDsktGEEVLELLREL--NRELGTTIVMVTHDPELAARADRVIRL 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-185 |
5.53e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 109.61 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQellwLGHL---PGIKAALTADENLA 96
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR----IGALieaPGFYPNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 97 FYH--PQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAA 174
Cdd:cd03268 95 LLArlLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD 174
|
170
....*....|.
gi 1354918145 175 RGGAVIVTTHQ 185
Cdd:cd03268 175 QGITVLISSHL 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-185 |
6.13e-30 |
|
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: 109.68 E-value: 6.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLahqrSAFHQELlwLGHLP---GIKAALTADEN 94
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNR--IGYLPeerGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 95 LAFY---HPQTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRR 168
Cdd:cd03269 91 LVYLaqlKGLKKEEARRRIdewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
170
....*....|....*..
gi 1354918145 169 LEAHAARGGAVIVTTHQ 185
Cdd:cd03269 171 IRELARAGKTVILSTHQ 187
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-196 |
2.32e-29 |
|
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: 107.99 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA----HQRS---AFHQ 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTgvppERRNigmVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 75 ELLWlGHLpgikaalTADENLAF-----YHPQTRRETRWQALAA-IGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLW 148
Cdd:cd03259 81 YALF-PHL-------TVAENIAFglklrGVPKAEIRARVRELLElVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1354918145 149 VLDEPLTALDAAGVATLTRRL-EAHAARG-GAVIVTTHQPLAFNVAHRTL 196
Cdd:cd03259 153 LLDEPLSALDAKLREELREELkELQRELGiTTIYVTHDQEEALALADRIA 202
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-194 |
4.16e-29 |
|
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: 108.14 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QRSAFHQEL 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 lwlghlpGI---KAAL----TADENLAF---YH----PQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWL 142
Cdd:COG1127 85 -------GMlfqGGALfdslTVFENVAFplrEHtdlsEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 143 SEASLWVLDEPLTALD---AAGVATLTRRLeaHAARGGAVIVTTHQ-PLAFNVAHR 194
Cdd:COG1127 158 LDPEILLYDEPTAGLDpitSAVIDELIREL--RDELGLTSVVVTHDlDSAFAIADR 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-186 |
4.79e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.18 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPE---EGEVYWRGEPL----AHQRSA-- 71
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLtalpAEQRRIgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 -FHQELLWlghlpgikAALTADENLAFYHPQT-----RRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEA 145
Cdd:COG4136 81 lFQDDLLF--------PHLSVGENLAFALPPTigraqRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1354918145 146 SLWVLDEPLTALDAAGVATlTRRL--EAHAARGGAVIVTTHQP 186
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQ-FREFvfEQIRQRGIPALLVTHDE 194
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-203 |
5.61e-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: 108.25 E-value: 5.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNL----ACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA--HQRSAF-H 73
Cdd:COG1116 7 ALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTgpGPDRGVvF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 QE--LL-WLghlpgikaalTADENLAF-------YHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLS 143
Cdd:COG1116 87 QEpaLLpWL----------TVLDNVALglelrgvPKAERRERAR-ELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354918145 144 EASLWVLDEPLTALDAagvatLTRR------LEAHAARGGAVIVTTHQPL-AFNVAHRTLTLTPEPA 203
Cdd:COG1116 156 DPEVLLMDEPFGALDA-----LTRErlqdelLRLWQETGKTVLFVTHDVDeAVFLADRVVVLSARPG 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-194 |
1.06e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.42 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRSA---FH 73
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglpPEKRNVgmvFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 QELLWlGHlpgikaaLTADENLAFY-----HPQTRRETRWQ-ALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASL 147
Cdd:COG3842 85 DYALF-PH-------LTVAENVAFGlrmrgVPKAEIRARVAeLLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1354918145 148 WVLDEPLTALDA---AGVATLTRRLeaHAARGGAVIVTTHQPL-AFNVAHR 194
Cdd:COG3842 157 LLLDEPLSALDAklrEEMREELRRL--QRELGITFIYVTHDQEeALALADR 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-198 |
1.72e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.29 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAF-----------HQELLWL 79
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrrigvvFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHlpgikaaLTADENLAF---YHPQTRRETRWQALAAI---GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:COG2884 92 PD-------RTVYENVALplrVTGKSRKEIRRRVREVLdlvGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1354918145 154 LTALDAAGVATLTRRLEAHAARGGAVIVTTH-QPLAFNVAHRTLTL 198
Cdd:COG2884 165 TGNLDPETSWEIMELLEEINRRGTTVLIATHdLELVDRMPKRVLEL 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-198 |
1.82e-28 |
|
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: 106.03 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QRSAFH--------QELLWLGHlpgikaa 88
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekELAAFRrrhigfvfQSFNLLPD------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTADENLA---FYHPQTRRETRWQALAA---IGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD---A 159
Cdd:cd03255 97 LTALENVElplLLAGVPKKERRERAEELlerVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDsetG 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1354918145 160 AGVATLTRRLeaHAARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:cd03255 177 KEVMELLREL--NKEAGTTIVVVTHDPELAEYADRIIEL 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-185 |
5.24e-28 |
|
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: 105.28 E-value: 5.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAfhqELLWLGH 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEA---ELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGI---KAAL----TADENLAFYHPQTRRETRW-------QALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASL 147
Cdd:cd03261 78 RMGMlfqSGALfdslTVFENVAFPLREHTRLSEEeireivlEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1354918145 148 WVLDEPLTALD--AAGV-ATLTRRLeaHAARGGAVIVTTHQ 185
Cdd:cd03261 158 LLYDEPTAGLDpiASGViDDLIRSL--KKELGLTSIMVTHD 196
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-194 |
5.47e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 105.52 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAC-LRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQEL--- 76
Cdd:COG3638 2 MLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 ---LW-------------------LGHLPGIKAALtadenlAFYHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRR 134
Cdd:COG3638 82 igmIFqqfnlvprlsvltnvlagrLGRTSTWRSLL------GLFPPEDRERAL-EALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1354918145 135 VALARLWLSEASLWVLDEPLTALD---AAGVATLTRRLeaHAARGGAVIVTTHQP-LAFNVAHR 194
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDpktARQVMDLLRRI--AREDGITVVVNLHQVdLARRYADR 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-198 |
8.75e-28 |
|
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: 109.30 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFHQELLWLGHLPGIKAAL 89
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TAdENLAFYHPQTRRETRWQALAAIGLGGY-EDLPV----------EQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:TIGR02857 412 IA-ENIRLARPDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1354918145 159 AAGVATLTRRLEAhAARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:TIGR02857 491 AETEAEVLEALRA-LAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-185 |
1.50e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.58 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNL--------AcLRDerllfraLSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL--AHQR- 69
Cdd:COG4152 1 MLELKGLtkrfgdktA-VDD-------VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpEDRRr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 70 --------------SAFHQeLLWLGHLPGIKAAlTADENLAFYhpqtrretrwqaLAAIGLGGYEDLPVEQLSAGQQRRV 135
Cdd:COG4152 73 igylpeerglypkmKVGEQ-LVYLARLKGLSKA-EAKRRADEW------------LERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1354918145 136 ALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQ 185
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-184 |
2.47e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 103.73 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAC----LRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQR------- 69
Cdd:COG1124 1 MLEVRNLSVsygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 70 ---------SAFHqellwlghlP--GIKAALtaDENLAFYHPQTRRETRWQALAAIGLG-GYEDLPVEQLSAGQQRRVAL 137
Cdd:COG1124 81 vqmvfqdpyASLH---------PrhTVDRIL--AEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1354918145 138 ARLWLSEASLWVLDEPLTALDA---AGVATLTRRLeaHAARGGAVIVTTH 184
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVsvqAEILNLLKDL--REERGLTYLFVSH 197
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-198 |
4.03e-27 |
|
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: 107.61 E-value: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFHQellWLGHLP------- 83
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRR---QIGVVLqdvflfs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 84 GikaalTADENLAFYHPQTRRETRWQALAAIGL--------GGYeDLPV----EQLSAGQQRRVALARLWLSEASLWVLD 151
Cdd:COG2274 563 G-----TIRENITLGDPDATDEEIIEAARLAGLhdfiealpMGY-DTVVgeggSNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1354918145 152 EPLTALDAAGVATLTRRLEAHaARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:COG2274 637 EATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVL 682
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-198 |
1.43e-26 |
|
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: 100.79 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH---QRSAF-------HQ------ 74
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkerRKSIGyvmqdvdYQlftdsv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 75 --ELLwLGhlpgikaaltaDENLAFYHPQTRretrwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDE 152
Cdd:cd03226 90 reELL-LG-----------LKELDAGNEQAE-----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1354918145 153 PLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP-LAFNVAHRTLTL 198
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYeFLAKVCDRVLLL 199
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-186 |
2.02e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 100.33 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFrALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFhqeLLWLG 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTADENLAFYHP-QTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEiYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180
....*....|....*....|....*..
gi 1354918145 160 AGVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:PRK13541 157 ENRDLLNNLIVMKANSGGIVLLSSHLE 183
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-194 |
9.49e-26 |
|
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: 99.43 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRSAfhqellwLG-----HLPG 84
Cdd:cd03219 13 LVALddvSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglpPHEIAR-------LGigrtfQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 85 IKAALTADENL-------------AFYHPQTRRETR---WQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLW 148
Cdd:cd03219 86 LFPELTVLENVmvaaqartgsgllLARARREEREAReraEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1354918145 149 VLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH-QPLAFNVAHR 194
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHdMDVVMSLADR 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-186 |
1.07e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.06 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDErLLFRAlSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA-------Fh 73
Cdd:COG3840 1 MLRLDDLTYRYGD-FPLRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvsmlF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 QE--LLWlgHLpgikaalTADENLAF-YHPQTR-----RETRWQALAAIGLGGYED-LPvEQLSAGQQRRVALARLWLSE 144
Cdd:COG3840 78 QEnnLFP--HL-------TVAQNIGLgLRPGLKltaeqRAQVEQALERVGLAGLLDrLP-GQLSGGQRQRVALARCLVRK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1354918145 145 ASLWVLDEPLTALDAA---GVATLTRRLeaHAARGGAVIVTTHQP 186
Cdd:COG3840 148 RPILLLDEPFSALDPAlrqEMLDLVDEL--CRERGLTVLMVTHDP 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-198 |
1.60e-25 |
|
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: 102.92 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFHQELLWLGHLPGIKAAlTA 91
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLAFYHPQTRRETRWQALAAIGLGGY-EDLPV----------EQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:COG4987 426 RENLRLARPDATDEELWAALERVGLGDWlAALPDgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAA 505
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 161 GVATLTRRLEAHaARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:COG4987 506 TEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVL 542
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-203 |
1.94e-25 |
|
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: 98.31 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA----FHQELL--WlghlpgikaaLTADE 93
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDrgyvFQQDALlpW----------LTVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAF---YHPQTRRETRWQALAAI---GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAagvatLTR 167
Cdd:cd03293 93 NVALgleLQGVPKAEARERAEELLelvGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDA-----LTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 168 R------LEAHAARGGAVIVTTHQpL--AFNVAHRTLTLTPEPA 203
Cdd:cd03293 168 EqlqeelLDIWRETGKTVLLVTHD-IdeAVFLADRVVVLSARPG 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-198 |
2.21e-25 |
|
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: 96.87 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRsafhqellwlgh 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 lpGIKAALTADENLAFYHPQ-----TRRETrwqalaaIGLGgyedlpveqLSAGQQRRVALARLWLSEASLWVLDEPLTA 156
Cdd:cd03229 69 --DELPPLRRRIGMVFQDFAlfphlTVLEN-------IALG---------LSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 157 LDAAGVATLTRRLEA-HAARGGAVIVTTHQP-LAFNVAHRTLTL 198
Cdd:cd03229 131 LDPITRREVRALLKSlQAQLGITVVLVTHDLdEAARLADRVVVL 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-184 |
2.74e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.00 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAfhqeLLWL 79
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS----LLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHLPGIKA--------ALTADENLAFYH-----PQTRRETR-WQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEA 145
Cdd:PRK13639 77 RKTVGIVFqnpddqlfAPTVEEDVAFGPlnlglSKEEVEKRvKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1354918145 146 SLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-184 |
7.12e-25 |
|
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: 96.67 E-value: 7.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFRA---LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQEL 76
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAvdgVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 LWLGHLPGIKAALTADENLAFY---HPQTRRE--TRWQALAA-IGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVL 150
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFaglYGLKGDEltARLEELADrLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 1354918145 151 DEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-184 |
8.90e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 8.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 4 ARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGE----------PLAHQRSAFH 73
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqepPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 QELLWLGHLPGIKAAL-TADENLAFYHPQTRRETRWQA-LAAigLGGYE-------------------DLPVEQLSAGQQ 132
Cdd:COG0488 81 TVLDGDAELRALEAELeELEAKLAEPDEDLERLAELQEeFEA--LGGWEaearaeeilsglgfpeedlDRPVSELSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 133 RRVALARLWLSEASLWVLDEPLTALDAAGVAtltrRLEAH-AARGGAVIVTTH 184
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIE----WLEEFlKNYPGTVLVVSH 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-184 |
1.41e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWrGEPLahQRSAFHQellwlg 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--KIGYFDQ------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTADENLAFYHPQTRRETRWQALAAIGLGGyEDL--PVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:COG0488 386 HQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSG-DDAfkPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
170 180
....*....|....*....|....*.
gi 1354918145 159 aagVATLTRRLEAHAARGGAVIVTTH 184
Cdd:COG0488 465 ---IETLEALEEALDDFPGTVLLVSH 487
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-194 |
2.04e-24 |
|
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: 94.03 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPlahqrsafhqellwlghlpgikaaltade 93
Cdd:cd03216 13 VKALdgvSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 nlafYHPQTRREtrwqALAA-IGLggyedlpVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAH 172
Cdd:cd03216 64 ----VSFASPRD----ARRAgIAM-------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170 180
....*....|....*....|...
gi 1354918145 173 AARGGAVIVTTHQ-PLAFNVAHR 194
Cdd:cd03216 129 RAQGVAVIFISHRlDEVFEIADR 151
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-184 |
2.63e-24 |
|
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: 95.26 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQEL--------LWLGhlpgikaaLTA 91
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgycpqfdaLFDE--------LTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLAFY------HPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAgvatl 165
Cdd:cd03263 93 REHLRFYarlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA----- 167
|
170 180
....*....|....*....|...
gi 1354918145 166 TRR----LEAHAARGGAVIVTTH 184
Cdd:cd03263 168 SRRaiwdLILEVRKGRSIILTTH 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-198 |
3.02e-24 |
|
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: 95.27 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNL-ACLRDERLLFRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QRSAF 72
Cdd:cd03257 1 LLEVKNLsVSFPTGGGSVKALddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 73 HQELLWLGHLPG--------IKAALTadENLAFYHPQTRRETRWQA--LAAIGLGGYED----LPvEQLSAGQQRRVALA 138
Cdd:cd03257 81 RKEIQMVFQDPMsslnprmtIGEQIA--EPLRIHGKLSKKEARKEAvlLLLVGVGLPEEvlnrYP-HELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1354918145 139 RLWLSEASLWVLDEPLTALDA---AGVATLTRRLeaHAARGGAVIVTTHQ-PLAFNVAHRTLTL 198
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVsvqAQILDLLKKL--QEELGLTLLFITHDlGVVAKIADRVAVM 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-184 |
3.25e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.82 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAC--LRDERLLFRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRsafHQE 75
Cdd:COG1123 260 LLEVRNLSKryPVRGKGGVRAVddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS---RRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 76 LLWLGHLPGI-----KAAL----TADENLAF---YHPQTRRETRW----QALAAIGLG-GYEDLPVEQLSAGQQRRVALA 138
Cdd:COG1123 337 LRELRRRVQMvfqdpYSSLnprmTVGDIIAEplrLHGLLSRAERRervaELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1354918145 139 RLWLSEASLWVLDEPLTALDA---AGVATLTRRLeaHAARGGAVIVTTH 184
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVsvqAQILNLLRDL--QRELGLTYLFISH 463
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-184 |
5.03e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-------AHQR--SAFHQEL--------- 76
Cdd:COG1129 18 KALdgvSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprdAQAAgiAIIHQELnlvpnlsva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 --LWLGHLPGIKAALtaDenlafyHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:COG1129 98 enIFLGREPRRGGLI--D------WRAMRRRAR-ELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 155 TALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:COG1129 169 ASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-198 |
5.38e-24 |
|
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: 94.40 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRS------------AFhQELLWLGHLpgika 87
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylrrkigvVF-QDFRLLPDR----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 alTADENLAF-----YHPqtRRETRWQ---ALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:cd03292 94 --NVYENVAFalevtGVP--PREIRKRvpaALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1354918145 160 AGVATLTRRLEAHAARGGAVIVTTH-QPLAFNVAHRTLTL 198
Cdd:cd03292 170 DTTWEIMNLLKKINKAGTTVVVATHaKELVDTTRHRVIAL 209
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-184 |
6.50e-24 |
|
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: 92.13 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWrgeplahqrsafhqellwlghLPGIKAalta 91
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW---------------------GSTVKI---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 denlafyhpqtrretrwqalaaiglgGYedlpVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEA 171
Cdd:cd03221 66 --------------------------GY----FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
170
....*....|...
