|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 |
2.81e-114 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 327.05 E-value: 2.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGGVKTNSIYNHIA 80
Cdd:COG1121 9 LENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL----------FGKPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDYPITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:COG1121 79 YVPQRAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNRRLVGMGPVRDIVGSPILDETY 237
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAY 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-222 |
2.48e-101 |
|
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: 292.90 E-value: 2.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGGVKTNSIYNHIA 80
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV----------FGKPLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDYPITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:cd03235 72 YVPQRRSIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNRRLVGMG 222
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-237 |
5.68e-65 |
|
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: 202.20 E-value: 5.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIAY 81
Cdd:COG1120 5 ENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV--LLDGRDLASL---SRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWdyPITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:COG1120 80 VPQEPPAPF--GLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 162 VYILDEPfkgidkTT-------EAVLvKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSPI 232
Cdd:COG1120 158 LLLLDEP------TShldlahqLEVL-ELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDgRIVAQGPPEEVLTPEL 230
|
....*
gi 2786564536 233 LDETY 237
Cdd:COG1120 231 LEEVY 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-238 |
1.64e-57 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 183.93 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldaktvsaygGVKTNSIY--N 77
Cdd:PRK15056 9 VNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIL----------GQPTRQALqkN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQTSAVDWDYPITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:PRK15056 79 LVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 158 ENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNRRLVGMGPVRDIVGSPILDETY 237
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAF 238
|
.
gi 2786564536 238 S 238
Cdd:PRK15056 239 S 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
7-213 |
1.15e-56 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 178.97 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 7 AYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKtvsayggvktnsiynhIAYVPQTS 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR----------------VAYVPQRS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 AVDWDYPITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILD 166
Cdd:NF040873 65 EVPDSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 167 EPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLC 213
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
19-222 |
6.66e-55 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 175.42 E-value: 6.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 19 FQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGGVKTNSIYNHIAYVPQTSAVDWDYPITVFE 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKV----------AGASPGKGWRHIGYVPQRHEFAWDFPISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 99 VVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEA 178
Cdd:TIGR03771 71 TVMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2786564536 179 VLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNRRLVGMG 222
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADG 194
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-237 |
7.84e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.93 E-value: 7.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT-LDAKTVSAyggvktnSIYNHIA 80
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgEDVARDPA-------EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypITVFE-VVLMGTYRRLgwftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:COG1131 77 YVPQEPALYPD--LTVREnLRFFARLYGL-----PRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSpILDETY 237
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDELKAR-LLEDVF 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
2.77e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 161.76 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIYNHI 79
Cdd:COG3638 5 LRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV--DGQDVTALRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQtsavdwDYPI----TVFEVVLMGtyrRLG-------WFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQ 148
Cdd:COG3638 83 GMIFQ------QFNLvprlSVLTNVLAG---RLGrtstwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGID-KTTEAVLvKIMKDMQAA-GKTLLIVHHNLQTLEAYFDqvlcvnrRLVGM 221
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDpKTARQVM-DLLRRIAREdGITVVVNLHQVDLARRYAD-------RIIGL 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-216 |
3.15e-48 |
|
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: 158.01 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDD--TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHI 79
Cdd:cd03225 3 KNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV--LVDGKDLTKL---SLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQtsavdwdYP------ITVFEVVLMGtYRRLGWftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLA 153
Cdd:cd03225 78 GLVFQ-------NPddqffgPTVEEEVAFG-LENLGL---PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 154 RALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-221 |
8.96e-48 |
|
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: 157.73 E-value: 8.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHIA 80
Cdd:cd03256 4 ENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSV--LIDGTDINKLKGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwDYPI----TVFEVVLMGtyrRLG-------WFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQR 149
Cdd:cd03256 82 MIFQ------QFNLierlSVLENVLSG---RLGrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 150 VFLARALVENQDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDqvlcvnrRLVGM 221
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDpASSRQVMDLLKRINREEGITVIVSLHQVDLAREYAD-------RIVGL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
4.07e-47 |
|
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: 155.57 E-value: 4.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKtnsIYNHIA 80
Cdd:COG1122 4 ENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV--LVDGKDITKKNLRE---LRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwdYP------ITVFEVVLMGTyRRLGWftrpGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLA 153
Cdd:COG1122 79 LVFQ-------NPddqlfaPTVEEDVAFGP-ENLGL----PREEIRErVEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 154 RALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDgRIVADGTPREV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-214 |
1.20e-45 |
|
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: 151.09 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAyggvktNSIYNHIAY 81
Cdd:COG4133 6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR------EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVLMgtYRRLgwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:COG4133 80 LGHADGL---KPeLTVRENLRF--WAAL----YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHnlQTLEAYFDQVLCV 214
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDL 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-212 |
1.77e-45 |
|
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: 149.89 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKtnsIYNHIAY 81
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI--LLDGKDLASLSPKE---LARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQtsavdwdypitvfevvlmgtyrrlgwftrpgkrerdeatkALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:cd03214 78 VPQ----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVL 212
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVI 169
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-237 |
1.25e-44 |
|
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: 149.85 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEG-TIELtLDAKtvsaYGGVKTNSIYNHI 79
Cdd:COG1119 6 LRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRL-FGER----RGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVpqTSAVDWDYP--ITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:COG1119 81 GLV--SPALQLRFPrdETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 158 ENQDVYILDEPFKGIDKTTEAVLVKIMKD-MQAAGKTLLIVHHNLQTLEAYFDQVLC-VNRRLVGMGPVRDIVGSPILDE 235
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHHVEEIPPGITHVLLlKDGRVVAAGPKEEVLTSENLSE 238
|
..