gi 1354918145 172 HAargGAVIVTTH 184
Cdd:cd03221 116 YP---GTVILVSH 125
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-198 |
7.72e-24 |
|
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: 92.83 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFHQELLWLGHlpgiKAALT 90
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQ----DPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 AD---ENLafyhpqtrretrwqalaaiglggyedlpveqLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTR 167
Cdd:cd03228 89 SGtirENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|.
gi 1354918145 168 RLEAHaARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:cd03228 138 ALRAL-AKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-159 |
1.37e-23 |
|
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: 93.46 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQR---SAFhQELLWLGHLpgikaalTAD 92
Cdd:cd03300 19 VSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlpPHKRpvnTVF-QNYALFPHL-------TVF 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 93 ENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:cd03300 91 ENIAFglrlkkLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-186 |
1.54e-23 |
|
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: 94.00 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEG-EVYWRGEPLAH-------QR--- 69
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGedvwelrKRigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 70 --SAFHQELlwLGHLPGIKAALTadenlAFY-------HPQTRRETR-WQALAAIGLGGYEDLPVEQLSAGQQRRVALAR 139
Cdd:COG1119 83 vsPALQLRF--PRDETVLDVVLS-----GFFdsiglyrEPTDEQRERaRELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1354918145 140 LWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGG-AVIVTTHQP 186
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHV 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-194 |
1.86e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA--------FHQELLWlGHLpgi 85
Cdd:COG1118 15 FTLLddvSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgfvFQHYALF-PHM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 86 kaalTADENLAF---YHPQTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:COG1118 91 ----TVAENIAFglrVRPPSKAEIRARVeelLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 160 AgVATLTRRL--EAHAARGGAVIVTTHQPL-AFNVAHR 194
Cdd:COG1118 167 K-VRKELRRWlrRLHDELGGTTVFVTHDQEeALELADR 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-199 |
2.18e-23 |
|
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: 92.74 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 26 PGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----------AHQR--SAFHQELLWLGHLpgikaalTADE 93
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlpPQQRkiGLVFQQYALFPHL-------NVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAF-YHPQTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRL 169
Cdd:cd03297 95 NLAFgLKRKRNREDRISVdelLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 170 -EAHAARGGAVIVTTHQPL-AFNVAHRTLTLT 199
Cdd:cd03297 175 kQIKKNLNIPVIFVTHDLSeAEYLADRIVVME 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-184 |
4.10e-23 |
|
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: 91.87 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 14 RLLFRALSFRVSPGeIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQEllwLGHLP---GIKAALT 90
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR---IGYLPqefGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAFY------HPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVAT 164
Cdd:cd03264 89 VREFLDYIawlkgiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR 168
|
170 180
....*....|....*....|
gi 1354918145 165 LtRRLEAHAARGGAVIVTTH 184
Cdd:cd03264 169 F-RNLLSELGEDRIVILSTH 187
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-186 |
5.24e-23 |
|
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: 92.25 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----------AHQRSAF-HQELLWLGHLPGIKAAL 89
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqLRRQIGMiFQQFNLIERLSVLENVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TADEN--------LAFYHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAg 161
Cdd:cd03256 101 SGRLGrrstwrslFGLFPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPA- 178
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 162 vatLTRR-----LEAHAARGGAVIVTTHQP 186
Cdd:cd03256 179 ---SSRQvmdllKRINREEGITVIVSLHQV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-184 |
5.66e-23 |
|
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: 91.66 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGH 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAALTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:cd03265 81 DLSVDDELTGWENLYIharlygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 156 ALDAAGVATLTRRLEAHAARGG-AVIVTTH 184
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGmTILLTTH 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-184 |
9.47e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 9.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVY--------WRGEPLAHQRSAF 72
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 73 HQ-----------ELLWLGHLPGiKAALTADENLAFyhpqtrretrwQALAAIGLGGYEDLPVEQLSAGQQRRVALAR-- 139
Cdd:PRK13548 82 PQhsslsfpftveEVVAMGRAPH-GLSRAEDDALVA-----------AALAQVDLAHLAGRDYPQLSGGEQQRVQLARvl 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1354918145 140 --LWLSEA--SLWVLDEPLTALDAA---GVATLTRRLeAHaARGGAVIVTTH 184
Cdd:PRK13548 150 aqLWEPDGppRWLLLDEPTSALDLAhqhHVLRLARQL-AH-ERGLAVIVVLH 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-184 |
1.39e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 19 ALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAALTADENLAFY 98
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 99 HPQTRRETRwQALAAIG-------LGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEA 171
Cdd:PRK13536 139 GRYFGMSTR-EIEAVIPsllefarLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRS 217
|
170
....*....|...
gi 1354918145 172 HAARGGAVIVTTH 184
Cdd:PRK13536 218 LLARGKTILLTTH 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-194 |
2.53e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.87 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLaclrdeRLLFRAL------SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRS 70
Cdd:COG0411 4 LLEVRGL------TKRFGGLvavddvSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 71 A------------FHQ----ELLWLGHLPGIKAALTADENLAFYHPQTRRETR---WQALAAIGLGGYEDLPVEQLSAGQ 131
Cdd:COG0411 78 RlgiartfqnprlFPEltvlENVLVAAHARLGRGLLAALLRLPRARREEREAReraEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 132 QRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRL-EAHAARGGAVIVTTHQ-PLAFNVAHR 194
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIrRLRDERGITILLIEHDmDLVMGLADR 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-186 |
2.90e-22 |
|
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: 89.15 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDE------RLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPE--EGEVYWRGEPLAHQ----R 69
Cdd:cd03213 4 LSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRsfrkI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 70 SAF-HQELLWLGHlpgikaaLTADENLAFyhpqtrretrwqalaAIGLGGyedlpveqLSAGQQRRVALARLWLSEASLW 148
Cdd:cd03213 84 IGYvPQDDILHPT-------LTVRETLMF---------------AAKLRG--------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 149 VLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQP 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-184 |
5.09e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLfRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRS---AFHQELLWLGHLPGIKA 87
Cdd:PRK13638 12 QDEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 ALT-ADENLAFYHPQ--------TRRETrwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK13638 91 FYTdIDSDIAFSLRNlgvpeaeiTRRVD--EALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180
....*....|....*....|....*.
gi 1354918145 159 AAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-194 |
9.32e-22 |
|
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: 89.63 E-value: 9.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqrSAFHQELLWL------------GHLPgi 85
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA---AMSRKELRELrrkkismvfqsfALLP-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 86 kaALTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:cd03294 116 --HRTVLENVAFglevqgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1354918145 160 agvatLTRR------LEAHAARGGAVIVTTHQPL-AFNVAHR 194
Cdd:cd03294 194 -----LIRRemqdelLRLQAELQKTIVFITHDLDeALRLGDR 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-198 |
9.71e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.42 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFHQELLWLGHLPGIKAAlT 90
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAFYHPQTRRETRWQALAAIGLG--------GYeDLPV----EQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:cd03245 94 LRDNITLGAPLADDERILRAAELAGVTdfvnkhpnGL-DLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1354918145 159 AAGVATLTRRLEAhAARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:cd03245 173 MNSEERLKERLRQ-LLGDKTLIIITHRPSLLDLVDRIIVM 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-199 |
1.04e-21 |
|
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: 88.75 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA----HQRSAfhqelL 77
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmHKRAR-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 78 WLGHLP---GIKAALTADENLA-----FYHPQTRRETRWQA-LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLW 148
Cdd:cd03218 76 GIGYLPqeaSIFRKLTVEENILavleiRGLSKKEREEKLEElLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1354918145 149 VLDEPLTALDAAGVA---TLTRRLeahAARGGAVIVTTHqplafNVaHRTLTLT 199
Cdd:cd03218 156 LLDEPFAGVDPIAVQdiqKIIKIL---KDRGIGVLITDH-----NV-RETLSIT 200
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-194 |
1.96e-21 |
|
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: 87.49 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSafHQEL-LWLGHLP---GIKAALTADE 93
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP--HERArAGIGYVPegrRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAF-YHPQTRRETRWQaLAAIglggYEDLPV---------EQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVA 163
Cdd:cd03224 95 NLLLgAYARRRAKRKAR-LERV----YELFPRlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 164 TLTRRLEAHAARGGAVI-VTTHQPLAFNVAHR 194
Cdd:cd03224 170 EIFEAIRELRDEGVTILlVEQNARFALEIADR 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-184 |
2.92e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.09 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGH 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAALTADENLAFY------HPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFgryfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180
....*....|....*....|....*....
gi 1354918145 156 ALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-153 |
3.20e-21 |
|
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: 87.34 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRSAfhqel 76
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpPHRIAR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 LWLGHLP---GIKAALTADENL--AFYHPQTRRETRWqALAAIglggYEDLPV---------EQLSAGQQRRVALARLWL 142
Cdd:COG0410 78 LGIGYVPegrRIFPSLTVEENLllGAYARRDRAEVRA-DLERV----YELFPRlkerrrqraGTLSGGEQQMLAIGRALM 152
|
170
....*....|.
gi 1354918145 143 SEASLWVLDEP 153
Cdd:COG0410 153 SRPKLLLLDEP 163
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-184 |
9.27e-21 |
|
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: 86.17 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA----HQRSAfhqelL 77
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlpmHERAR-----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 78 WLGHLP-------------GIKAALTADENLafyhPQTRRETRWQAL-AAIGLGGYEDLPVEQLSAGQQRRVALARLWLS 143
Cdd:TIGR04406 77 GIGYLPqeasifrkltveeNIMAVLEIRKDL----DRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1354918145 144 EASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-198 |
1.02e-20 |
|
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: 84.58 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLaCLR---DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELlw 78
Cdd:cd03246 1 LEVENV-SFRypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 79 LGHLPgikaaltADENLafyHPQTRREtrwqalaAIglggyedlpveqLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:cd03246 78 VGYLP-------QDDEL---FSGSIAE-------NI------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1354918145 159 AAGVATLTRRLEAHAARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-198 |
1.82e-20 |
|
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: 85.18 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLaCLR----DERL-LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QRSA 71
Cdd:COG4181 8 IIELRGL-TKTvgtgAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 FHQELLwlG------HLpgiKAALTADENLA-----FYHPQTRRETRwQALAAIGLGGYED-LPVeQLSAGQQRRVALAR 139
Cdd:COG4181 87 LRARHV--GfvfqsfQL---LPTLTALENVMlplelAGRRDARARAR-ALLERVGLGHRLDhYPA-QLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 140 LWLSEASLWVLDEPLTALDAA---GVATLTRRLeaHAARGGAVIVTTH-QPLAfNVAHRTLTL 198
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAAtgeQIIDLLFEL--NRERGTTLVLVTHdPALA-ARCDRVLRL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-184 |
2.39e-20 |
|
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: 86.29 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAALTADENL-- 95
Cdd:TIGR01188 10 DGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLem 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 96 --AFY-HPQTRRETRW-QALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEA 171
Cdd:TIGR01188 90 mgRLYgLPKDEAEERAeELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRA 169
|
170
....*....|...
gi 1354918145 172 HAARGGAVIVTTH 184
Cdd:TIGR01188 170 LKEEGVTILLTTH 182
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-198 |
4.37e-20 |
|
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: 84.70 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKaALTADE 93
Cdd:cd03296 15 FVALddvSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFR-HMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAFYHPQTRRETRWQA----------LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVA 163
Cdd:cd03296 94 NVAFGLRVKPRSERPPEaeirakvhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 164 TLTRRL-EAHAARGGAVIVTTH-QPLAFNVAHRTLTL 198
Cdd:cd03296 174 ELRRWLrRLHDELHVTTVFVTHdQEEALEVADRVVVM 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-186 |
4.44e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGE---PLAHQrSAFHQEllwlghlpgikaaLT 90
Cdd:COG1134 39 FWALkdvSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLLELG-AGFHPE-------------LT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAFY---HPQTRRETRwQALAAI----GLGGYEDLPVEQLSAGQQRRVALArlwLS---EASLWVLDEPLTALDAA 160
Cdd:COG1134 105 GRENIYLNgrlLGLSRKEID-EKFDEIvefaELGDFIDQPVKTYSSGMRARLAFA---VAtavDPDILLVDEVLAVGDAA 180
|
170 180
....*....|....*....|....*.
gi 1354918145 161 GVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:COG1134 181 FQKKCLARIRELRESGRTVIFVSHSM 206
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
17-194 |
4.90e-20 |
|
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: 86.24 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA-------FHQELLWlghlPGik 86
Cdd:TIGR03265 17 FTALkdiSLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQkrdygivFQSYALF----PN-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 aaLTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:TIGR03265 91 --LTVADNIAYglknrgMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 1354918145 161 GVATLTRRLEAHAARGG--AVIVTTHQPLAFNVAHR 194
Cdd:TIGR03265 169 VREHLRTEIRQLQRRLGvtTIMVTHDQEEALSMADR 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-194 |
5.42e-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: 83.84 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGE-----PLAHQRSA--FHQ 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRDIAmvFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 75 ELLWlGHLpgikaalTADENLAFyhPQTRRETRWQALAA--------IGLGGYEDLPVEQLSAGQQRRVALARLWLSEAS 146
Cdd:cd03301 81 YALY-PHM-------TVYDNIAF--GLKLRKVPKDEIDErvrevaelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1354918145 147 LWVLDEPLTALDAA-GVATLTRRLEAHAARGGAVIVTTH-QPLAFNVAHR 194
Cdd:cd03301 151 VFLMDEPLSNLDAKlRVQMRAELKRLQQRLGTTTIYVTHdQVEAMTMADR 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-167 |
8.19e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.14 E-value: 8.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNL----ACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH---QRSAFH 73
Cdd:COG4525 3 MLTVRHVsvryPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgaDRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 QE---LLWLghlpgikaalTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSE 144
Cdd:COG4525 83 QKdalLPWL----------NVLDNVAFglrlrgVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180
....*....|....*....|...
gi 1354918145 145 ASLWVLDEPLTALDAagvatLTR 167
Cdd:COG4525 153 PRFLLMDEPFGALDA-----LTR 170
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-186 |
8.64e-20 |
|
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: 83.35 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqrsafhqeLLWLGHlpGIKAALT 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---------LLGLGG--GFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAFY---HPQTRRETRwQALAAI----GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVA 163
Cdd:cd03220 101 GRENIYLNgrlLGLSRKEID-EKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180
....*....|....*....|...
gi 1354918145 164 TLTRRLEAHAARGGAVIVTTHQP 186
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDP 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-159 |
2.48e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QRS---AFhQELLWLGHLpgikaalTAD 92
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsiqQRDicmVF-QSYALFPHM-------SLG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 93 ENLAF-----YHPQTRRETRWQ-ALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:PRK11432 97 ENVGYglkmlGVPKEERKQRVKeALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-184 |
8.30e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.81 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA-------FHQELLWlghlPgikaALTAD 92
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrniamvFQSYALY----P----HMTVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 93 ENLAFY-----HPQTRRETRWQALAAI-GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLT 166
Cdd:COG3839 94 ENIAFPlklrkVPKAEIDRRVREAAELlGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMR 173
|
170
....*....|....*....
gi 1354918145 167 RRL-EAHAARGGAVIVTTH 184
Cdd:COG3839 174 AEIkRLHRRLGTTTIYVTH 192
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-204 |
1.13e-18 |
|
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: 80.59 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH---QRSAFHQE---LLWLGHLPGIkaALTADE 93
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNyslLPWLTVRENI--ALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAFYHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLE--A 171
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMqiW 161
|
170 180 190
....*....|....*....|....*....|...
gi 1354918145 172 HAARGGAVIVTTHQPLAFNVAHRTLTLTPEPAA 204
Cdd:TIGR01184 162 EEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAA 194
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-185 |
1.23e-18 |
|
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: 80.81 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACL-RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQ-----RSAFHQ 74
Cdd:TIGR02315 1 MLEVENLSKVyPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 75 ELLWLGHLPGIKAaLTADEN---------------LAFYHPQTRRETrWQALAAIGLGGYEDLPVEQLSAGQQRRVALAR 139
Cdd:TIGR02315 81 IGMIFQHYNLIER-LTVLENvlhgrlgykptwrslLGRFSEEDKERA-LSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1354918145 140 LWLSEASLWVLDEPLTALDAAG---VATLTRRLEAHaaRGGAVIVTTHQ 185
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTskqVMDYLKRINKE--DGITVIINLHQ 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-184 |
1.30e-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: 80.45 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFhqeLLWLGHLPGIKAALTAD----E 93
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF---LRRIGVVFGQKTQLWWDlpviD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAFYH------PQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTR 167
Cdd:cd03267 115 SFYLLAaiydlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170
....*....|....*...
gi 1354918145 168 RL-EAHAARGGAVIVTTH 184
Cdd:cd03267 195 FLkEYNRERGTTVLLTSH 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-198 |
1.48e-18 |
|
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: 79.01 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAClrdeRLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLaHQRSAFHQELLWLG 80
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV-TRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLP------GIKAALTADENLAFYHpqtrretrwqalaaiglggyedlpveQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:cd03215 79 YVPedrkreGLVLDLSVAENIALSS--------------------------LLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1354918145 155 TALDAAGVATLTRRLEAHAARGGAVI-VTTHQPLAFNVAHRTLTL 198
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLlISSELDELLGLCDRILVM 177
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-194 |
1.85e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 16 LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAF-----HQELLWLGHLPGIKAALT 90
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaelrNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVAT 164
Cdd:PRK11629 104 ALENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|.
gi 1354918145 165 LTRRL-EAHAARGGAVIVTTHQplaFNVAHR 194
Cdd:PRK11629 184 IFQLLgELNRLQGTAFLVVTHD---LQLAKR 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-194 |
2.06e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.52 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQ-----RSAF---HQE--LLwlgh 81
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtleslRRQIgvvPQDtfLF---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 lpgikaALTADENLAFYHPQTRRETRWQALAAIGL--------GGYeDLPVEQ----LSAGQQRRVALARLWLSEASLWV 149
Cdd:COG1132 427 ------SGTIRENIRYGRPDATDEEVEEAAKAAQAhefiealpDGY-DTVVGErgvnLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1354918145 150 LDEPLTALDAAGVATLTRRLEAhAARGGAVIVtthqplafnVAHR 194
Cdd:COG1132 500 LDEATSALDTETEALIQEALER-LMKGRTTIV---------IAHR 534
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-199 |
2.44e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.69 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA----HQRSafhqeL 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmHKRA-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 LWLGHLP---GIKAALTADENL------AFYHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASL 147
Cdd:COG1137 78 LGIGYLPqeaSIFRKLTVEDNIlavlelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 148 WVLDEPLTALDAAGVA---TLTRRLeahAARGGAVIVTTHqplafNVaHRTLTLT 199
Cdd:COG1137 158 ILLDEPFAGVDPIAVAdiqKIIRHL---KERGIGVLITDH-----NV-RETLGIC 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-160 |
3.00e-18 |
|
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: 81.30 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----------AHQRSA---FhQELLWLGHLpgika 87
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargiflpPHRRRIgyvF-QEARLFPHL----- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354918145 88 alTADENLAFYHPQTRRETRWQALAAI----GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:COG4148 93 --SVRGNLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-184 |
3.09e-18 |
|
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: 81.87 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAC--LRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPE---EGEVYWRGEPLAHQRSAFhqe 75
Cdd:COG1123 4 LLEVRDLSVryPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 76 llwLGHLPGIKA--------ALTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLW 141
Cdd:COG1123 81 ---RGRRIGMVFqdpmtqlnPVTVGDQIAEalenlgLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 142 LSEASLWVLDEPLTALDAAGVATLTRRL-EAHAARGGAVIVTTH 184
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLrELQRERGTTVLLITH 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-184 |
3.12e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-AHQRSAFHQ---EL 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTvrkRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 LWLGHLPGIKAALTADENLAF---YH----PQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWV 149
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYplrEHtqlpAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1354918145 150 LDEPLTALDAAGVATLTRRL-EAHAARGGAVIVTTH 184
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLIsELNSALGVTCVVVSH 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-204 |
3.54e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.78 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGL--------ARPEEGEVYWrgepLAhQRSa 71
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLF----LP-QRP- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 fhqellwlgHLPG--IKAALTadenlafyHPQTRR----ETRWQALAAIGLGGY-EDLPVEQ-----LSAGQQRRVALAR 139
Cdd:COG4178 436 ---------YLPLgtLREALL--------YPATAEafsdAELREALEAVGLGHLaERLDEEAdwdqvLSLGEQQRLAFAR 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 140 LWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAArGGAVIVTTHQPLAFNVAHRTLTLTPEPAA 204
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELP-GTTVISVGHRSTLAAFHDRVLELTGDGSW 562
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-186 |
4.50e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLahqrsAFHQELLWLGHLPGIKAALT 90
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-----QFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADEnlafyhpqtrretrwqALAAIGLGgyeDL-----PVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD------- 158
Cdd:COG2401 115 AVE----------------LLNAVGLS---DAvlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtakrv 175
|
170 180
....*....|....*....|....*...
gi 1354918145 159 AAGVATLTRRleahaaRGGAVIVTTHQP 186
Cdd:COG2401 176 ARNLQKLARR------AGITLVVATHHY 197
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-194 |
5.53e-18 |
|
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: 78.72 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRSAfhqelL 77
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklpPHERAR-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 78 WLGHLP---GIKAALTADENLafyhpQTRRETRWQALAAIGLGGYEDLPVEQ---------LSAGQQRRVALARLWLSEA 145
Cdd:TIGR03410 76 GIAYVPqgrEIFPRLTVEENL-----LTGLAALPRRSRKIPDEIYELFPVLKemlgrrggdLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1354918145 146 SLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQPLAF--NVAHR 194
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFarELADR 201
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-186 |
6.06e-18 |
|
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: 78.30 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 10 LRDERLLFRALSFR----VSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRG------EPLAHQRSAFHQELLWL 79
Cdd:cd03298 3 LDKIRFSYGEQPMHfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaaPPADRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHL-----------PGIKaaLTADEnlafyhpqtrRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLW 148
Cdd:cd03298 83 AHLtveqnvglglsPGLK--LTAED----------RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1354918145 149 VLDEPLTALDAAGVATLTRR-LEAHAARGGAVIVTTHQP 186
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLvLDLHAETKMTVLMVTHQP 189
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-186 |
6.85e-18 |
|
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: 78.47 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEE---GEVYWRGEPL-AHQ---RSAF-HQELLWLGHL 82
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRkPDQfqkCVAYvRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 pgikaalTADENLAFY--------HPQTRRETRWQ--ALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDE 152
Cdd:cd03234 97 -------TVRETLTYTailrlprkSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|....
gi 1354918145 153 PLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-194 |
6.92e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.26 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QR--SAFHQ 74
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppyQRpiNMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 75 ELLWLGHlpgikaaLTADENLAFYHPQTR------RETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLW 148
Cdd:PRK11607 99 SYALFPH-------MTVEQNIAFGLKQDKlpkaeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1354918145 149 VLDEPLTALDaagvATLTRRLEAHAA----RGGA--VIVTTHQPLAFNVAHR 194
Cdd:PRK11607 172 LLDEPMGALD----KKLRDRMQLEVVdileRVGVtcVMVTHDQEEAMTMAGR 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-185 |
7.86e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.66 E-value: 7.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLR-DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLArPEEGEVYWRGEPLAH-QRSAFHQELLWL 79
Cdd:PRK11174 350 IEAEDLEILSpDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 G---HLPgikaALTADENLAFYHPQTRRETRWQALA-----------AIGLggyeDLPV-EQ---LSAGQQRRVALARLW 141
Cdd:PRK11174 429 GqnpQLP----HGTLRDNVLLGNPDASDEQLQQALEnawvseflpllPQGL----DTPIgDQaagLSVGQAQRLALARAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 142 LSEASLWVLDEPLTALDAAGVATLTRRLEaHAARGGAVIVTTHQ 185
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALN-AASRRQTTLMVTHQ 543
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-184 |
1.02e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLaRPE---EGEVYWRGEPL--AHQR-------SAFHQEL------ 76
Cdd:PRK13549 19 KALdnvSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRdteragiAIIHQELalvkel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 -----LWLGHLPGiKAALTADENLafyhpqTRRETRWqaLAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLD 151
Cdd:PRK13549 98 svlenIFLGNEIT-PGGIMDYDAM------YLRAQKL--LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1354918145 152 EPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-184 |
1.23e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL--AHQRSAF-------HQEL--------- 76
Cdd:PRK11288 18 KALddiSFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALaagvaiiYQELhlvpemtva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 --LWLGHLPGiKAALTADENLafyhpqtRRETRWQaLAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:PRK11288 98 enLYLGQLPH-KGGIVNRRLL-------NYEAREQ-LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 155 TALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-194 |
1.35e-17 |
|
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: 77.18 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA---------- 71
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelrqkvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 -FHQELLWlghlpgikAALTADENLAFYHPQTRRETRWQA-------LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLS 143
Cdd:cd03262 81 vFQQFNLF--------PHLTVLENITLAPIKVKGMSKAEAeeralelLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 144 EASLWVLDEPLTALD---AAGVATLTRRLeahAARGGAVIVTTHQpLAF--NVAHR 194
Cdd:cd03262 153 NPKVMLFDEPTSALDpelVGEVLDVMKDL---AEEGMTMVVVTHE-MGFarEVADR 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-184 |
1.61e-17 |
|
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: 79.98 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWrGEPLAhqrsafhqellwLGH 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK------------LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAALTADENLafyhpqtrretrWQALAA----IGLGGYE-----------------DLPVEQLSAGQQRRVALARL 140
Cdd:TIGR03719 390 VDQSRDALDPNKTV------------WEEISGgldiIKLGKREipsrayvgrfnfkgsdqQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1354918145 141 WLSEASLWVLDEPLTALDaagVATLtRRLE-AHAARGGAVIVTTH 184
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLD---VETL-RALEeALLNFAGCAVVISH 498
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-195 |
1.61e-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: 77.22 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGL-----ARPEEGEVYWRGE--------PLAHQ 68
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKdiydldvdVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 69 RS---AFHQELLwlghLPGikaalTADENLAF------YHPQTRRETR-WQALAAIGLGGYED--LPVEQLSAGQQRRVA 136
Cdd:cd03260 81 RRvgmVFQKPNP----FPG-----SIYDNVAYglrlhgIKLKEELDERvEEALRKAALWDEVKdrLHALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 137 LARLWLSEASLWVLDEPLTALDAAGvatlTRRLE---AHAARGGAVIVTTHQPL-AFNVAHRT 195
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPIS----TAKIEeliAELKKEYTIVIVTHNMQqAARVADRT 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-158 |
1.40e-16 |
|
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: 76.38 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 32 LTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRS--AFHQELLWLGHLpgikaalTADENLAF-----YHP 100
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtnvpPHLRHinMVFQSYALFPHM-------TVEENVAFglkmrKVP 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1354918145 101 QTRRETR-WQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:TIGR01187 74 RAEIKPRvLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
12-184 |
1.55e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLfrALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLArPEEGEVY--------WRGEPLAHQRSAFHQELLWLghlp 83
Cdd:PRK03695 9 STRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQfagqpleaWSAAELARHRAYLSQQQTPP---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 84 gikAALTADENLAFYHPQTRRETRWQAL-----AAIGLGGYEDLPVEQLSAGQQRRVALARLWL-------SEASLWVLD 151
Cdd:PRK03695 82 ---FAMPVFQYLTLHQPDKTRTEAVASAlnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLD 158
|
170 180 190
....*....|....*....|....*....|...
gi 1354918145 152 EPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-186 |
1.62e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 26 PGEIVHLTGANGAGKTSLLRLLVGLARPE---EGEVYWRGEPLA----HQRSAF-HQELLWLGHLpgikaalTADENLAF 97
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDakemRAISAYvQQDDLFIPTL-------TVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 98 ---------YHPQTRRETRWQALAAIGLGGYEDL------PVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGV 162
Cdd:TIGR00955 123 qahlrmprrVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180
....*....|....*....|....
gi 1354918145 163 ATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQP 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-184 |
1.71e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAF---------HQellwlgHL-- 82
Cdd:COG3845 18 VVANddvSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaialgigmvHQ------HFml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 -PgikaALTADENLAFYHPQT------RRETRwQALAAI----GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLD 151
Cdd:COG3845 92 vP----NLTVAENIVLGLEPTkggrldRKAAR-ARIRELseryGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190
....*....|....*....|....*....|...
gi 1354918145 152 EPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:COG3845 167 EPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-198 |
3.85e-16 |
|
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: 74.06 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAALTA 91
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLAFYHPQTRRETRWQALAAIGLG--------GYEDLPVEQ---LSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHdfiselpeGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 161 GVATLTRRLEAHAArGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:cd03252 173 SEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVM 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-185 |
3.96e-16 |
|
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: 73.77 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA------------F-HQELLWlghlpgik 86
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkarrrigmiFqHFNLLS-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 aALTADENLAF-----YHPQTRRETR-WQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:cd03258 96 -SRTVFENVALpleiaGVPKAEIEERvLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180
....*....|....*....|....*...
gi 1354918145 161 ---GVATLTRRLeaHAARGGAVIVTTHQ 185
Cdd:cd03258 175 ttqSILALLRDI--NRELGLTIVLITHE 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-186 |
6.44e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 75.09 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQR-SAFHQELLWLGHLPGIKAAlTADENL 95
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqDEVRRRVSVCAQDAHLFDT-TVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 96 AFYHPQTRRETRWQALAAIGLGGY-EDLP----------VEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVAT 164
Cdd:TIGR02868 430 RLARPDATDEELWAALERVGLADWlRALPdgldtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
170 180
....*....|....*....|..
gi 1354918145 165 LTRRLEAhAARGGAVIVTTHQP 186
Cdd:TIGR02868 510 LLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-196 |
9.86e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.86 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYW------RGEPLAHQRS---A 71
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGlirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 FHQELLWLGHLPGIKAALTADENLAFYHPQTRRETRWQA-------LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSE 144
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEAtararelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1354918145 145 ASLWVLDEPLTALDAAGVATL--TRRLEAHAARgGAVIVTTHQPLAFNVAHRTL 196
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVlnTIRQLAQEKR-TMVIVTHEMSFARDVADRAI 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-184 |
1.30e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.23 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLA-CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGeplahqrSAFHQE-LLWL 79
Cdd:PRK13647 5 IEVEDLHfRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG-------REVNAEnEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHLPGIKA--------ALTADENLAFyHPQTRRETRWQ-------ALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSE 144
Cdd:PRK13647 78 RSKVGLVFqdpddqvfSSTVWDDVAF-GPVNMGLDKDEverrveeALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1354918145 145 ASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-184 |
1.42e-15 |
|
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: 71.19 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAAlTAD 92
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 93 ENLAfyhpqtrretrwqalaaiglggyedlpvEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTrRLEAH 172
Cdd:cd03247 93 NNLG----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFE 143
|
170
....*....|..