gi 2786564536 236 TY 237
Cdd:COG1119 239 AF 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
3.36e-44 |
|
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: 155.06 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAY-----DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYN 77
Cdd:COG1123 265 NLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI--LFDGKDLTKLSRRSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQ--TSAVDwdyP-ITVFEVVLMGtYRRLGWFTRPGKRERdeATKALQTVGM-LDYAQRSISQLSGGQQQRVFLA 153
Cdd:COG1123 343 RVQMVFQdpYSSLN---PrMTVGDIIAEP-LRLHGLLSRAERRER--VAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 154 RALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDgRIVEDGPTEEVFANP 496
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-239 |
4.21e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 148.73 E-value: 4.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIAY 81
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV--RLNGRPLAAW---SPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwDYPITVFEVVLMGtyrRLGWFtRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL----- 156
Cdd:COG4559 80 LPQHSSL--AFPFTVEEVVALG---RAPHG-SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 157 -VENQDVYI-LDEPFKGID-KTTEAVLvKIMKDMQAAGKTLLIVHHNLQtLEA-YFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:COG4559 154 pVDGGPRWLfLDEPTSALDlAHQHAVL-RLARQLARRGGGVVAVLHDLN-LAAqYADRILLLHQgRLVAQGTPEEVLTDE 231
|
....*...
gi 2786564536 232 ILDETYSY 239
Cdd:COG4559 232 LLERVYGA 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-216 |
3.73e-42 |
|
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: 141.00 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyggvKTNSIYNHIAY 81
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI--KVLGKDIKK----EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWDYpiTVFEVVlmgtyrrlgwftrpgkrerdeatkalqtvgmldyaqrsisQLSGGQQQRVFLARALVENQD 161
Cdd:cd03230 78 LPEEPSLYENL--TVRENL----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-212 |
7.33e-42 |
|
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: 142.44 E-value: 7.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHIA 80
Cdd:TIGR02315 5 ENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSI--LLEGTDITKLRGKKLRKLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwDY----PITVFEVVLMGtyrRLG-------WFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQR 149
Cdd:TIGR02315 83 MIFQ------HYnlieRLTVLENVLHG---RLGykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVL 212
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIV 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-227 |
3.28e-41 |
|
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: 140.76 E-value: 3.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeltldakTVSAYGGVKTNSIY-NHIA 80
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-------LIDGEDVRKEPREArRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdWDYpITVFEVVlmgtyRRLGWFTRPGKRERDEATKAL-QTVGMLDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:COG4555 78 VLPDERGL-YDR-LTVRENI-----RYFAELYGLFDEELKKRIEELiELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKgKVVAQGSLDEL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-222 |
5.15e-41 |
|
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: 139.58 E-value: 5.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNsiynhIAY 81
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI--LIDGRDVTGVPPERRN-----IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVLMGTYRRLgwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:cd03259 77 VFQDYAL---FPhLTVAENIAFGLKLRG----VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQtlEAYF--DQVLCVNR-RLVGMG 222
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQE--EALAlaDRIAVMNEgRIVQVG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-222 |
9.76e-40 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 137.45 E-value: 9.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGgvkTNSIYNHIAY 81
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV--FLGDKPISMLS---SRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWDypITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:PRK11231 81 LPQHHLTPEG--ITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQ-VLCVNRRLVGMG 222
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHlVVLANGHVMAQG 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
1.39e-39 |
|
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: 143.36 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDD-TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIA 80
Cdd:COG4988 340 EDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI--LINGVDLSDL---DPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYPITVFEVVLMGtyrrlgwftRPGkRERDEATKALQTVGMLDYAQR-------SI----SQLSGGQQQR 149
Cdd:COG4988 415 WVPQNPYL---FAGTIRENLRLG---------RPD-ASDEELEAALEAAGLDEFVAAlpdgldtPLgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEAYfDQVLCVNR-RLVGMG 222
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQA-DRILVLDDgRIVEQG 553
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
2.22e-39 |
|
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: 135.31 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDD----TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYN 77
Cdd:cd03255 4 KNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV--RVDGTDISKLSEKELAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 -HIAYVPQtsavdwDY---P-ITVFEVVLMGtyrrLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFL 152
Cdd:cd03255 82 rHIGFVFQ------SFnllPdLTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 153 ARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQA-AGKTLLIVHHNLQtLEAYFDQVL 212
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPE-LAEYADRII 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
3.55e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.56 E-value: 3.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSiynHIA 80
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI--YLDGKPLSAMPPPEWRR---QVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdWDYpiTVfevvlmGTYRRLGWFTRPGKRERDEATKALQTVGM-LDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:COG4619 78 YVPQEPAL-WGG--TV------RDNLPFPFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 160 QDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVN 215
Cdd:COG4619 149 PDVLLLDEPTSALDpENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLE 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-239 |
1.70e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 134.13 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIAY 81
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV--RLNGRPLADW---SPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwDYPITVFEVVLMGtyrRLGWfTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE--N 159
Cdd:PRK13548 81 LPQHSSL--SFPFTVEEVVAMG---RAPH-GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 160 QD----VYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSPIL 233
Cdd:PRK13548 155 PDgpprWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAEVLTPETL 234
|
....*.