gi 1354918145 173 AARGGAVIVTTH 184
Cdd:cd03247 144 VLKDKTLIWITH 155
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-158 |
1.43e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QR---SAFHQELLWlGHlpgikaaLTAD 92
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaeNRhvnTVFQSYALF-PH-------MTVF 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1354918145 93 ENLAF-----YHPQTRRETR-WQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK09452 105 ENVAFglrmqKTPAAEITPRvMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-159 |
1.83e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRSAFHQEL 76
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 L--WLGHLPGIKAALtadeNLAFYHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:PRK11248 81 LlpWRNVQDNVAFGL----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
....*
gi 1354918145 155 TALDA 159
Cdd:PRK11248 157 GALDA 161
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-185 |
2.01e-15 |
|
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: 73.71 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLaRPE---EGEVYWRGEPLAHQR---------SAFHQEL----------- 76
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNirdteragiVIIHQELtlvpelsvaen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 LWLGHLPGIKAALTADENLAFYHPQTRRETRWQALAaiglggyEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEP--- 153
Cdd:TIGR02633 99 IFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADN-------VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPsss 171
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 154 LTALDAAGVATLTRRLEAHaarGGAVIVTTHQ 185
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAH---GVACVYISHK 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-184 |
2.68e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAfhqeLLWLGHLPGI----------K 86
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG----LMKLRESVGMvfqdpdnqlfS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 AALTAD-----ENLAFYHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG 161
Cdd:PRK13636 98 ASVYQDvsfgaVNLKLPEDEVRKRVD-NALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180
....*....|....*....|....
gi 1354918145 162 VATLTRRL-EAHAARGGAVIVTTH 184
Cdd:PRK13636 177 VSEIMKLLvEMQKELGLTIIIATH 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-198 |
4.13e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHqrsafhqellwL 79
Cdd:PRK13644 1 MIRLENVSySYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD-----------F 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHLPGIKAAL--------------TADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALAR 139
Cdd:PRK13644 70 SKLQGIRKLVgivfqnpetqfvgrTVEEDLAFgpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1354918145 140 LWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQPLAFNVAHRTLTL 198
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-184 |
4.79e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLwlg 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 hlpgikAALTADENLAF-----------YHPQTRRETRW---------QALAAIGLGGYEDLPVEQLSAGQQRRVALARL 140
Cdd:PRK09536 80 ------ASVPQDTSLSFefdvrqvvemgRTPHRSRFDTWtetdraaveRAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1354918145 141 WLSEASLWVLDEPLTALD---AAGVATLTRRLeahAARGGAVIVTTH 184
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDinhQVRTLELVRRL---VDDGKTAVAAIH 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-184 |
6.68e-15 |
|
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: 70.79 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQ------RS---AFHQellwLGHLPgikaALT 90
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelrRKigyVIQQ----IGLFP----HMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAF------YHPQTRRETRWQALAAIGL--GGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGV 162
Cdd:cd03295 92 VEENIALvpkllkWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180
....*....|....*....|....*
gi 1354918145 163 ATLT---RRLeaHAARGGAVIVTTH 184
Cdd:cd03295 172 DQLQeefKRL--QQELGKTIVFVTH 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-201 |
7.61e-15 |
|
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: 69.10 E-value: 7.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 9 CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVywrgeplahqrsafhqellwlgHLPgikaa 88
Cdd:cd03223 9 ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------------GMP----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 ltADENLAF-----YHPQ-TRRET---RWQalaaiglggyedlpvEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:cd03223 62 --EGEDLLFlpqrpYLPLgTLREQliyPWD---------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1354918145 160 AGVATLTRRLEAHaarGGAVIVTTHQPLAFNVAHRTLTLTPE 201
Cdd:cd03223 125 ESEDRLYQLLKEL---GITVISVGHRPSLWKFHDRVLDLDGE 163
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-196 |
8.56e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.06 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH---------QRSAF---HQELLWLGHLpgika 87
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalaqlRREHFgfiFQRYHLLSHL----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 alTADENL---AFYH--PQTRRETRWQAL-AAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG 161
Cdd:PRK10535 102 --TAAQNVevpAVYAglERKQRLLRAQELlQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1354918145 162 VATLTRRLEAHAARGGAVIVTTHQPLAFNVAHRTL 196
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-159 |
9.19e-15 |
|
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: 70.19 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-AHQRSAFHQELLWLGHLPGIKAAL 89
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TADeNLAFYHPQTRRETRWQALAAIGLGGY-EDLPVE----------QLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:cd03248 104 LQD-NIAYGLQSCSFECVKEAAQKAHAHSFiSELASGydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
.
gi 1354918145 159 A 159
Cdd:cd03248 183 A 183
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-184 |
1.41e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.04 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH---QRSAFHQELL 77
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 78 WLGHL--PGIKA----ALTADENLAFYHPQTRRETRW--QALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWV 149
Cdd:PRK11231 82 PQHHLtpEGITVrelvAYGRSPWLSLWGRLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1354918145 150 LDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-194 |
1.45e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 69.64 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNL-------ACLRDerllfraLSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFH 73
Cdd:COG1126 1 MIEIENLhksfgdlEVLKG-------ISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 ---QEL--------LWlGHLpgikaalTADENLAfYHP-----QTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRR 134
Cdd:COG1126 74 klrRKVgmvfqqfnLF-PHL-------TVLENVT-LAPikvkkMSKAEAEERAmelLERVGLADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 135 VALAR---------LwlseaslwvLDEPLTALD---AAGVATLTRRLeahAARGGAVIVTTHQ-PLAFNVAHR 194
Cdd:COG1126 145 VAIARalamepkvmL---------FDEPTSALDpelVGEVLDVMRDL---AKEGMTMVVVTHEmGFAREVADR 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-181 |
1.76e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAClrdeRLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQ--RSAFHQEllw 78
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRspRDAIRAG--- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 79 LGHLP------GIKAALTADEN--LAFYHPQTR-------RETRwQALAAIG-LG---GYEDLPVEQLSAGQQRRVALAR 139
Cdd:COG1129 329 IAYVPedrkgeGLVLDLSIRENitLASLDRLSRgglldrrRERA-LAEEYIKrLRiktPSPEQPVGNLSGGNQQKVVLAK 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1354918145 140 lWL-SEASLWVLDEPlTaldaAGV---A-----TLTRRLeahAARGGAVIV 181
Cdd:COG1129 408 -WLaTDPKVLILDEP-T----RGIdvgAkaeiyRLIREL---AAEGKAVIV 449
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-184 |
1.96e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.12 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFrvSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEV---------YWRGEP-LAHQRSAFHQELLWLGHlpgIKAAL 89
Cdd:TIGR03719 26 LSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEArpqpgikvgYLPQEPqLDPTKTVRENVEEGVAE---IKDAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TA-DE-NLAFYHP----------QTRRETRWQALAAIGLGGY------------EDLPVEQLSAGQQRRVALARLWLSEA 145
Cdd:TIGR03719 101 DRfNEiSAKYAEPdadfdklaaeQAELQEIIDAADAWDLDSQleiamdalrcppWDADVTKLSGGERRRVALCRLLLSKP 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1354918145 146 SLWVLDEPLTALDAAGVATLTRRLEAHAargGAVIVTTH 184
Cdd:TIGR03719 181 DMLLLDEPTNHLDAESVAWLERHLQEYP---GTVVAVTH 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-184 |
2.23e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWrGEPLAhqrsafhqellwLGH 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK------------LAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAALTADENLafyhpqtrretrWQALAA----IGLGGYE-----------------DLPVEQLSAGQQRRVALARL 140
Cdd:PRK11819 392 VDQSRDALDPNKTV------------WEEISGgldiIKVGNREipsrayvgrfnfkggdqQKKVGVLSGGERNRLHLAKT 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1354918145 141 WLSEASLWVLDEPLTALDaagVATLtRRLE-AHAARGGAVIVTTH 184
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD---VETL-RALEeALLEFPGCAVVISH 500
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-167 |
2.34e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRS---AFHQE---LLWLGHLPGIK 86
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdtrLMFQDarlLPWKKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 AALTADenlafYHPQTRretrwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAagvatLT 166
Cdd:PRK11247 104 LGLKGQ-----WRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-----LT 168
|
.
gi 1354918145 167 R 167
Cdd:PRK11247 169 R 169
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-184 |
2.78e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 68.90 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLfRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGE------PLAHQRSAFHQE 75
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlpPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 76 LLWLGHLpgikaalTADENLAF-----YHPQTRRETRWQALAA-IGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWV 149
Cdd:cd03299 80 YALFPHM-------TVYKNIAYglkkrKVDKKEIERKVLEIAEmLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1354918145 150 LDEPLTALDAAGVATLTRRL-EAHAARGGAVIVTTH 184
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELkKIRKEFGVTVLHVTH 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-160 |
3.45e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QR--SAFHQELLWLGHLpgikaalTADEN 94
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtppsRRpvSMLFQENNLFSHL-------TVAQN 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 95 LAF-YHPQTR-----RETRWQALAAIGLGGY-EDLPvEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:PRK10771 92 IGLgLNPGLKlnaaqREKLHAIARQMGIEDLlARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-184 |
4.48e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.56 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH----QRSAFHQE--LLWLGHLPGIKAALTA 91
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDiqMVFQDSISAVNPRKTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLA--FYH----PQTRRETRWQA-LAAIGL--GGYEDLPvEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGV 162
Cdd:PRK10419 109 REIIRepLRHllslDKAERLARASEmLRAVDLddSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180
....*....|....*....|...
gi 1354918145 163 ATLTRRLEAHAARGG-AVIVTTH 184
Cdd:PRK10419 188 AGVIRLLKKLQQQFGtACLFITH 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-199 |
5.13e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 14 RLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA------------FHQELLWLGH 81
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflrrqigmiFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 -------LPGIKAALTADEnlafyhpqTRRETRwQALAAIG-LGGYEDLPVeQLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:PRK10908 95 tvydnvaIPLIIAGASGDD--------IRRRVS-AALDKVGlLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1354918145 154 LTALDAAGVATLTRRLEAHAARGGAVIVTTHQ-PLAFNVAHRTLTLT 199
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDiGLISRRSYRMLTLS 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-158 |
5.52e-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: 68.02 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEP-----LAHQRSAFH---QElLWLghLPGikaal 89
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisRKSLRSMIGvvlQD-TFL--FSG----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TADENLAFYHPQTRRETRWQALAAIGL--------GGYEDLPVEQ---LSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:cd03254 92 TIMENIRLGRPNATDEEVIEAAKEAGAhdfimklpNGYDTVLGENggnLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-161 |
1.16e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYwrgeplahqrsafHQELLWLGHLPgikAALTAD 92
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------RNGKLRIGYVP---QKLYLD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 93 ENLAF-------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG 161
Cdd:PRK09544 80 TTLPLtvnrflrLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-185 |
1.22e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRS---------------------- 70
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlrllrtrltm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 71 AFHQELLWlGHLPGIKAALTADENLAFYHPQTRRETRWQALAAIGLGGYE--DLPVEqLSAGQQRRVALARLWLSEASLW 148
Cdd:PRK10619 97 VFQHFNLW-SHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqgKYPVH-LSGGQQQRVSIARALAMEPEVL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 149 VLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQ 185
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-184 |
1.26e-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: 68.89 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 24 VSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAALTADENLAFY----- 98
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYarlrg 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 99 --HPQTRRETRWqALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARG 176
Cdd:TIGR01257 2042 vpAEEIEKVANW-SIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG 2120
|
....*...
gi 1354918145 177 GAVIVTTH 184
Cdd:TIGR01257 2121 RAVVLTSH 2128
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-196 |
1.46e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.04 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRG----EPLAHQRS------ 70
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKVDERLirqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 71 -AFHQELLWlghlpgikAALTADENLAFYHPQTRRETRWQA-------LAAIGLGGYEDLPVEQLSAGQQRRVALARLWL 142
Cdd:PRK09493 81 mVFQQFYLF--------PHLTALENVMFGPLRVRGASKEEAekqarelLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 143 SEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQ-PLAFNVAHRTL 196
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEiGFAEKVASRLI 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-185 |
2.12e-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: 65.95 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 16 LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGeplahqRSAFHQELLWLghLPGikaalTADENL 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIAYVSQEPWI--QNG-----TIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 96 AFYHPqtRRETR-WQALAAIGLggYEDLPV----------EQ---LSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG 161
Cdd:cd03250 87 LFGKP--FDEERyEKVIKACAL--EPDLEIlpdgdlteigEKginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180
....*....|....*....|....*
gi 1354918145 162 VATLTRR-LEAHAARGGAVIVTTHQ 185
Cdd:cd03250 163 GRHIFENcILGLLLNNKTRILVTHQ 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-184 |
2.23e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFrvSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEvywrgeplahqrsAFHQELLWLGHLP---------------- 83
Cdd:PRK11819 28 LSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------------ARPAPGIKVGYLPqepqldpektvrenve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 84 ----GIKAALTA-DE-NLAFYHP----------QTRRETR------W-------QALAAIGLGGyEDLPVEQLSAGQQRR 134
Cdd:PRK11819 93 egvaEVKAALDRfNEiYAAYAEPdadfdalaaeQGELQEIidaadaWdldsqleIAMDALRCPP-WDAKVTKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1354918145 135 VALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAargGAVIVTTH 184
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP---GTVVAVTH 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-185 |
2.31e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.83 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAF-HQELLWLGHLPGIKAAl 89
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlHRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TADENLAFYHPQTRREtrwQALAAIGLGGYEDLPVE--------------QLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:TIGR00958 570 SVRENIAYGLTDTPDE---EIMAAAKAANAHDFIMEfpngydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 156 ALDAAGVATLTrrlEAHAARGGAVIVTTHQ 185
Cdd:TIGR00958 647 ALDAECEQLLQ---ESRSRASRTVLLIAHR 673
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-194 |
2.75e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-----QRSAF-HQELLWLGHLpgikaalTADE 93
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhardRKVGFvFQHYALFRHM-------TVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAF---YHPQTRRETRW-------QALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVA 163
Cdd:PRK10851 94 NIAFgltVLPRRERPNAAaikakvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190
....*....|....*....|....*....|...
gi 1354918145 164 TLTRRL-EAHAA-RGGAVIVTTHQPLAFNVAHR 194
Cdd:PRK10851 174 ELRRWLrQLHEElKFTSVFVTHDQEEAMEVADR 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-200 |
3.43e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLR------DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFH 73
Cdd:PRK10247 1 MQENSPLLQLQnvgylaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 QELLWLGHLPgikaALTAD---ENLAFyhP-QTRRETRWQALAAIGLGGYE------DLPVEQLSAGQQRRVALARLWLS 143
Cdd:PRK10247 81 QQVSYCAQTP----TLFGDtvyDNLIF--PwQIRNQQPDPAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 144 EASLWVLDEPLTALDAAG---VATLTRRLEAHaaRGGAVIVTTHQPLAFNVAHRTLTLTP 200
Cdd:PRK10247 155 MPKVLLLDEITSALDESNkhnVNEIIHRYVRE--QNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-194 |
4.59e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 7 LACLRDERLLF------RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAF-HQELLWL 79
Cdd:PRK15439 11 LLCARSISKQYsgvevlKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKaHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 -GHLPGIKAALTADENLAFYHPQTRRETR--WQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTA 156
Cdd:PRK15439 91 vPQEPLLFPNLSVKENILFGLPKRQASMQkmKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1354918145 157 LDAAGVATLTRRLEAHAARGGAVIVTTHQ-PLAFNVAHR 194
Cdd:PRK15439 171 LTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADR 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-181 |
1.05e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLaCLRDER--LLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQElLWL 79
Cdd:COG3845 258 LEVENL-SVRDDRgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR-LGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHLP------GIKAALTADENLAFYHPQTRRETRW--------QALAA-------IGLGGyEDLPVEQLSAGQQRRVALA 138
Cdd:COG3845 336 AYIPedrlgrGLVPDMSVAENLILGRYRRPPFSRGgfldrkaiRAFAEelieefdVRTPG-PDTPARSLSGGNQQKVILA 414
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1354918145 139 RLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIV 181
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-184 |
1.07e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLahqRSAFHQELL----------W-- 78
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVayvpqseevdWsf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 79 ------------LGHLPGIKAALTADenlafyhpqtrRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEAS 146
Cdd:PRK15056 94 pvlvedvvmmgrYGHMGWLRRAKKRD-----------RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 147 LWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-185 |
1.08e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqRSAFHQELLWL 79
Cdd:PRK13652 3 LIETRDLCySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 GHL---PGIKA-ALTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWV 149
Cdd:PRK13652 81 GLVfqnPDDQIfSPTVEQDIAFgpinlgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 150 LDEPLTALDAAGVATLTRRLEAHAAR-GGAVIVTTHQ 185
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-184 |
1.25e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVY------WRGEP-LAH-------QRSafhqELLWlgHLPGI 85
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpFKRRKeFARrigvvfgQRS----QLWW--DLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 86 kaaltadENLAFYH-----PQTRRETRWQALAAI-GLGGYEDLPVEQLSAGQQRRVALArlwlseASLW------VLDEP 153
Cdd:COG4586 115 -------DSFRLLKaiyriPDAEYKKRLDELVELlDLGELLDTPVRQLSLGQRMRCELA------AALLhrpkilFLDEP 181
|
170 180 190
....*....|....*....|....*....|....