gi 2786564536 234 DETYSY 239
Cdd:PRK13548 235 RRVYGA 240
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-212 |
2.32e-38 |
|
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: 131.35 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDT--VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNH 78
Cdd:cd03228 3 FKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI--LIDGVDLRDL---DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVdwdYPITVFEVVlmgtyrrlgwftrpgkrerdeatkalqtvgmldyaqrsisqLSGGQQQRVFLARALVE 158
Cdd:cd03228 78 IAYVPQDPFL---FSGTIRENI-----------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEaYFDQVL 212
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR-DADRII 165
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-212 |
3.21e-38 |
|
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: 130.44 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAYGGVKtnsiyNHIA 80
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR-----RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwdypitvfevvlmgtyrrlgwftrpgkrerdeatkalqtvgmldyaqrsisqLSGGQQQRVFLARALVENQ 160
Cdd:cd00267 77 YVPQ---------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVL 212
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVI 151
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-212 |
5.00e-38 |
|
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: 132.24 E-value: 5.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDD----TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIYN 77
Cdd:cd03257 5 KNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF--DGKDLLKLSRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQ--TSAVDwdyPI-TVFEVvLMGTYRRLGwftRPGKRERDEATKALQTVGML---DYAQRSISQLSGGQQQRVF 151
Cdd:cd03257 83 EIQMVFQdpMSSLN---PRmTIGEQ-IAEPLRIHG---KLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 152 LARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVL 212
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVA 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-212 |
5.77e-38 |
|
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: 139.13 E-value: 5.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTV--VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGvktNSIYNH 78
Cdd:COG4987 336 LEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI--TLGGVDLRDLDE---DDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVdwdypitvfevvLMGTYR---RLGwftRPGKRErDEATKALQTVGMLDYAQRSI-----------SQLSG 144
Cdd:COG4987 411 IAVVPQRPHL------------FDTTLRenlRLA---RPDATD-EELWAALERVGLGDWLAALPdgldtwlgeggRRLSG 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 145 GQQQRVFLARALVENQDVYILDEPFKGIDKTTEAvlvKIMKDM--QAAGKTLLIVHHNLQTLEAyFDQVL 212
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQ---ALLADLleALAGRTVLLITHRLAGLER-MDRIL 540
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
14-169 |
2.26e-37 |
|
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: 128.15 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSiynHIAYVPQTSAVdwDYP 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI--LLDGQDLTDDERKSLRK---EIGYVFQDPQL--FPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVFEVVLMGTYrrlgwFTRPGKRERD-EATKALQTVGMLDYAQRSI----SQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:pfam00005 74 LTVRENLRLGLL-----LKGLSKREKDaRAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
.
gi 2786564536 169 F 169
Cdd:pfam00005 149 T 149
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
4.15e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.59 E-value: 4.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY----DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGvktnsiy 76
Cdd:COG1116 10 LRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV--LVDGKPVTGPGP------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 nHIAYVPQTSAVdwdYP-ITVFEVVLMGtyRRLGWFTRPGKRERdeATKALQTVGMLDYAQRSISQLSGGQQQRVFLARA 155
Cdd:COG1116 81 -DRGVVFQEPAL---LPwLTVLDNVALG--LELRGVPKAERRER--ARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 156 LVENQDVYILDEPFKGIDKTT----EAVLVKImkdMQAAGKTLLIVHHNLQtlEAYF--DQVL 212
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTrerlQDELLRL---WQETGKTVLFVTHDVD--EAVFlaDRVV 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-231 |
4.77e-37 |
|
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: 129.93 E-value: 4.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEltLDAKTVSAYGGVKTNSIYNHIA 80
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL--IDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypITVFEVVLMGTYRRlgwFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:cd03261 81 MLFQSGALFDS--LTVFENVAFPLREH---TRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGSP 231
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEGTPEELRASD 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-231 |
1.25e-36 |
|
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: 128.71 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSaygGVKTNSIYNH-IAY 81
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF--DGEDIT---GLPPHEIARLgIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVLMGTYRRLG---WFTRPGKRE---RDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLAR 154
Cdd:cd03219 80 TFQIPRL---FPeLTVLENVMVAAQARTGsglLLARARREEreaRERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 155 ALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPDEVRNNP 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
1.36e-36 |
|
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: 134.65 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP---LVEGTIELT---LDAKTVSAYGgvktns 74
Cdd:COG1123 9 DLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDgrdLLELSEALRG------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 iyNHIAYVPQTSAVDWDyPITVFEVVLMGtyrrLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLAR 154
Cdd:COG1123 83 --RRIGMVFQDPMTQLN-PVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 155 ALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILAAP 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-237 |
5.22e-36 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 131.12 E-value: 5.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL------TLDAKTVSayggvktnsiyN 77
Cdd:PRK09536 9 LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddveALSARAAS-----------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQTSAVDWDYpiTVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:PRK09536 78 RVASVPQDTSLSFEF--DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 158 ENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQ-VLCVNRRLVGMGPVRDIVGSPILDET 236
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDElVLLADGRVRAAGPPADVLTADTLRAA 235
|
.