gi 1354918145 154 LTALDAagVATLTRR---LEAHAARGGAVIVTTH 184
Cdd:COG4586 182 TIGLDV--VSKEAIReflKEYNRERGTTILLTSH 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-161 |
1.54e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLaCLRDERLL-FRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqrsafhqellwl 79
Cdd:PRK11300 5 LLSVSGL-MMRFGGLLaVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 80 gHLPGIKAA----------------LTADENLA---------------FYHPQTRRETR--------WqaLAAIGLGGYE 120
Cdd:PRK11300 71 -GLPGHQIArmgvvrtfqhvrlfreMTVIENLLvaqhqqlktglfsglLKTPAFRRAESealdraatW--LERVGLLEHA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1354918145 121 DLPVEQLSAGQQRRVALARLWLSEASLWVLDEPltaldAAG 161
Cdd:PRK11300 148 NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP-----AAG 183
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-184 |
1.78e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA----HQRSafhqeLL 77
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARA-----RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 78 WLGHLP-------------GIKAALTADENLAFYHPQTRREtrwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSE 144
Cdd:PRK10895 79 GIGYLPqeasifrrlsvydNLMAVLQIRDDLSAEQREDRAN---ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1354918145 145 ASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-160 |
1.80e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVG----LARPE----EGEVYWRGEPLAH---QR 69
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAidaPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 70 SAFHQELLWLGHLPGIkaALTADENLAF-YHPQTRR---------ETRWQALAAIGLGGYEDLPVEQLSAGQQRRV---- 135
Cdd:PRK13547 81 LARLRAVLPQAAQPAF--AFSAREIVLLgRYPHARRagalthrdgEIAWQALALAGATALVGRDVTTLSGGELARVqfar 158
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 136 ALARLWLSEASL-----WVLDEPLTALDAA 160
Cdd:PRK13547 159 VLAQLWPPHDAAqppryLLLDEPTAALDLA 188
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-160 |
2.81e-12 |
|
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: 63.72 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 16 LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGeplahqRSAFHQELLWLghLPGikaalTADENL 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------RISFSSQFSWI--MPG-----TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 96 AF--YHPQTRRETRWQAL--------------AAIGLGGYedlpveQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:cd03291 119 IFgvSYDEYRYKSVVKACqleeditkfpekdnTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
.
gi 1354918145 160 A 160
Cdd:cd03291 193 F 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-194 |
4.64e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 14 RLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRS-AFHQELLWL-GHLPGIKaALTA 91
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkAFARKVAYLpQQLPAAE-GMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLAF----YH------PQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA- 160
Cdd:PRK10575 103 RELVAIgrypWHgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAh 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1354918145 161 --GVATLTRRLEAHaaRGGAVIVTTHQplaFNVAHR 194
Cdd:PRK10575 183 qvDVLALVHRLSQE--RGLTVIAVLHD---INMAAR 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-198 |
5.26e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 62.72 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA---------------FHQELLWlGHLpg 84
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPsekairllrqkvgmvFQQYNLW-PHL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 85 ikaalTADENLaFYHP-----QTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTA 156
Cdd:COG4161 98 -----TVMENL-IEAPckvlgLSKEQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1354918145 157 LD---AAGVATLTRRLeahAARGGAVIVTTHQ-PLAFNVAHRTLTL 198
Cdd:COG4161 172 LDpeiTAQVVEIIREL---SQTGITQVIVTHEvEFARKVASQVVYM 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-185 |
6.72e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.72 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 19 ALSFRVSPGEIVHLTGANGAGKTSLLRLLVGL----ARPEE-----GEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAAL 89
Cdd:PRK09984 22 AVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGShiellGRTVQREGRLARDIRKSRANTGYIFQQFNLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TADEN---------------LAFYHPQTRRETrWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:PRK09984 102 SVLENvligalgstpfwrtcFSWFTREQKQRA-LQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 155 TALDAAGVATLTRRL-EAHAARGGAVIVTTHQ 185
Cdd:PRK09984 181 ASLDPESARIVMDTLrDINQNDGITVVVTLHQ 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-186 |
7.33e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.51 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPE---EGEVYWRGEPLAHQRSAFHQELLWLG----HLP 83
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSeedvHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 84 gikaALTADENLAFyhpqtrretrwqalaAIGLGGYEDlpVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVA 163
Cdd:cd03233 97 ----TLTVRETLDF---------------ALRCKGNEF--VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180
....*....|....*....|....*
gi 1354918145 164 TLTRRLE--AHAArGGAVIVTTHQP 186
Cdd:cd03233 156 EILKCIRtmADVL-KTTTFVSLYQA 179
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-184 |
1.06e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWrgeplahqrsafhQELLWLGH 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-------------SENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAA-LTADENLAFYHPQTRRETR-WQALAAIgLG----GYEDL--PVEQLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:PRK15064 387 YAQDHAYdFENDLTLFDWMSQWRQEGDdEQAVRGT-LGrllfSQDDIkkSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190
....*....|....*....|....*....|.
gi 1354918145 154 LTALDAAGVATLTRRLEAHAargGAVIVTTH 184
Cdd:PRK15064 466 TNHMDMESIESLNMALEKYE---GTLIFVSH 493
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-186 |
1.15e-11 |
|
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: 61.11 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGlaRPE----EGEVYWRGEPL--AHQRSAFHQELLWLgHLPG 84
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTagviTGEILINGRPLdkNFQRSTGYVEQQDV-HSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 85 ikaaltadenlafyhpQTRRET-RWQALaaigLGGyedlpveqLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVA 163
Cdd:cd03232 94 ----------------LTVREAlRFSAL----LRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|...
gi 1354918145 164 TLTRRLEAHAARGGAVIVTTHQP 186
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIHQP 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-184 |
1.78e-11 |
|
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: 60.62 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPE--EGEVYWRGEPLA----HQRSafhqe 75
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITdlppEERA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 76 llwlghlpgiKAALTadenLAFYHPqtrretrwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:cd03217 76 ----------RLGIF----LAFQYP--------PEIPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180
....*....|....*....|....*....
gi 1354918145 156 ALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-180 |
1.94e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 24 VSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRsafhQELlwLGHLPGIKAALTADENLAFY-HPQT 102
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP----QYI--KADYEGTVRDLLSSITKDFYtHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 103 RRETrwqaLAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG---VATLTRRLEAHAARGGAV 179
Cdd:cd03237 96 KTEI----AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIRRFAENNEKTAFV 171
|
.
gi 1354918145 180 I 180
Cdd:cd03237 172 V 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-180 |
2.35e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHqRSAFHQELLWLGHLP------GI----- 85
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA-LSTAQRLARGLVYLPedrqssGLyldap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 86 ----KAALTADENLAFYHPQTRRETRWQALAAIGLG-GYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:PRK15439 358 lawnVCALTHNRRGFWIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180
....*....|....*....|
gi 1354918145 161 GVATLTRRLEAHAARGGAVI 180
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVL 457
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-158 |
2.99e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 24 VSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA----HQRSAFH-QELLWLGHLPGIKAALTADENL--- 95
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeEARAKLRaKHVGFVFQSFMLIPTLNALENVelp 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 96 AFYHPQTRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK10584 113 ALLRGESSRQSRNGAkalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-167 |
4.64e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-AHQRSAFHQ---------ELLWLGH 81
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItDDNFEKLRKhigivfqnpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPGIKAALTAdENLAFYHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAG 161
Cdd:PRK13648 100 IVKYDVAFGL-ENHAVPYDEMHRRVS-EALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
....*.
gi 1354918145 162 VATLTR 167
Cdd:PRK13648 178 RQNLLD 183
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-74 |
4.73e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.97 E-value: 4.73e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-AHQRSAFHQ 74
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRQ 406
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-184 |
5.03e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.99 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQR-SAFHQELLWLGHLPGIKAAlTADENL 95
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeAALRQAISVVSQRVHLFSA-TLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 96 AFYHPQTRRETRWQALAAIGLGGY--EDLPVE--------QLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATL 165
Cdd:PRK11160 435 LLAAPNASDEALIEVLQQVGLEKLleDDKGLNawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQI 514
|
170
....*....|....*....
gi 1354918145 166 TRRLEAHaARGGAVIVTTH 184
Cdd:PRK11160 515 LELLAEH-AQNKTVLMITH 532
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-159 |
5.75e-11 |
|
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: 61.11 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEplahqrSAFHQELLWLGHLpgikaalT 90
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS------VAYVPQQAWIQND-------S 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAFYHPQtrRETRWQAL--AAIGLGGYEDLPVE----------QLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:TIGR00957 715 LRENILFGKAL--NEKYYQQVleACALLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
.
gi 1354918145 159 A 159
Cdd:TIGR00957 793 A 793
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-158 |
6.00e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA-FHQELLWLGHLPGIKAALTADENLA 96
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1354918145 97 F-YHPQTRRETRWQ---------ALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK10253 104 RgRYPHQPLFTRWRkedeeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-158 |
8.27e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 16 LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGeplahqRSAFHQELLWLghLPGikaalTADENL 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------RISFSPQTSWI--MPG-----TIKDNI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354918145 96 AFyhPQTRRETRWQA-LAAIGLggYEDLPV-------------EQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:TIGR01271 508 IF--GLSYDEYRYTSvIKACQL--EEDIALfpekdktvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-157 |
9.33e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALS---FRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGE------PLAHQR---SAFHQELLWLGHlpgi 85
Cdd:PRK10762 18 KALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngPKSSQEagiGIIHQELNLIPQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 86 kaaLTADENLAFYHPQTRRETR--WQA--------LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:PRK10762 94 ---LTIAENIFLGREFVNRFGRidWKKmyaeadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
..
gi 1354918145 156 AL 157
Cdd:PRK10762 171 AL 172
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-184 |
9.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.36 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqrsafhQELLW-LGHLPG----------IKAA 88
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT-------EENVWdIRHKIGmvfqnpdnqfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTAD-----ENLAFYHpQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVA 163
Cdd:PRK13650 99 VEDDvafglENKGIPH-EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180
....*....|....*....|..
gi 1354918145 164 TLTRRLEAHAARGG-AVIVTTH 184
Cdd:PRK13650 178 ELIKTIKGIRDDYQmTVISITH 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-185 |
1.00e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.71 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA------------F-HQELLWlg 80
Cdd:COG1135 18 VTALddvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraarrkigmiFqHFNLLS-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 hlpgikaALTADENLAF-----YHPQTRRETRWQALAA-IGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:COG1135 96 -------SRTVAENVALpleiaGVPKAEIRKRVAELLElVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190
....*....|....*....|....*....|....
gi 1354918145 155 TALD---AAGVATLTRRLeaHAARGGAVIVTTHQ 185
Cdd:COG1135 169 SALDpetTRSILDLLKDI--NRELGLTIVLITHE 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-186 |
1.13e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPE--EGEVYWRGEPLAHQ---RSAF-HQELLWLGHLpgik 86
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQilkRTGFvTQDDILYPHL---- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 aalTADENLAFYH----PQ--TRRETRWQA---LAAIGLGGYEDLPV-----EQLSAGQQRRVALARLWLSEASLWVLDE 152
Cdd:PLN03211 156 ---TVRETLVFCSllrlPKslTKQEKILVAesvISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|....
gi 1354918145 153 PLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP 266
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-158 |
1.20e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRA---LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWR-GE---------PLAHQRSA-----FHQ 74
Cdd:TIGR03269 293 DRGVVKAvdnVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvdmtkpgPDGRGRAKryigiLHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 75 ELLWLGHlPGIKAALTADENLAFYHPQTRRetrwQALAAIGLGGYEDLPVE--------QLSAGQQRRVALARLWLSEAS 146
Cdd:TIGR03269 373 EYDLYPH-RTVLDNLTEAIGLELPDELARM----KAVITLKMVGFDEEKAEeildkypdELSEGERHRVALAQVLIKEPR 447
|
170
....*....|..
gi 1354918145 147 LWVLDEPLTALD 158
Cdd:TIGR03269 448 IVILDEPTGTMD 459
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-184 |
1.45e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.87 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqrsafhQELLWlghlpGIKA---- 87
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS-------EETVW-----DVRRqvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 -----------ALTAD------ENLAFYHPQTRRETRWqALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVL 150
Cdd:PRK13635 86 vfqnpdnqfvgATVQDdvafglENIGVPREEMVERVDQ-ALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 151 DEPLTALDAAG---VATLTRRLEAHaaRGGAVIVTTH 184
Cdd:PRK13635 165 DEATSMLDPRGrreVLETVRQLKEQ--KGITVLSITH 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-153 |
1.78e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA--FHQELLWLGHLPGIKAALTADENLAF 97
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEENLAM 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 98 YHPQTRRETRWQALAAIglggYEDLPVEQ---------LSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:PRK11614 104 GGFFAERDQFQERIKWV----YELFPRLHerriqragtMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-185 |
1.91e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 23 RVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEP---------LAHQRSAFHQEL-----------LWLGHL 82
Cdd:PRK10982 20 KVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksskeaLENGISMVHQELnlvlqrsvmdnMWLGRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 PgiKAALTADenlafyHPQTRRETRwqalaAIglggYEDL--------PVEQLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:PRK10982 100 P--TKGMFVD------QDKMYRDTK-----AI----FDELdididpraKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190
....*....|....*....|....*....|.
gi 1354918145 155 TALDAAGVATLTRRLEAHAARGGAVIVTTHQ 185
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHK 193
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-184 |
2.08e-10 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 58.91 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNL-ACLRDERLLFRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARP---EEGEVYWRGEPLAH----QR 69
Cdd:COG0444 1 LLEVRNLkVYFPTRRGVVKAVdgvSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 70 SAF--------HQEllwlghlpgikaALTA-----------DENLAFYHPQTRRETRWQA---LAAIGLggyeDLPVE-- 125
Cdd:COG0444 81 RKIrgreiqmiFQD------------PMTSlnpvmtvgdqiAEPLRIHGGLSKAEARERAielLERVGL----PDPERrl 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354918145 126 -----QLSAGQQRRVALARLWLSEASLWVLDEPLTALDA---AGVATLTRRLeaHAARGGAVIVTTH 184
Cdd:COG0444 145 dryphELSGGMRQRVMIARALALEPKLLIADEPTTALDVtiqAQILNLLKDL--QRELGLAILFITH 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-197 |
2.37e-10 |
|
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: 57.93 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLahqRSafhQELLWLGHLPGI---KA 87
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RD---LNLRWLRSQIGLvsqEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 AL---TADENLAFYHPQTRRETRWQA--LAAI-----GL-GGYEDLPVE---QLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:cd03249 87 VLfdgTIAENIRYGKPDATDEEVEEAakKANIhdfimSLpDGYDTLVGErgsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 154 LTALDAAGVATLTRRLEAhAARGGAVIVtthqplafnVAHRTLT 197
Cdd:cd03249 167 TSALDAESEKLVQEALDR-AMKGRTTIV---------IAHRLST 200
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-184 |
5.90e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 14 RLLFRaLSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVywRGEPLAHQRSAFHQELLWLGHLPGIKAAL---- 89
Cdd:PRK13643 20 RALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSKQKEIKPVRKKVGVVFQFpesq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 ----TADENLAFyHPQTRRETRWQA-------LAAIGLGG--YEDLPVEqLSAGQQRRVALARLWLSEASLWVLDEPLTA 156
Cdd:PRK13643 97 lfeeTVLKDVAF-GPQNFGIPKEKAekiaaekLEMVGLADefWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180
....*....|....*....|....*...