gi 2786564536 237 Y 237
Cdd:PRK09536 236 F 236
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-231 |
2.20e-35 |
|
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: 126.07 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY----DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVsayGGVKTNSIYN 77
Cdd:COG1124 5 RNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEV--TFDGRPV---TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQ--TSAVDwdyP-ITVFEVvLMGTYRRLGwftRPGKRERdeATKALQTVGM-LDYAQRSISQLSGGQQQRVFLA 153
Cdd:COG1124 80 RVQMVFQdpYASLH---PrHTVDRI-LAEPLRIHG---LPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 154 RALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNgRIVEELTVADLLAGP 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
3.40e-35 |
|
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: 124.32 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAyggvktnSIYNHIAY 81
Cdd:cd03269 4 ENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF--DGKPLDI-------AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVL-MGTYRRLGwftrpgKRE-RDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:cd03269 75 LPEERGL---YPkMKVIDQLVyLAQLKGLK------KEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-201 |
5.58e-35 |
|
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: 124.08 E-value: 5.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEltLDAKTVSaygGVKTNSIYNH-IAY 81
Cdd:cd03224 5 NLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR--FDGRDIT---GLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVLMGTYRRLGwftRPGKRERDEatkalqtvgMLDY--------AQRSiSQLSGGQQQRVFL 152
Cdd:cd03224 80 VPEGRRI---FPeLTVEENLLLGAYARRR---AKRKARLER---------VYELfprlkerrKQLA-GTLSGGEQQMLAI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2786564536 153 ARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNL 201
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNA 192
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-227 |
8.30e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.14 E-value: 8.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSaygGVKTNsiYNHIAY 81
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI--LLDGRDVT---GLPPE--KRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQtsavdwDYPI----TVFEVVLMG-TYRRLGwftrpgKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARA 155
Cdd:COG3842 82 VFQ------DYALfphlTVAENVAFGlRMRGVP------KAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 156 LVENQDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQtlEAYF--DQVLCVNR-RLVGMGPVRDI 227
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDaKLREEMREELRRLQRELGITFIYVTHDQE--EALAlaDRIAVMNDgRIEQVGTPEEI 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-216 |
1.44e-34 |
|
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: 122.69 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGtMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGgvktNSIYNHIAYV 82
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI--DGQDVLKQP----QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 83 PQTSAVdwdYP-ITVFEVVlmgtyRRLGWFTR-PGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:cd03264 78 PQEFGV---YPnFTVREFL-----DYIAWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDmQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-223 |
2.09e-34 |
|
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: 129.95 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL-TLDAKTVSayggvkTNSIYN 77
Cdd:COG2274 476 LENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdGIDLRQID------PASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQtsavdwdypitvfEVVLM-GTYR---RLGwftRPGkRERDEATKALQTVGMLDYAQR-------SI----SQL 142
Cdd:COG2274 550 QIGVVLQ-------------DVFLFsGTIReniTLG---DPD-ATDEEIIEAARLAGLHDFIEAlpmgydtVVgeggSNL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 143 SGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLeAYFDQVLCVNR-RLVGM 221
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTI-RLADRIIVLDKgRIVED 690
|
..
gi 2786564536 222 GP 223
Cdd:COG2274 691 GT 692
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-231 |
2.76e-34 |
|
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: 122.78 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIYNHIAYV 82
Cdd:COG1127 10 NLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV--DGQDITGLSEKELYELRRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 83 PQTSAVdWDYpITVFEVVLMGTYRrlgwFTRPGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:COG1127 88 FQGGAL-FDS-LTVFENVAFPLRE----HTDLSEAEIRElVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGSP 231
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLaDGKIIAEGTPEELLASD 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-212 |
3.00e-34 |
|
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: 128.17 E-value: 3.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDT-VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGGVKTNSI---- 75
Cdd:TIGR02857 324 FSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV----------NGVPLADAdads 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 -YNHIAYVPQTSAVdwdYPITVFEVVLMGtyrrlgwftRPGKRErDEATKALQTVGMLDYAQ-----------RSISQLS 143
Cdd:TIGR02857 394 wRDQIAWVPQHPFL---FAGTIAENIRLA---------RPDASD-AEIREALERAGLDEFVAalpqgldtpigEGGAGLS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 144 GGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEAYfDQVL 212
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALA-DRIV 527
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-217 |
7.98e-34 |
|
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: 121.04 E-value: 7.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDD----TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEltldaktvsaYGGVKTNSIYNH 78
Cdd:cd03293 5 NVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL----------VDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAV-DWdypITVFEVVLMGtYRRLGWftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:cd03293 75 RGYVFQQDALlPW---LTVLDNVALG-LELQGV---PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 158 ENQDVYILDEPFKGIDKTT----EAVLVKIMKDMqaaGKTLLIVHHNLQtlEAYF--DQVLCVNRR 217
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTreqlQEELLDIWRET---GKTVLLVTHDID--EAVFlaDRVVVLSAR 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
2-237 |
9.56e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 121.73 E-value: 9.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIAY 81
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV--LVDGLDVATT---PSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwDYPITVFEVVLMGTY---RrlGwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:COG4604 80 LRQENHI--NSRLTVRELVAFGRFpysK--G---RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 159 NQDVYILDEPFKGID-KTTeavlVKIMKDMQAA----GKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGSPI 232
Cdd:COG4604 153 DTDYVLLDEPLNNLDmKHS----VQMMKLLRRLadelGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEIITPEV 228
|
....*
gi 2786564536 233 LDETY 237
Cdd:COG4604 229 LSDIY 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-227 |
1.50e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyggvktnSIYNHIAY 81
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV--LWDGEPLDP-------EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVLmgtyrrlgWFTR----PGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:COG4152 76 LPEERGL---YPkMKVGEQLV--------YLARlkglSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 157 VENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKgRKVLSGSVDEI 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-212 |