gi 1354918145 157 LDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-197 |
6.53e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVY-------WRGEPLAHQRSA--------FHQELLWlGHLpg 84
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIRElrrnvgmvFQQYNLW-PHL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 85 ikaalTADENLaFYHPQ-----TRRETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTA 156
Cdd:PRK11124 98 -----TVQQNL-IEAPCrvlglSKDQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 157 LD---AAGVATLTRRLeahAARGGAVIVTTHQplaFNVAHRTLT 197
Cdd:PRK11124 172 LDpeiTAQIVSIIREL---AETGITQVIVTHE---VEVARKTAS 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-185 |
7.30e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARpEEGE-----VYWRGEPLAHQRSAFhqellwlGHLPGIK 86
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEiqidgVSWNSVTLQTWRKAF-------GVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 AALTAD--ENLAFYHpQTRRETRWQALAAIGL-----------------GGYedlpveQLSAGQQRRVALARLWLSEASL 147
Cdd:TIGR01271 1302 FIFSGTfrKNLDPYE-QWSDEEIWKVAEEVGLksvieqfpdkldfvlvdGGY------VLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 148 WVLDEPLTALDAAGVATLTRRLEaHAARGGAVIVTTHQ 185
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLK-QSFSNCTVILSEHR 1411
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-196 |
7.95e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.86 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEplahqrsafHQELLWLG 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR---------DGQLRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLP---------------------GIKAALTADEN-------LAFYHPQTRRET--RWQALAAIGLGGYEDLPvEQLSAG 130
Cdd:PRK11701 77 ALSeaerrrllrtewgfvhqhprdGLRMQVSAGGNigerlmaVGARHYGDIRATagDWLERVEIDAARIDDLP-TTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 131 QQRRVALARLWLSEASLWVLDEPLTALDA---AGVATLTRRLEAHAarGGAVIVTTHQ-PLAFNVAHRTL 196
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVsvqARLLDLLRGLVREL--GLAVVIVTHDlAVARLLAHRLL 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-158 |
1.26e-09 |
|
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: 55.58 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA----HQ-RSAFH---QE-LLWLGhlpgikaalT 90
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiglHDlRSRISiipQDpVLFSG---------T 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1354918145 91 ADENLAFYHPQTRrETRWQALAAIGL-------GGYEDLPVE----QLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:cd03244 94 IRSNLDPFGEYSD-EELWQALERVGLkefveslPGGLDTVVEeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-184 |
1.39e-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: 55.70 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEP-----LAHQRSAfhqellwLGHLPGiK 86
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtLDSLRRA-------IGVVPQ-D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 AAL---TADENLAFYHPQ-TRRETRWQALAA------IGL-GGYEDLPVEQ---LSAGQQRRVALARLWLSEASLWVLDE 152
Cdd:cd03253 84 TVLfndTIGYNIRYGRPDaTDEEVIEAAKAAqihdkiMRFpDGYDTIVGERglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 153 PLTALDAAGVATLTRRLEAhAARGGAVIVTTH 184
Cdd:cd03253 164 ATSALDTHTEREIQAALRD-VSKGRTTIVIAH 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-184 |
1.42e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.38 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAfhqellwlghlPGIKAaLTADENLAFYH 99
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN-----------KNLKK-LRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 100 PQTR---------------------RETRWQALAAIG-LGGYEDL----PVEqLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:PRK13641 94 PEAQlfentvlkdvefgpknfgfseDEAKEKALKWLKkVGLSEDLisksPFE-LSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190
....*....|....*....|....*....|.
gi 1354918145 154 LTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-198 |
1.52e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAC---LRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGlARP--EEGEVYWRGEPLAhQRSAFHQE 75
Cdd:TIGR02633 257 ILEARNLTCwdvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPgkFEGNVFINGKPVD-IRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 76 LLWLGHLP------GIKAALTADEN--LAFYHPQTRReTRWQALAAIGLGGYE-----------DLPVEQLSAGQQRRVA 136
Cdd:TIGR02633 335 RAGIAMVPedrkrhGIVPILGVGKNitLSVLKSFCFK-MRIDAAAELQIIGSAiqrlkvktaspFLPIGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1354918145 137 LARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQ-PLAFNVAHRTLTL 198
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVI 476
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-170 |
1.53e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----AHQRSAFHQELLW-----LGHL-PGIKAALT 90
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMifqdpLASLnPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 91 ADENLAFYHPQTRRE---TRWQA-LAAIGLggyedLP------VEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA- 159
Cdd:PRK15079 121 IAEPLRTYHPKLSRQevkDRVKAmMLKVGL-----LPnlinryPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVs 195
|
170
....*....|...
gi 1354918145 160 --AGVATLTRRLE 170
Cdd:PRK15079 196 iqAQVVNLLQQLQ 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-185 |
1.56e-09 |
|
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: 56.95 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 28 EIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQEllwLGHLPG---IKAALTADENLAFYhPQTRR 104
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS---LGMCPQhniLFHHLTVAEHILFY-AQLKG 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 105 ETRWQA-------LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAArGG 177
Cdd:TIGR01257 1033 RSWEEAqlemeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GR 1111
|
....*...
gi 1354918145 178 AVIVTTHQ 185
Cdd:TIGR01257 1112 TIIMSTHH 1119
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-198 |
1.67e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 27 GEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYW------------RGEPLAHQRSAFHQellwlgHLpgikaalTADEN 94
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrmndvppaeRGVGMVFQSYALYP------HL-------SVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 95 LAF-----YHPQTRRETRWQALAAI-GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA-------G 161
Cdd:PRK11000 96 MSFglklaGAKKEEINQRVNQVAEVlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriE 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 162 VATLTRRLeahaarGGAVIVTTH-QPLAFNVAHRTLTL 198
Cdd:PRK11000 176 ISRLHKRL------GRTMIYVTHdQVEAMTLADKIVVL 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-181 |
1.87e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQ--RSAFHQELLWlghLP------GIKAALTAD 92
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRspRDAIRAGIML---CPedrkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 93 ENLA------------FYHPQTRRET---RWQALAAIGLGGyeDLPVEQLSAGQQRRVALARlWLSEA-SLWVLDEPLTA 156
Cdd:PRK11288 350 DNINisarrhhlragcLINNRWEAENadrFIRSLNIKTPSR--EQLIMNLSGGNQQKAILGR-WLSEDmKVILLDEPTRG 426
|
170 180
....*....|....*....|....*
gi 1354918145 157 LDAAGVATLTRRLEAHAARGGAVIV 181
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-184 |
2.62e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 15 LLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYwrgeplahqRSA------FHQEllwlgHLPGIKAA 88
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---------RSAkvrmavFSQH-----HVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTADENLAFYHPQTRRETRWQALAAIGLGGYEDL-PVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTR 167
Cdd:PLN03073 589 SNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALqPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ 668
|
170
....*....|....*..
gi 1354918145 168 RLeahAARGGAVIVTTH 184
Cdd:PLN03073 669 GL---VLFQGGVLMVSH 682
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-185 |
3.22e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRG---EPLAHQRSA------FHQELlwlghlpGIKAA 88
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAAqlgigiIYQEL-------SVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTADENLAFYHPQTR----------RETRWQA---LAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:PRK09700 95 LTVLENLYIGRHLTKkvcgvniidwREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 156 ALDAAGVATLTRRLEAHAARGGAVIVTTHQ 185
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-158 |
4.18e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA-----HQRSAFHQELLWLGHLPGIKAALTADENL 95
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1354918145 96 AF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK10070 128 AFgmelagINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-188 |
4.97e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLL-----RLLVGLArpEEGEVYWRGEPL--AHQRSAFH---QELlwlgH 81
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGRPLdsSFQRSIGYvqqQDL----H 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 82 LPgikaALTADENLAFY----HPQ--TRRETRWQALAAIGLGGYED-------LPVEQLSAGQQRRVALA-RLWLSEASL 147
Cdd:TIGR00956 848 LP----TSTVRESLRFSaylrQPKsvSKSEKMEYVEEVIKLLEMESyadavvgVPGEGLNVEQRKRLTIGvELVAKPKLL 923
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1354918145 148 WVLDEPLTALD---AAGVATLTRRLEAHaarGGAVIVTTHQPLA 188
Cdd:TIGR00956 924 LFLDEPTSGLDsqtAWSICKLMRKLADH---GQAILCTIHQPSA 964
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-200 |
5.36e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 53.98 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-----CLRDERLL--FRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWR--GEP--LAhqr 69
Cdd:COG4778 4 LLEVENLSktftlHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWvdLA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 70 SAFHQELLWL-----GH-------LPGIKA---------ALTADENLAfyhpqtRRETRwQALAAIGLGgyE---DLPVE 125
Cdd:COG4778 81 QASPREILALrrrtiGYvsqflrvIPRVSAldvvaepllERGVDREEA------RARAR-ELLARLNLP--ErlwDLPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 126 QLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQPLAFN-VAHRTLTLTP 200
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREaVADRVVDVTP 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-158 |
5.61e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTS----LLRLLvglarPEEGEVYWRGEPLaHQRSafHQELLWLGHL----- 82
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL-HNLN--RRQLLPVRHRiqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 --------PGIKAALTADENLAFYHPQ---TRRETR-WQALAAIGL--GGYEDLPVEqLSAGQQRRVALARLWLSEASLW 148
Cdd:PRK15134 369 qdpnsslnPRLNVLQIIEEGLRVHQPTlsaAQREQQvIAVMEEVGLdpETRHRYPAE-FSGGQRQRIAIARALILKPSLI 447
|
170
....*....|
gi 1354918145 149 VLDEPLTALD 158
Cdd:PRK15134 448 ILDEPTSSLD 457
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-184 |
6.52e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 24 VSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRgeplahQRSAFH-QELlwlghlpGIKAALTADENLAFYHPQT 102
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKISYKpQYI-------SPDYDGTVEEFLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 103 RRETRWQALAAIGLGGYE--DLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA---AGVATLTRRLEahAARGG 177
Cdd:COG1245 430 FGSSYYKTEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIRRFA--ENRGK 507
|
....*..
gi 1354918145 178 AVIVTTH 184
Cdd:COG1245 508 TAMVVDH 514
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-184 |
7.07e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 3 EARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYwRGEPLahQRSAFHQEllwlghl 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL--EVAYFDQH------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 pgiKAAL----TADENLA----------------------FYHPQtRRETrwqalaaiglggyedlPVEQLSAGQQRRVA 136
Cdd:PRK11147 391 ---RAELdpekTVMDNLAegkqevmvngrprhvlgylqdfLFHPK-RAMT----------------PVKALSGGERNRLL 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1354918145 137 LARLWLSEASLWVLDEPLTALDaagVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLD---VETLELLEELLDSYQGTVLLVSH 495
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-158 |
7.99e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 22 FRVSPGEIVHLTGANGAGKTSLLRLL---VGL--------------------ARPEEGEVY-WRGEPLAHQRS---AFHQ 74
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILngeVLLddgriiyeqdlivarlqqdpPRNVEGTVYdFVAEGIEEQAEylkRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 75 ELLWLGHLPGIK-----AALTAD-ENLAFYHPQTRREtrwQALAAIGLGGyeDLPVEQLSAGQQRRVALARLWLSEASLW 148
Cdd:PRK11147 104 ISHLVETDPSEKnlnelAKLQEQlDHHNLWQLENRIN---EVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170
....*....|
gi 1354918145 149 VLDEPLTALD 158
Cdd:PRK11147 179 LLDEPTNHLD 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-185 |
8.50e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVG-LARPEEGEVYWRGEplahqrSAFHQELLWLGHLpgikaalTADENLAF- 97
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS------VAYVPQVSWIFNA-------TVRENILFg 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 98 --YHPqtrrETRWQALAAIGLGGYEDL-PVEQL----------SAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVAT 164
Cdd:PLN03232 703 sdFES----ERYWRAIDVTALQHDLDLlPGRDLteigergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180
....*....|....*....|.
gi 1354918145 165 LTRRLEAHAARGGAVIVTTHQ 185
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQ 799
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-169 |
9.60e-09 |
|
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: 54.31 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLAC--------LRDERLLFRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLArPEEGEVYWRGEPLAHQRs 70
Cdd:COG4172 276 LEARDLKVwfpikrglFRRTVGHVKAVdgvSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLS- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 71 afHQELLWL------------GHL-PGIKAALTADENLAFYHPQTRRETR----WQALAAIGLGGyEDL---PVEqLSAG 130
Cdd:COG4172 354 --RRALRPLrrrmqvvfqdpfGSLsPRMTVGQIIAEGLRVHGPGLSAAERrarvAEALEEVGLDP-AARhryPHE-FSGG 429
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1354918145 131 QQRRVALARLWLSEASLWVLDEPLTALDA---AGVATLTRRL 169
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVsvqAQILDLLRDL 471
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-167 |
9.71e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.94 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 19 ALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-AHQRSAFHQELLWLGHLPGIK-AALTADENLA 96
Cdd:PRK13642 25 GVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtAENVWNLRRKIGMVFQNPDNQfVGATVEDDVA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354918145 97 FYH-----PQTRRETRW-QALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTR 167
Cdd:PRK13642 105 FGMenqgiPREEMIKRVdEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-197 |
1.01e-08 |
|
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: 53.39 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYW-----RGEPLAHQRSAF---HQE-LLWLGhl 82
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvRDYTLASLRRQIglvSQDvFLFND-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 83 pgikaalTADENLAFYHPQTRRETRWQALAAIGL--------GGYEDLPVE---QLSAGQQRRVALARLWLSEASLWVLD 151
Cdd:cd03251 91 -------TVAENIAYGRPGATREEVEEAARAANAhefimelpEGYDTVIGErgvKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1354918145 152 EPLTALDAAGVATLTRRLEaHAARGGAVIVtthqplafnVAHRTLT 197
Cdd:cd03251 164 EATSALDTESERLVQAALE-RLMKNRTTFV---------IAHRLST 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-185 |
1.01e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLL--FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQrsaFHQE 75
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEneLVALnniSYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDK---KNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 76 LLWLGHLP-GIKAA--LTADENLAFYHP---------------------QTRRETRWQA---LAAIGLG-GYEDLPVEQL 127
Cdd:PRK13631 98 ELITNPYSkKIKNFkeLRRRVSMVFQFPeyqlfkdtiekdimfgpvalgVKKSEAKKLAkfyLNKMGLDdSYLERSPFGL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1354918145 128 SAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQ 185
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-176 |
1.11e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 10 LRDERLLfRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEvywrgeplaHQRSAFHQELLWLGHLPGIKAAL 89
Cdd:PRK10938 13 LSDTKTL-QLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---------RQSQFSHITRLSFEQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TADENLAFYHP---------------QTRRETRWQALAAI-GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:PRK10938 83 WQRNNTDMLSPgeddtgrttaeiiqdEVKDPARCEQLAQQfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180
....*....|....*....|...
gi 1354918145 154 LTALDAAGVATLTRRLEAHAARG 176
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSG 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-200 |
1.50e-08 |
|
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: 52.41 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGE-----PLAHQRSAF----HQELLWLGhlpgikaa 88
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLtiipQDPTLFSG-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 lTADENLAFYHPQTRRETRwQALaAIGLGGyedlpvEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRR 168
Cdd:cd03369 97 -TIRSNLDPFDEYSDEEIY-GAL-RVSEGG------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 169 LeaHAARGGAVIVTthqplafnVAHRTLTLTP 200
Cdd:cd03369 168 I--REEFTNSTILT--------IAHRLRTIID 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-184 |
1.77e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.17 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYW--RGEPLAHQRSAFHQEL----LWLGHLPGIKA 87
Cdd:PRK13651 20 LKALdnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifKDEKNKKKTKEKEKVLeklvIQKTRFKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 A--------------------LTADENLAF---YHPQTRRETRWQALAAIGLGGyedLPVE-------QLSAGQQRRVAL 137
Cdd:PRK13651 100 IkeirrrvgvvfqfaeyqlfeQTIEKDIIFgpvSMGVSKEEAKKRAAKYIELVG---LDESylqrspfELSGGQKRRVAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1354918145 138 ARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-184 |
2.16e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RALS---FRVSPGEIVHLTGANGAGKTSLLRLLVGL--ARPEEGEVYWRGEPLahqrsAF--------------HQEL-- 76
Cdd:NF040905 15 KALDdvnLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVC-----RFkdirdsealgiviiHQELal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 ---------LWLGHLPGIKAALTADEnlafyhpqTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASL 147
Cdd:NF040905 90 ipylsiaenIFLGNERAKRGVIDWNE--------TNRRAR-ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 148 WVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
9-201 |
2.30e-08 |
|
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: 51.21 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 9 CLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLR---LLVGLARPEE--GEVYWRGEPLAHQRSAFHQELLwlghlp 83
Cdd:cd03227 3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATrrRSGVKAGCIVAAVSAELIFTRL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 84 gikaaltadenlafyhpqtrretrwqalaaiglggyedlpveQLSAGQQRRVALA---RLW-LSEASLWVLDEPLTALDA 159
Cdd:cd03227 77 ------------------------------------------QLSGGEKELSALAlilALAsLKPRPLYILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1354918145 160 AGVATLTRRLEAHAARGGAVIVTTHQPLAFNVAHRTLTLTPE 201
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
12-203 |
2.83e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.42 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFrvSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWrgeplahqrsafhqellwlghlPGIKAAlta 91
Cdd:cd03222 12 VFFLLVELGVV--KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW----------------------DGITPV--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 denlafYHPQtrretrwqalaaiglggYEDlpveqLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA---GVATLTRR 168
Cdd:cd03222 65 ------YKPQ-----------------YID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|....*.