2.24e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.15 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDD----TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYN- 77
Cdd:COG1136 9 NLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV--LIDGQDISSLSERELARLRRr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQtsavdwDY---P-ITVFE-VVLMGTYRRlgwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFL 152
Cdd:COG1136 87 HIGFVFQ------FFnllPeLTALEnVALPLLLAG-----VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 153 ARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQtLEAYFDQVL 212
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPE-LAARADRVI 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
2.41e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.77 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGGVKTNSI-YNH 78
Cdd:COG2884 4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV----------NGQDLSRLkRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAY-------VPQtsavdwDYPI----TVFEVVLMGTyRRLGwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQ 147
Cdd:COG2884 74 IPYlrrrigvVFQ------DFRLlpdrTVYENVALPL-RVTG---KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 148 QRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVL-CVNRRLV 219
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLeLEDGRLV 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-212 |
2.74e-32 |
|
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: 116.59 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTnsiynhIAY 81
Cdd:cd03226 4 NISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL--NGKPIKAKERRKS------IGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSavdwDYPI---TVFEVVLMGTyrrlgwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:cd03226 76 VMQDV----DYQLftdSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVL 212
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-199 |
4.55e-32 |
|
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: 116.48 E-value: 4.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyGGVKTNSIYNHIA 80
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI--IIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYP-ITVFEVVLMGTYRRLGwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:cd03262 80 MVFQQFNL---FPhLTVLENITLAPIKVKG---MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 160 QDVYILDEPFKGID-KTTEAVLvKIMKDMQAAGKTLLIVHH 199
Cdd:cd03262 154 PKVMLFDEPTSALDpELVGEVL-DVMKDLAEEGMTMVVVTH 193
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-212 |
6.62e-32 |
|
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: 115.64 E-value: 6.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTV-----VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeltldaktvsayggvktnSI 75
Cdd:cd03250 3 VEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV------------------SV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 YNHIAYVPQTSavdWDYPITVFEVVLmgtyrrlgwFTRPGKRER-DEATKA-------------LQT-VGmldyaQRSIS 140
Cdd:cd03250 65 PGSIAYVSQEP---WIQNGTIRENIL---------FGKPFDEERyEKVIKAcalepdleilpdgDLTeIG-----EKGIN 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 141 qLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVK--IMKDMqAAGKTLLIVHHNLQTLEaYFDQVL 212
Cdd:cd03250 128 -LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL-LNNKTRILVTHQLQLLP-HADQIV 198
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
8.20e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.81 E-value: 8.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYD-DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIA 80
Cdd:COG1132 343 ENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI--LIDGVDIRDL---TLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwdypitvfEVVLM-GTYR---RLGwftRPGkRERDEATKALQTVGMLDYAQR------SI-----SQLSGG 145
Cdd:COG1132 418 VVPQ-------------DTFLFsGTIReniRYG---RPD-ATDEEVEEAAKAAQAHEFIEAlpdgydTVvgergVNLSGG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEAyFDQVLCVNR-RLVGMGP 223
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDgRIVEQGT 557
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-237 |
1.13e-31 |
|
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: 115.85 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSaygGVKTNSIYNH-IA 80
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI--RFDGEDIT---GLPPHRIARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYP-ITVFEVVLMGTYRRlgwftrpgkRERDEATKALQTVgmLDY--------AQRSiSQLSGGQQQRVF 151
Cdd:COG0410 82 YVPEGRRI---FPsLTVEENLLLGAYAR---------RDRAEVRADLERV--YELfprlkerrRQRA-GTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 152 LARALVENQDVYILDEPFKGIdktteA-VLVK----IMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVR 225
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL-----ApLIVEeifeIIRRLNREGVTILLVEQNARFALEIADRAYVLERgRIVLEGTAA 221
|
250
....*....|..
gi 2786564536 226 DIVGSPILDETY 237
Cdd:COG0410 222 ELLADPEVREAY 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-215 |
2.39e-31 |
|
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: 113.44 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGvKTNSIYNHIA 80
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI--DGEDLTDLED-ELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYP-ITVFEVVLMGtyrrlgwftrpgkrerdeatkalqtvgmldyaqrsisqLSGGQQQRVFLARALVEN 159
Cdd:cd03229 80 MVFQDFAL---FPhLTVLENIALG--------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDMQA-AGKTLLIVHHNLQTLEAYFDQVLCVN 215
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-212 |
6.42e-31 |
|
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: 112.31 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDT--VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGgvkTNSIYNHIAY 81
Cdd:cd03246 6 VSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--RLDGADISQWD---PNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQtsavdwdypitvfEVVLMgtyrrlgwftrPGkrerdeatkalqtvgmldyaqrSISQ--LSGGQQQRVFLARALVEN 159
Cdd:cd03246 81 LPQ-------------DDELF-----------SG----------------------SIAEniLSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAyFDQVL 212
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRIL 166
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
7.74e-31 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 114.06 E-value: 7.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKtvsayggvktnsiynhIA 80
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR----------------IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDYPITVfevvlmGTYRRLgwftRPGKRERD--EATKALQTVGMLDYaqrSISQLSGGQQQRVFLARALVE 158
Cdd:PRK09544 71 YVPQKLYLDTTLPLTV------NRFLRL----RPGTKKEDilPALKRVQAGHLIDA---PMQKLSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-231 |
8.60e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.19 E-value: 8.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYD----DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYG---GVktns 74
Cdd:COG4525 7 RHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI--TLDGVPVTGPGadrGV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 IYNHIAYVPqtsavdWdypITVFEVVLMGTyrRLgwfTRPGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLA 153
Cdd:COG4525 81 VFQKDALLP------W---LNVLDNVAFGL--RL---RGVPKAERRArAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 154 RALVENQDVYILDEPFKGIDK-TTEAVLVKIMKDMQAAGKTLLIVHHNLQtlEAYF---DQVLC--------------VN 215
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDAlTREQMQELLLDVWQRTGKGVFLITHSVE--EALFlatRLVVMspgpgriverleldFS 224
|
250
....*....|....*.
gi 2786564536 216 RRLVGMGPVRDIVGSP 231
Cdd:COG4525 225 RRFLAGEDARAIKSDP 240
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
1-201 |
1.03e-30 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 112.71 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIY-NHI 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYL--NGQETPPLNSKKASKFRrEKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSA-VDWDypiTVFEVVLMGtyrrLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:TIGR03608 79 GYLFQNFAlIENE---TVEENLDLG----LKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNL 201
Cdd:TIGR03608 152 PPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-227 |
1.25e-30 |
|
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: 113.04 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKA---MLGLVPL--VEGTIEltLDAKTVSAYgGVKTNSIYNH 78
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPGapDEGEVL--LDGKDIYDL-DVDVLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVdwdYPITVFEVVLMG-TYRRLgwftRPGKRERDEATKALQTVGMLDYAQR--SISQLSGGQQQRVFLARA 155
Cdd:cd03260 83 VGMVFQKPNP---FPGSIYDNVAYGlRLHGI----KLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 156 LVENQDVYILDEPFKGIDKTT----EAVLVKIMKDMqaagkTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPIStakiEELIAELKKEY-----TIVIVTHNMQQAARVADRTAFLLNgRLVEFGPTEQI 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-237 |
1.58e-30 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.93 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGgvkTNSIYNHIAY 81
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV--WLDGEHIQHYA---SKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWDypITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:PRK10253 86 LAQNATTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSPILDETY 237
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPKEIVTAELIERIY 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-232 |
2.89e-30 |
|
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: 112.33 E-value: 2.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVK--TNSIYNHIA 80
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI--LLDGKDITNLPPHKrpVNTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwdypITVFEVVLMGTYRRlgwfTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:cd03300 83 LFPH---------LTVFENIAFGLRLK----KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 161 DVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSPI 232
Cdd:cd03300 150 KVLLLDEPLGALDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKgKIQQIGTPEEIYEEPA 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-173 |
3.01e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGGVKTNSIY----N 77
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI----------GGRDVTDLPpkdrN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 hIAYVPQTSAVdwdYP-ITVFEVVLMG-TYRRLGwftrpgKRERDEA-TKALQTVGMLDYAQRSISQLSGGQQQRVFLAR 154
Cdd:COG3839 77 -IAMVFQSYAL---YPhMTVYENIAFPlKLRKVP------KAEIDRRvREAAELLGLEDLLDRKPKQLSGGQRQRVALGR 146
|
170
....*....|....*....
gi 2786564536 155 ALVENQDVYILDEPFKGID 173
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLD 165
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-206 |
3.11e-30 |
|
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: 111.30 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL--TLDAKTVSAYGgvktnsiyNHIAY 81
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngTPLAEQRDEPH--------ENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWDypITVFEvvlmgtyrRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:TIGR01189 78 LGHLPGLKPE--LSALE--------NLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKD-MQAAGKTLLIVHHNLQTLEA 206
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLVEA 193
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-199 |
3.63e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 112.01 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyGGVKTNSIYNHIA 80
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI--TVDGEDLTD-SKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwDY---P-ITVFEVVLMGTYRRLGWftrpGKRE-RDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARA 155
Cdd:COG1126 81 MVFQ------QFnlfPhLTVLENVTLAPIKVKKM----SKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 156 LVENQDVYILDEPfkgidktTEA--------VLvKIMKDMQAAGKTLLIVHH 199
Cdd:COG1126 151 LAMEPKVMLFDEP-------TSAldpelvgeVL-DVMRDLAKEGMTMVVVTH 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-231 |
2.12e-29 |
|
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: 110.51 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSaygGVKTNSIYNH-IAY 81
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRI--LFDGRDIT---GLPPHRIARLgIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVLMGTYRRLG--------WFTRPGKRE---RDEATKALQTVGMLDYAQRSISQLSGGQQQR 149
Cdd:COG0411 84 TFQNPRL---FPeLTVLENVLVAAHARLGrgllaallRLPRARREEreaRERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTPAEV 240
|
....
gi 2786564536 228 VGSP 231
Cdd:COG0411 241 RADP 244
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-231 |
5.15e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNsiynHIAY 81
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL--NGRDLFTNLPPRER----RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQtsavdwDY---P-ITVFEVVLMGTYRRlgwftRPGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:COG1118 80 VFQ------HYalfPhMTVAENIAFGLRVR-----PPSKAEIRArVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 157 VENQDVYILDEPFKGID----KTTEAVLVKIMKDMqaaGKTLLIVHHNLqtLEAY--FDQVLCVNR-RLVGMGPVRDIVG 229
Cdd:COG1118 149 AVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQ--EEALelADRVVVMNQgRIEQVGTPDEVYD 223
|
..
gi 2786564536 230 SP 231
Cdd:COG1118 224 RP 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-215 |
1.55e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 19 FQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYG----GVKT----NSIYNHIayvpqtsavdw 90
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI--LWNGQDLTALPpaerPVSMlfqeNNLFPHL----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dypiTVFEVVLMGTYRRLgwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:COG3840 87 ----TVAQNIGLGLRPGL----KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVN 215
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVA 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-222 |
3.47e-28 |
|
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: 106.30 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeltldakTVSAYGGVK-TNSIYNHIAY 81
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA-------TVAGHDVVRePREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWDypITVFEVVLMgtYRRLgwFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:cd03265 78 VFQDLSVDDE--LTGWENLYI--HARL--YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMG 222
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-231 |
5.35e-28 |
|
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: 106.13 E-value: 5.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDT----VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIY 76
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV--DGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAYVPQTSAVDWDYpiTVFEVVlmgTY--RRLGWftrpGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLA 153
Cdd:cd03258 82 RRIGMIFQHFNLLSSR--TVFENV---ALplEIAGV----PKAEIEErVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 154 RALVENQDVYILDEPFKGID-KTTEAVLvKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGS 230
Cdd:cd03258 153 RALANNPKVLLCDEATSALDpETTQSIL-ALLRDINRElGLTIVLITHEMEVVKRICDRVAVMeKGEVVEEGTVEEVFAN 231
|
.
gi 2786564536 231 P 231
Cdd:cd03258 232 P 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-216 |
6.33e-28 |
|
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: 105.91 E-value: 6.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDD----TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT-LDakTVSAYGGVKTNsiy 76
Cdd:cd03266 5 DALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgFD--VVKEPAEARRR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 nhIAYVPQTSAVdwdYP-ITVFEVvlmgtyrrLGWFTRPGKRERDEATKAL----QTVGMLDYAQRSISQLSGGQQQRVF 151
Cdd:cd03266 80 --LGFVSDSTGL---YDrLTAREN--------LEYFAGLYGLKGDELTARLeelaDRLGMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 152 LARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-219 |
1.45e-27 |
|
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: 104.80 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIYNHIAYVPQTSAVD 89
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV--NGQDVSDLRGRAIPYLRRKIGVVFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 WDypITVFEVVLMGtyrrLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPF 169
Cdd:cd03292 91 PD--RNVYENVAFA----LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2786564536 170 KGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNRRLV 219
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-201 |
1.51e-27 |
|
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: 106.19 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 11 TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL------TLDAKTVSAYGGVKTNSIYNHIAYVPQ 84
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdgqdiaAMSRKELRELRRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 TSAVDwdypITVFEVVLMGTyrrlgwftrpGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVY 163
Cdd:cd03294 117 RTVLE----NVAFGLEVQGV----------PRAEREErAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2786564536 164 ILDEPFKGIDKTteavlvkIMKDMQ--------AAGKTLLIVHHNL 201
Cdd:cd03294 183 LMDEAFSALDPL-------IRREMQdellrlqaELQKTIVFITHDL 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-231 |
2.48e-27 |
|
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: 104.69 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKtnsIYNHIAY 81
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI--FIDGEDIREQDPVE---LRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFE-VVLMGTYrrLGWftrPGKRERDEATKALQTVGM--LDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:cd03295 80 VIQQIGL---FPhMTVEEnIALVPKL--LKW---PKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 158 ENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQtlEAY-FDQVLCV--NRRLVGMGPVRDIVGSP 231
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDID--EAFrLADRIAImkNGEIVQVGTPDEILRSP 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-222 |
2.65e-27 |
|
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: 104.23 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSaygGVKTNSIYNHIAYVPQTsavDWDY 92
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI--LIDGIDIR---DISRKSLRSMIGVVLQD---TFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PITVFEVVLMGtyrrlgwftRPGKRERDEAtKALQTVGMLDYAQRSI-----------SQLSGGQQQRVFLARALVENQD 161
Cdd:cd03254 90 SGTIMENIRLG---------RPNATDEEVI-EAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 162 VYILDEPFKGIDKTTEAV----LVKIMKdmqaaGKTLLIVHHNLQTLEaYFDQVLCVNR-RLVGMG 222
Cdd:cd03254 160 ILILDEATSNIDTETEKLiqeaLEKLMK-----GRTSIIIAHRLSTIK-NADKILVLDDgKIIEEG 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-199 |
2.79e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 108.99 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDT-VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGvktNSIYNHIAY 81
Cdd:TIGR02868 339 DLSAGYPGApPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV--TLDGVPVSSLDQ---DEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYPITVFEVVLMGtyrrlgwftRPGKRErDEATKALQTVGMLDYAQRSI-----------SQLSGGQQQRV 150
Cdd:TIGR02868 414 CAQDAHL---FDTTVRENLRLA---------RPDATD-EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2786564536 151 FLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHH 199
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
5.26e-27 |
|
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: 102.39 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYD--DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG-LVPLvEGTIelTLDAKTVSAYGgvktNSIYNH 78
Cdd:cd03247 4 NNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQ-QGEI--TLDGVPVSDLE----KALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTsavdwdypITVFevvlmgtyrrlgwftrpgkrerdeATKALQTVGmldyaqrsiSQLSGGQQQRVFLARALVE 158
Cdd:cd03247 77 ISVLNQR--------PYLF------------------------DTTLRNNLG---------RRFSGGERQRLALARILLQ 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEaYFDQVL 212
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIE-HMDKIL 167
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-211 |
5.88e-27 |
|
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: 103.07 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVsayggVKTNSIYNHIAy 81
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI--TFDGKSY-----QKNIEALRRIG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 vpqtSAVD--WDYP-ITVFEVvlMGTYRRLgwftrPGKRERdEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:cd03268 76 ----ALIEapGFYPnLTAREN--LRLLARL-----LGIRKK-RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-227 |
1.05e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL---------TLDAKTVsaygGVK 71
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrsPRDAQAA----GIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 72 TnsIYNHIAYVPQtsavdwdypITVFEVVLMGTYRRLGWFTRPgKRERDEATKALQTVGM-LDyAQRSISQLSGGQQQRV 150
Cdd:COG1129 83 I--IHQELNLVPN---------LSVAENIFLGREPRRGGLIDW-RAMRRRARELLARLGLdID-PDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 151 FLARALVENQDVYILDEPfkgidkT---TEA---VLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVlCVNR--RLVGMG 222
Cdd:COG1129 150 EIARALSRDARVLILDEP------TaslTEReveRLFRIIRRLKAQGVAIIYISHRLDEVFEIADRV-TVLRdgRLVGTG 222
|
....*
gi 2786564536 223 PVRDI 227
Cdd:COG1129 223 PVAEL 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-216 |
1.60e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.17 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLV---PLVEGTIELTldAKTVSAYGGVKTN--SIYNH 78
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELL--GRTVQREGRLARDirKSRAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYV-PQTSAVDwdyPITVFEVVLMGT------YRR-LGWFTRpgkRERDEATKALQTVGMLDYAQRSISQLSGGQQQRV 150
Cdd:PRK09984 88 TGYIfQQFNLVN---RLSVLENVLIGAlgstpfWRTcFSWFTR---EQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 151 FLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-228 |
1.71e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 107.26 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL-TLDAKTVSAYggvktnSIYNHIA 80
Cdd:TIGR03375 469 VSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLdGVDIRQIDPA------DLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQtsavdwdypitvfEVVLM-GTYRR---LGwftRPGKRERdEATKALQTVGMLDYAQRS-------ISQ----LSGG 145
Cdd:TIGR03375 543 YVPQ-------------DPRLFyGTLRDniaLG---APYADDE-EILRAAELAGVTEFVRRHpdgldmqIGErgrsLSGG 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEaYFDQVLCVNR-RLVGMGPv 224
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLD-LVDRIIVMDNgRIVADGP- 682
|
....
gi 2786564536 225 RDIV 228
Cdd:TIGR03375 683 KDQV 686
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-168 |
2.19e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGlvplvegtiELTLDAKTVSAYGGVKtnsiynhIA 80
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG---------ELEPDSGEVSIPKGLR-------IG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDYpiTVFEVVLMG-------------TYRRLGWFTRPGKR---------ERD------EATKALQTVGM- 131
Cdd:COG0488 65 YLPQEPPLDDDL--TVLDTVLDGdaelraleaeleeLEAKLAEPDEDLERlaelqeefeALGgweaeaRAEEILSGLGFp 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 2786564536 132 LDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:COG0488 143 EEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-227 |
2.77e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 102.91 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYD-----DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIY 76
Cdd:TIGR04521 4 KNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTV--TIDGRDITAKKKKKLKDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAYVPQtsavdwdYP------ITVFEVVLMGTyRRLGWftrPGKRERDEATKALQTVGM-LDYAQRSISQLSGGQQQR 149
Cdd:TIGR04521 82 KKVGLVFQ-------FPehqlfeETVYKDIAFGP-KNLGL---SEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQ-AAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGTPREV 230
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-239 |
3.50e-26 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 101.99 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKA---MLGLVPLVEGTIELTLDAKTVSAYGgVKTNSIYNHI 79
Cdd:TIGR00972 6 NLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSlnrMNDLVPGVRIEGKVLFDGQDIYDKK-IDVVELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAvdwDYPITVFEVVLMGtYRRLGwfTRPGKRERDEATKALQTVGML----DYAQRSISQLSGGQQQRVFLARA 155
Cdd:TIGR00972 85 GMVFQKPN---PFPMSIYDNIAYG-PRLHG--IKDKKELDEIVEESLKKAALWdevkDRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 156 LVENQDVYILDEPFKGIDKTT----EAVLVKIMKDMqaagkTLLIVHHNLQTLEAYFDQV-LCVNRRLVGMGPVRDIVGS 230
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIAtgkiEELIQELKKKY-----TIVIVTHNMQQAARISDRTaFFYDGELVEYGPTEQIFTN 233
|
....*....
gi 2786564536 231 PILDETYSY 239
Cdd:TIGR00972 234 PKEKRTEDY 242
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-208 |
4.47e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.70 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYG---GVktnsIYN 77
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI--TLDGKPVEGPGaerGV----VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQTSAVDwdypITVFEVVLMGTyrrlgwftrpGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:PRK11248 78 NEGLLPWRNVQD----NVAFGLQLAGV----------EKMQRLEiAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARAL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 157 VENQDVYILDEPFKGIDK-TTEAVLVKIMKDMQAAGKTLLIVHHNLQtlEAYF 208
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAfTREQMQTLLLKLWQETGKQVLLITHDIE--EAVF 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-231 |
5.00e-26 |
|
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: 101.26 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNsiynhIAYVPQTSAVdwdY 92
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI--LLNGKDITNLPPEKRD-----ISYVPQNYAL---F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 P-ITVFEVVLMGTYRRlgwftRPGKRERDEatKALQTVGMLDYAQ---RSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:cd03299 84 PhMTVYKNIAYGLKKR-----KVDKKEIER--KVLEIAEMLGIDHllnRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 169 FKGIDKTTEAVLVKIMKDMQ-AAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNgKLIQVGKPEEVFKKP 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-206 |
7.34e-26 |
|
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: 100.27 E-value: 7.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeltldakTVSAYGGVKT-NSIYN 77
Cdd:cd03263 3 IRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-------YINGYSIRTDrKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 78 HIAYVPQTSAVDWDypITVFEVVLMgtYRRL-GwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:cd03263 76 SLGYCPQFDALFDE--LTVREHLRF--YARLkG---LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2786564536 157 VENQDVYILDEPFKGIDKTTEAVLVKIMKDMQaAGKTLLIVHHNLQTLEA 206
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEA 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
16-214 |
8.73e-26 |
|
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: 100.06 E-value: 8.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 16 DVFFQIEQGTmTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTlDAKTVSAYGGVKTNSIYNHIAYVPQTSAVdwdYP-I 94
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-GTVLFDSRKKINLPPQQRKIGLVFQQYAL---FPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 95 TVFEVVLMGTYRRlgwftRPGKReRDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDK 174
Cdd:cd03297 91 NVRENLAFGLKRK-----RNRED-RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 175 TTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCV 214
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-211 |
1.21e-25 |
|
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: 98.27 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGgvktnsiynhia 80
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI--LVDGKEVSFAS------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 yvPQTSavdwdypitvfevvlmgtyRRLGwftrpgkrerdeatkalqtVGMldyaqrsISQLSGGQQQRVFLARALVENQ 160
Cdd:cd03216 69 --PRDA-------------------RRAG-------------------IAM-------VYQLSVGERQMVEIARALARNA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRV 152
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-199 |
1.66e-25 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 101.32 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDD-TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKaML-GLVPLVEGTIelTLDAKTVSAYGGVKtnsIYNHIA 80
Cdd:COG1125 6 NVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLR-MInRLIEPTSGRI--LIDGEDIRDLDPVE---LRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYP-ITVFE---VVLmgtyRRLGWftrPGKRERDEATKALQTVGmLD---YAQRSISQLSGGQQQRVFLA 153
Cdd:COG1125 80 YVIQQIGL---FPhMTVAEniaTVP----RLLGW---DKERIRARVDELLELVG-LDpeeYRDRYPHELSGGQQQRVGVA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 154 RALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHH 199
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRElGKTIVFVTH 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-206 |
2.08e-25 |
|
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: 98.72 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVsaygGVKTNSIYNHIAYVP 83
Cdd:cd03231 6 LTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG--RVLLNGGPL----DFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVDwdypiTVFEVVlmgtyRRLGWFTRPGKRERDEatKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVY 163
Cdd:cd03231 80 HAPGIK-----TTLSVL-----ENLRFWHADHSDEQVE--EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2786564536 164 