gi 1354918145 169 LEAHAARggAVIVTTHQPLAFN-VAHRTLTLTPEPA 203
Cdd:cd03222 117 LSEEGKK--TALVVEHDLAVLDyLSDRIHVFEGEPG 150
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-158 |
3.40e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFR--------ALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSA 71
Cdd:PRK15112 4 LLEVRNLSkTFRYRTGWFRrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 FHQELLWL---------------GHLPGIKAALTADENlafyhPQTRRETRWQALAAIGLggyedLP------VEQLSAG 130
Cdd:PRK15112 84 YRSQRIRMifqdpstslnprqriSQILDFPLRLNTDLE-----PEQREKQIIETLRQVGL-----LPdhasyyPHMLAPG 153
|
170 180
....*....|....*....|....*...
gi 1354918145 131 QQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLD 181
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-158 |
4.87e-08 |
|
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: 51.18 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYW-----RGEPLAHQRSAFHQELLWLGHLPGIKAAlTADEN 94
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnkneSEPSFEATRSRNRYSVAYAAQKPWLLNA-TVEEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 95 LAFYHPQTRRetRWQALA-AIGLGGYED-LPVE----------QLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:cd03290 99 ITFGSPFNKQ--RYKAVTdACSLQPDIDlLPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-186 |
5.01e-08 |
|
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: 52.11 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGL--ARPEEGEVYWR----------------GE 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 64 PLAHQRSAFHQEL--LWLGHLPGIKA-----ALTADENLAFYHPQTRRETRWQALAAIGLGGYEDLP-----VEQ----- 126
Cdd:TIGR03269 81 PCPVCGGTLEPEEvdFWNLSDKLRRRirkriAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGravdlIEMvqlsh 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 127 --------LSAGQQRRVALARLWLSEASLWVLDEPLTALDAAgVATLTRR--LEAHAARGGAVIVTTHQP 186
Cdd:TIGR03269 161 rithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ-TAKLVHNalEEAVKASGISMVLTSHWP 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-161 |
5.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.59 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSafhqellwlgHLPGIKAAL---------- 89
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV----------KLSDIRKKVglvfqypeyq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 ----TADENLAFyHPQTRRETR-------WQALAAIGLGgYEDL----PVEqLSAGQQRRVALARLWLSEASLWVLDEPL 154
Cdd:PRK13637 96 lfeeTIEKDIAF-GPINLGLSEeeienrvKRAMNIVGLD-YEDYkdksPFE-LSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
....*..
gi 1354918145 155 TALDAAG 161
Cdd:PRK13637 173 AGLDPKG 179
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-185 |
8.28e-08 |
|
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: 51.01 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARpEEGE-----VYWRGEPLAHQRSAFhqellwlGHLPGIKAALTAD-- 92
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDiqidgVSWNSVPLQKWRKAF-------GVIPQKVFIFSGTfr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 93 ENLAFYHpQTRRETRWQALAAIGL-----------------GGYedlpveQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:cd03289 95 KNLDPYG-KWSDEEIWKVAEEVGLksvieqfpgqldfvlvdGGC------VLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 156 ALDAAGVATLTRRLEaHAARGGAVIVTTHQ 185
Cdd:cd03289 168 HLDPITYQVIRKTLK-QAFADCTVILSEHR 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-160 |
8.75e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 26 PGEIVHLTGANGAGKTSLLRLL----VGLARPEEGEVYWRGEPLAHQRSAFHQELLWLG----HLPGIKAALTADENLAF 97
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAetdvHFPHLTVGETLDFAARC 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1354918145 98 YHPQTR-----RETRWQ-----ALAAIGLGGYEDLPV-----EQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:TIGR00956 166 KTPQNRpdgvsREEYAKhiadvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-158 |
9.43e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLA--------CLRDERLLfRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLA---- 66
Cdd:PRK11308 6 LQAIDLKkhypvkrgLFKPERLV-KALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 67 HQRSAFHQELLWL-----GHL-PGIKAALTADENLAFYHPQTRRETRWQALAAIGLGG-----YEDLPvEQLSAGQQRRV 135
Cdd:PRK11308 85 EAQKLLRQKIQIVfqnpyGSLnPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGlrpehYDRYP-HMFSGGQRQRI 163
|
170 180
....*....|....*....|...
gi 1354918145 136 ALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALD 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-186 |
9.94e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.82 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFH-------QELLWLGHLPG 84
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQidaiklrKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 85 IKAALTADENLAF----YHPQTRRETR---WQALAAIGLGG--YEDL--PVEQLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:PRK14246 101 PFPHLSIYDNIAYplksHGIKEKREIKkivEECLRKVGLWKevYDRLnsPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190
....*....|....*....|....*....|...
gi 1354918145 154 LTALDAAGVATLtRRLEAHAARGGAVIVTTHQP 186
Cdd:PRK14246 181 TSMIDIVNSQAI-EKLITELKNEIAIVIVSHNP 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-184 |
1.01e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 27 GEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRgeplahQRSAFH-QELlwlghlpGIKAALTADENLAFyHPQTRRE 105
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKpQYI-------KPDYDGTVEDLLRS-ITDDLGS 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 106 TRWQALAAIGLGGYE--DLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA---AGVATLTRRLEahAARGGAVI 180
Cdd:PRK13409 431 SYYKSEIIKPLQLERllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIRRIA--EEREATAL 508
|
....
gi 1354918145 181 VTTH 184
Cdd:PRK13409 509 VVDH 512
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-184 |
2.33e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEV-YWRGEPLAHqrSAFHQellwlghLPGIKAALTA 91
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY--FAQHQ-------LEFLRADESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLAFYHPQTRRETRWQALAAIGLGGYE-DLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTrrlE 170
Cdd:PRK10636 395 LQHLARLAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT---E 471
|
170
....*....|....
gi 1354918145 171 AHAARGGAVIVTTH 184
Cdd:PRK10636 472 ALIDFEGALVVVSH 485
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-185 |
2.42e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 14 RLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYwrgeplAHQRSAFHQELLWlghlpgIKAAlTADE 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------AERSIAYVPQQAW------IMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 94 NLAFYHPQtrRETRWQA----------LAAIGlGGYEDLPVEQ---LSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:PTZ00243 740 NILFFDEE--DAARLADavrvsqleadLAQLG-GGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180
....*....|....*....|....*
gi 1354918145 161 GVATLTRRLEAHAARGGAVIVTTHQ 185
Cdd:PTZ00243 817 VGERVVEECFLGALAGKTRVLATHQ 841
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-161 |
2.69e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGeplahqRSAFHQELLWlghlpGIK------------- 86
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------LDTSDEENLW-----DIRnkagmvfqnpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 -AALTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:PRK13633 98 iVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
..
gi 1354918145 160 AG 161
Cdd:PRK13633 178 SG 179
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-171 |
3.40e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRG--------EPLAHQRSAFHQELLWLghlpgikaALTA 91
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtrASLRRNIAVVFQDAGLF--------NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLAFYHPQ-TRRETRWQALAAIGL-------GGYEDLPVE---QLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:PRK13657 426 EDNIRVGRPDaTDEEMRAAAERAQAHdfierkpDGYDTVVGErgrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170
....*....|.
gi 1354918145 161 GVATLTRRLEA 171
Cdd:PRK13657 506 TEAKVKAALDE 516
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-159 |
3.84e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVG-LARPEEGEVYWRGeplahqRSAFHQELLWlghlpgIKAAlTA 91
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG------TVAYVPQVSW------IFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 92 DENLAFYHPqTRRETRWQALAAIGL--------GGyeDLpVE------QLSAGQQRRVALARLWLSEASLWVLDEPLTAL 157
Cdd:PLN03130 696 RDNILFGSP-FDPERYERAIDVTALqhdldllpGG--DL-TEigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
..
gi 1354918145 158 DA 159
Cdd:PLN03130 772 DA 773
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
21-160 |
4.14e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.03 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGE--------PLAHQRSA----F-HQELLwlghlpgikA 87
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekELRKARRQigmiFqHFNLL---------S 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1354918145 88 ALTADENLAF-----YHPQTRRETRWQALAAI-GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:PRK11153 96 SRTVFDNVALplelaGTPKAEIKARVTELLELvGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-159 |
4.92e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.33 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 11 RDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH-QRSAFHQELLWLGHLPGIKAAl 89
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQQDPVVLAD- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 tadenlAFYHPQT-----RRETRWQALAAIGL--------GGYEDLPVEQ---LSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:PRK10790 430 ------TFLANVTlgrdiSEEQVWQALETVQLaelarslpDGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEA 503
|
....*.
gi 1354918145 154 LTALDA 159
Cdd:PRK10790 504 TANIDS 509
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-158 |
5.12e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.33 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQR-SAFHQELLWLGHLPGIKAALTADeNLAFY 98
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAVVSQTPFLFSDTVAN-NIALG 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1354918145 99 HPQTRRETRWQA--LAAIGLG------GYEDLPVEQ---LSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK10789 413 RPDATQQEIEHVarLASVHDDilrlpqGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-186 |
6.33e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.37 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLAR--PE---EGEVYWRGeplahqRSAFHQEL 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDG------QDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 LWLG-------HLPGIKAALTADENLAF-----YHPQTRRE----TRWqALAAIGLggYE------DLPVEQLSAGQQRR 134
Cdd:PRK14247 78 IELRrrvqmvfQIPNPIPNLSIFENVALglklnRLVKSKKElqerVRW-ALEKAQL--WDevkdrlDAPAGKLSGGQQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1354918145 135 VALARLWLSEASLWVLDEPLTALDAAGVATLtRRLEAHAARGGAVIVTTHQP 186
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHFP 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-184 |
7.83e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 18 RAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQR-----SAFHQELLWLGHLPGIKA-A 88
Cdd:PRK13649 21 RALfdvNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLVFQFPESQLfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTADENLAFyHPQ----TRRETRWQALAAIGLGGY-EDL----PVEqLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:PRK13649 101 ETVLKDVAF-GPQnfgvSQEEAEALAREKLALVGIsESLfeknPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180
....*....|....*....|....*
gi 1354918145 160 AGVATLTRRLEAHAARGGAVIVTTH 184
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-184 |
7.96e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLwlghlpGIK----- 86
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI------GIIfqnpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 ---AALTADENLAF------YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTAL 157
Cdd:PRK13632 94 nqfIGATVEDDIAFglenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180
....*....|....*....|....*...
gi 1354918145 158 DAAGVATLTRRL-EAHAARGGAVIVTTH 184
Cdd:PRK13632 174 DPKGKREIKKIMvDLRKTRKKTLISITH 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-184 |
9.17e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 26 PGEIVHLTGANGAGKTSLLRLLVGLARPE----EGEVYWRgEPLAHQRSAFHQELL---------------WLGHLPgiK 86
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNlgkfDDPPDWD-EILDEFRGSELQNYFtkllegdvkvivkpqYVDLIP--K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 87 AAL-TADENLAFYHPQTRRETRWQALaaiGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA---GV 162
Cdd:cd03236 102 AVKgKVGELLKKKDERGKLDELVDQL---ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNA 178
|
170 180
....*....|....*....|..
gi 1354918145 163 ATLTRRLEAHaarGGAVIVTTH 184
Cdd:cd03236 179 ARLIRELAED---DNYVLVVEH 197
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-184 |
9.96e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLaCLRDERLLFRALSFRVSPGEIVHLTGANGAGKT----SLLRLLVGLARPEEGEVYWRGEPLAHQ--------- 68
Cdd:PRK10418 5 IELRNI-ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCalrgrkiat 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 69 -----RSAFHqellwlghlPGIKAALTADENLAFYHPQTRRETRWQALAAIGLGGYE---DLPVEQLSAGQQRRVALARL 140
Cdd:PRK10418 84 imqnpRSAFN---------PLHTMHTHARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1354918145 141 WLSEASLWVLDEPLTALDAAGVATLTRRLEAHAA-RGGAVIVTTH 184
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTH 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-184 |
1.01e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGE---VYWRGEPLAhqrsafhQELLW-LGHLPGI---------- 85
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLT-------AKTVWdIREKVGIvfqnpdnqfv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 86 KAALTAD-----ENLAFYHPQTRRETRwQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAA 160
Cdd:PRK13640 99 GATVGDDvafglENRAVPRPEMIKIVR-DVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180
....*....|....*....|....*..
gi 1354918145 161 G---VATLTRRLEAHaaRGGAVIVTTH 184
Cdd:PRK13640 178 GkeqILKLIRKLKKK--NNLTVISITH 202
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-152 |
1.38e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 10 LRDERLLFRALSFRVSP-------GEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL-AHQRSAFHQEL----- 76
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFsavft 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 77 -LWL-GHLPGiKAALTADENLAFyhpqtrretRWqaLAAIGLGgyEDLPVE-------QLSAGQQRRVALARLWLSEASL 147
Cdd:PRK10522 405 dFHLfDQLLG-PEGKPANPALVE---------KW--LERLKMA--HKLELEdgrisnlKLSKGQKKRLALLLALAEERDI 470
|
....*
gi 1354918145 148 WVLDE 152
Cdd:PRK10522 471 LLLDE 475
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-170 |
1.49e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKT----SLLRLLvglarPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAA 88
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSPPVVYPSGDIRFHGESLLHASEQTLRGVRGNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTADENLAFYHP------------QTRRETRWQALAAIGLGGYE------------DLPvEQLSAGQQRRVALARLWLSE 144
Cdd:PRK15134 96 MIFQEPMVSLNPlhtlekqlyevlSLHRGMRREAARGEILNCLDrvgirqaakrltDYP-HQLSGGERQRVMIAMALLTR 174
|
170 180
....*....|....*....|....*....
gi 1354918145 145 ASLWVLDEPLTALDA---AGVATLTRRLE 170
Cdd:PRK15134 175 PELLIADEPTTALDVsvqAQILQLLRELQ 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-158 |
1.84e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.51 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAH--QRSafhqellwlghlpgIKAAL- 89
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvtQAS--------------LRAAIg 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 -----------TADENLAFYHPQTRRETRWQA--LAAI-----GL-GGYEDLPVE---QLSAGQQRRVALARLWLSEASL 147
Cdd:COG5265 436 ivpqdtvlfndTIAYNIAYGRPDASEEEVEAAarAAQIhdfieSLpDGYDTRVGErglKLSGGEKQRVAIARTLLKNPPI 515
|
170
....*....|.
gi 1354918145 148 WVLDEPLTALD 158
Cdd:COG5265 516 LIFDEATSALD 526
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-186 |
2.13e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERL-LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGlaRPE----EGEVYWRGEPLAHQRSA----------FH--- 73
Cdd:PLN03140 890 EDRLqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKKQETFArisgyceqndIHspq 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 ---QELLWLGHLPGIKAALTADENLAFYHpQTRRETRWQAL--AAIGLGGyedlpVEQLSAGQQRRVALARLWLSEASLW 148
Cdd:PLN03140 968 vtvRESLIYSAFLRLPKEVSKEEKMMFVD-EVMELVELDNLkdAIVGLPG-----VTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*...
gi 1354918145 149 VLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1079
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-158 |
2.42e-06 |
|
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: 46.99 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLA-CLRDERLLFRA---LSFRVSPGEIVHLTGANGAGKT----SLLRLLVGLARPEEGEVYWRGEPLAHQRSA- 71
Cdd:COG4172 6 LLSVEDLSvAFGQGGGTVEAvkgVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 72 ------------FhQEllwlghlPgikaaLTA-----------DENLAFYHPQTRRETRWQALAAIGLGG-------YED 121
Cdd:COG4172 86 lrrirgnriamiF-QE-------P-----MTSlnplhtigkqiAEVLRLHRGLSGAAARARALELLERVGipdperrLDA 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1354918145 122 LPvEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:COG4172 153 YP-HQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-185 |
2.50e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.94 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 27 GEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAfhQELLWLGHLPGI-----KAAL---TADENLAFy 98
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN--KKLKPLRKKVGIvfqfpEHQLfeeTVEKDICF- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 99 HPQ----TRRETRWQALAAIGLGGY-EDL----PVEqLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGvatltrRL 169
Cdd:PRK13634 110 GPMnfgvSEEDAKQKAREMIELVGLpEELlarsPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG------RK 182
|
170 180
....*....|....*....|...
gi 1354918145 170 EA-------HAARGGAVIVTTHQ 185
Cdd:PRK13634 183 EMmemfyklHKEKGLTTVLVTHS 205
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
88-185 |
2.88e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 ALTADENLAFY--HPQTRRetRWQALAAIGLGgYEDL--PVEQLSAGQQRRVALARLwLSEAS----LWVLDEPLTALDA 159
Cdd:cd03271 130 DMTVEEALEFFenIPKIAR--KLQTLCDVGLG-YIKLgqPATTLSGGEAQRIKLAKE-LSKRStgktLYILDEPTTGLHF 205
|
90 100
....*....|....*....|....*.
gi 1354918145 160 AGVATLTRRLEAHAARGGAVIVTTHQ 185
Cdd:cd03271 206 HDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-181 |
5.99e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.08 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDE---RLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGlARP--EEGEVYWRGEPLA--HQRSAFH 73
Cdd:PRK13549 259 ILEVRNLTAWDPVnphIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKirNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 74 QELlwlGHLP------GIKAALTADENLAFyhPQTRRETRWQAL-AAIGLGGYE-------------DLPVEQLSAGQQR 133
Cdd:PRK13549 338 QGI---AMVPedrkrdGIVPVMGVGKNITL--AALDRFTGGSRIdDAAELKTILesiqrlkvktaspELAIARLSGGNQQ 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1354918145 134 RVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIV 181
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-159 |
8.00e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.22 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRG------EP------LAHQRSAF--Hqellwlghlpgi 85
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelEPadrdiaMVFQNYALypH------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 86 kaaLTADENLAfYH------PQTRRETRWQALAAI-GLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK11650 91 ---MSVRENMA-YGlkirgmPKAEIEERVAEAARIlELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
.
gi 1354918145 159 A 159
Cdd:PRK11650 167 A 167
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
117-187 |
9.55e-06 |
|
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: 45.07 E-value: 9.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1354918145 117 GGYEDLPVEQLSAGQQRRVALARLWLS---EASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQPL 187
Cdd:pfam13304 227 GGGGELPAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-158 |
1.08e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 34 GANGAGKTSLLRLLVGLARPEEGEVYWRGEPL----------AHQRS---AFhQELLWLGHLpgikaalTADENLAFyhp 100
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgiclpPEKRRigyVF-QDARLFPHY-------KVRGNLRY--- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1354918145 101 QTRRETRWQALAAIGLGGYEDL----PVeQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPLldryPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-158 |
1.72e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGeplahqrSAfhqELLWLGhlPGIKAALTADENLAF-- 97
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SA---ALIAIS--SGLNGQLTGIENIELkg 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 98 ----YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK13545 111 lmmgLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-158 |
1.75e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 12 DERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVG---------LA----RPEEGEVYWR-GEPLAHQRSAFHQE-- 75
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndLTlfgrRRGSGETIWDiKKHIGYVSSSLHLDyr 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 76 -------LLWLGHLPGI---KAALTADENLAFyhpqtrretrwQALAAIGLGGY-EDLPVEQLSAGQQRRVALARLWLSE 144
Cdd:PRK10938 351 vstsvrnVILSGFFDSIgiyQAVSDRQQKLAQ-----------QWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKH 419
|
170
....*....|....
gi 1354918145 145 ASLWVLDEPLTALD 158
Cdd:PRK10938 420 PTLLILDEPLQGLD 433
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
89-201 |
2.08e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTADENLAFY--HPQTRRetRWQALAAIGLGgYEDL--PVEQLSAGQQRRVALARlWLSEAS----LWVLDEPLTALDAA 160
Cdd:TIGR00630 791 MTVEEAYEFFeaVPSISR--KLQTLCDVGLG-YIRLgqPATTLSGGEAQRIKLAK-ELSKRStgrtLYILDEPTTGLHFD 866
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1354918145 161 GVATLTRRLEAHAARGGAVIVTTHQPLAFNVAHRTLTLTPE 201
Cdd:TIGR00630 867 DIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPE 907
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
88-201 |
2.18e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 ALTADENLAFYHPQTRRETRWQALAAIGLGgYEDL--PVEQLSAGQQRRVALARLWLS---EASLWVLDEPLTALDAAGV 162
Cdd:PRK00635 770 EMTAYEAEKFFLDEPSIHEKIHALCSLGLD-YLPLgrPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDI 848
|
90 100 110
....*....|....*....|....*....|....*....
gi 1354918145 163 ATLTRRLEAHAARGGAVIVTTHQPLAFNVAHRTLTLTPE 201
Cdd:PRK00635 849 KALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPE 887
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-186 |
3.13e-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: 43.84 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRALSFRVSPGEIVhLTGANGAGKTSLLRLLVGLARPEEGEV-----YWRGEPLAHQR-----------SAFHQELLWLG 80
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRKfdeedFYLGDDPDLPEieieltfgsllSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAALTA-------------------------DENLAFyHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRV 135
Cdd:COG3593 93 DKEELEEALEElneelkealkalnellseylkelldGLDLEL-ELSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1354918145 136 ALA-RLWLSEA------SLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTTHQP 186
Cdd:COG3593 172 LLAlLSALAELkrapanPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSP 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-183 |
3.44e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLAclRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAhqrsafhqellwlg 80
Cdd:PRK09700 265 VFEVRNVT--SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-------------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 hlpgIKAALTADENLAFYHPQTRRETRW-------QALA---AIGLGGY--------------------EDL-----PVE 125
Cdd:PRK09700 329 ----PRSPLDAVKKGMAYITESRRDNGFfpnfsiaQNMAisrSLKDGGYkgamglfhevdeqrtaenqrELLalkchSVN 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1354918145 126 Q----LSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHAARGGAVIVTT 183
Cdd:PRK09700 405 QniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-158 |
4.66e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLaHQRSAfHQEL---------------LWLGHLPGI 85
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV-VTRSP-QDGLangivyisedrkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1354918145 86 KAALTADENLAFYHPQTRRETRWQALAA-IGLGGYE----DLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK10762 350 NMSLTALRYFSRAGGSLKHADEQQAVSDfIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-184 |
8.01e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 42.30 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 17 FRAL---SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYW------RGEPLAHQRSAFHQELLWLGHLPGIKA 87
Cdd:PRK13645 24 FKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQFPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 88 -ALTADENLAFyHPQTRRETRWQALAAI-GLGGYEDLPVE-------QLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK13645 104 fQETIEKDIAF-GPVNLGENKQEAYKKVpELLKLVQLPEDyvkrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180
....*....|....*....|....*....
gi 1354918145 159 AAG---VATLTRRLEAHaaRGGAVIVTTH 184
Cdd:PRK13645 183 PKGeedFINLFERLNKE--YKKRIIMVTH 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-63 |
8.90e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 8.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGlaRPE----EGEVYWRGE 63
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGE 71
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-158 |
1.19e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.68 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLL--VGLARPE---EGEVYWRGEPLAHQRS----- 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTdtvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 71 ------AFHQ---------ELLWLG-HLPGIKAALTADENLafyHPQTRRETRWQAL------AAIGLGGyedlpveqls 128
Cdd:PRK14239 85 rkeigmVFQQpnpfpmsiyENVVYGlRLKGIKDKQVLDEAV---EKSLKGASIWDEVkdrlhdSALGLSG---------- 151
|
170 180 190
....*....|....*....|....*....|
gi 1354918145 129 aGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK14239 152 -GQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-194 |
1.51e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.62 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 29 IVHLTGANGAGKTSLLRLLVGLARPEEGEVYwRGEPLAHQRSAF-HQELL-------WLGHLPGIKAALTADENLAFYHP 100
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYRY-SGDVLLGGRSIFnYRDVLefrrrvgMLFQRPNPFPMSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 101 QT---RRETRWQA---LAAIGL-----GGYEDLPVeQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRL 169
Cdd:PRK14271 128 HKlvpRKEFRGVAqarLTEVGLwdavkDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180
....*....|....*....|....*
gi 1354918145 170 EAHAARGGAVIVTTHQPLAFNVAHR 194
Cdd:PRK14271 207 RSLADRLTVIIVTHNLAQAARISDR 231
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
2-199 |
2.03e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 40.37 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 2 LEARNLACLRDERLLFRALSFRVspgeivhLTGANGAGKTSLL-RLLVGLarpeegevywrGEPLAHQRSAFHQELLWLG 80
Cdd:cd03239 4 ITLKNFKSYRDETVVGGSNSFNA-------IVGPNGSGKSNIVdAICFVL-----------GGKAAKLRRGSLLFLAGGG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 81 HLPGIKAA---LTADENLaFYHPQTRretrwqalaaiglggyedlpVEQ-LSAGQQRRVALARLW----LSEASLWVLDE 152
Cdd:cd03239 66 VKAGINSAsveITFDKSY-FLVLQGK--------------------VEQiLSGGEKSLSALALIFalqeIKPSPFYVLDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1354918145 153 PLTALDAAGVATLTRRLEAHAARGGAVIVTTHQPLAFNVAHRTLTLT 199
Cdd:cd03239 125 IDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVL 171
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-65 |
2.03e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 2.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354918145 1 MLEARNLACLRDERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPE--EGEVYWRGEPL 65
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDL 67
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-184 |
2.67e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 24 VSPGEIVHLTGANGAGKTSLLRLLVGLARP----EEGEVYWRgEPLAHQR-SAFHQ--ELLWLGhlpGIKAAL------- 89
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWD-EVLKRFRgTELQNyfKKLYNG---EIKVVHkpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 --------------TADEnlafyhpqtrRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLT 155
Cdd:PRK13409 172 ipkvfkgkvrellkKVDE----------RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|..
gi 1354918145 156 ALDAA---GVATLTRRLeahaARGGAVIVTTH 184
Cdd:PRK13409 242 YLDIRqrlNVARLIREL----AEGKYVLVVEH 269
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-157 |
2.75e-04 |
|
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: 40.89 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 16 LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGL--------ARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKA 87
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1354918145 88 ALTADENLAFY------HPQTRRETRWQALAaiglgGYEDLpveqLSAGQQRRVALARLWLSEASLWVLDEPLTAL 157
Cdd:TIGR00954 547 RGLSDKDLEQIldnvqlTHILEREGGWSAVQ-----DWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-158 |
5.73e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 16 LFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAFHQELLWLGHLPGIKAALTADENL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1354918145 96 AFYHPQTRRETrWQAL-----------AAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PLN03232 1331 DPFSEHNDADL-WEALerahikdvidrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-158 |
1.25e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 39.23 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 13 ERLLFRALSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRG--------EPLAHQRSAFHQELlwlgHLPG 84
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlASLRNQVALVSQNV----HLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 85 IKAAltadENLAFyhPQTRRETRWQALAA--------------------IGLGGYedlpveQLSAGQQRRVALARLWLSE 144
Cdd:PRK11176 431 DTIA----NNIAY--ARTEQYSREQIEEAarmayamdfinkmdngldtvIGENGV------LLSGGQRQRIAIARALLRD 498
|
170
....*....|....
gi 1354918145 145 ASLWVLDEPLTALD 158
Cdd:PRK11176 499 SPILILDEATSALD 512
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-158 |
1.42e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPLAHQRSAfhqellwlghlpGIKAALTADENLAF-- 97
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISA------------GLSGQLTGIENIEFkm 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1354918145 98 ----YHPQTRRETRWQALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALD 158
Cdd:PRK13546 111 lcmgFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-153 |
1.62e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.95 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 21 SFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYWRGEPL------AHQR-----SAFHqelLWlghlpgikAAL 89
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagdiaTRRRvgymsQAFS---LY--------GEL 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 90 TADENLAF----YH-PQTRRETRWQALAA-IGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEP 153
Cdd:NF033858 355 TVRQNLELharlFHlPAAEIAARVAEMLErFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-184 |
1.94e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.59 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 32 LTGANGAGKTSLLR-LLVGLArpeeGEVYWRGEPLAHQRSAFH------QELLWLGHLPGIKAALTAD----ENLAFYHp 100
Cdd:cd03240 27 IVGQNGAGKTTIIEaLKYALT----GELPPNSKGGAHDPKLIRegevraQVKLAFENANGKKYTITRSlailENVIFCH- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 101 qtRRETRWQALaaiglggyedLPVEQLSAGQQR------RVALARLWLSEASLWVLDEPLTALDAAGVAT-LTRRLEAHA 173
Cdd:cd03240 102 --QGESNWPLL----------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERK 169
|
170
....*....|..
gi 1354918145 174 A-RGGAVIVTTH 184
Cdd:cd03240 170 SqKNFQLIVITH 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-184 |
2.19e-03 |
|
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: 38.23 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 26 PGEIVHLTGANGAGKTSLLRLLVGLARPE----EGEVYWRgEPLAHQR-SAFHQellwlgHLPGIkaaltADENL-AFYH 99
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlgdyDEEPSWD-EVLKRFRgTELQD------YFKKL-----ANGEIkVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 100 PQ-----------TRRET--------RWQALA-AIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:COG1245 166 PQyvdlipkvfkgTVRELlekvdergKLDELAeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*...
gi 1354918145 160 ---AGVATLTRRLeahAARGGAVIVTTH 184
Cdd:COG1245 246 yqrLNVARLIREL---AEEGKYVLVVEH 270
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
120-194 |
2.49e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.62 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 120 EDLPVEQLSAGQQRRVALArLWLS-----EASLWVLDEPLTALDA---AGVATLTRRLeahaARGGAVIVTTHQPLAFNV 191
Cdd:cd03272 152 EQQEMQQLSGGQKSLVALA-LIFAiqkcdPAPFYLFDEIDAALDAqyrTAVANMIKEL----SDGAQFITTTFRPELLEV 226
|
...
gi 1354918145 192 AHR 194
Cdd:cd03272 227 ADK 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-186 |
3.19e-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: 36.58 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 26 PGEIVHLTGANGAGKTSLLRLLVGLARPEEGEVYwrgeplahqrsafhqellwlghlpgikaALTADENLAfyhpqtrre 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------------YIDGEDILE--------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 106 trwqALAAIGLGGYEDLPVEQLSAGQQRRVALARLWLSEASLWVLDEPLTALDAAGVATLTRRLEAHA------ARGGAV 179
Cdd:smart00382 44 ----EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllksEKNLTV 119
|
....*..
gi 1354918145 180 IVTTHQP 186
Cdd:smart00382 120 ILTTNDE 126
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-58 |
3.75e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 37.80 E-value: 3.75e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1354918145 20 LSFRVSPGEIVHLTGANGAGKTSLLRLLVGLARPEEGEV 58
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI 1296
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
89-184 |
5.26e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354918145 89 LTADENLAFY--HPQTRRetRWQALAAIGLGgYEDL--PVEQLSAGQQRRVALARlWLSEAS----LWVLDEPLTALDAA 160
Cdd:COG0178 788 MTVEEALEFFenIPKIAR--KLQTLQDVGLG-YIKLgqPATTLSGGEAQRVKLAS-ELSKRStgktLYILDEPTTGLHFH 863
|
90 100
....*....|....*....|....
gi 1354918145 161 GVATLTRRLEAHAARGGAVIVTTH 184
Cdd:COG0178 864 DIRKLLEVLHRLVDKGNTVVVIEH 887
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-159 |
5.30e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 37.32 E-value: 5.30e-03
10 20 30
....*....|....*....|....*....|....*
gi 1354918145 125 EQLSAGQQRRVALARLWLSEASLWVLDEPLTALDA 159
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-59 |
7.32e-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: 7.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1354918145 2 LEARNLACLRDerllfRALSFRVSPGEIVhLTGANGAGKTSLLRLLVGLARPEEGEVY 59
Cdd:COG3950 6 LTIENFRGFED-----LEIDFDNPPRLTV-LVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| |
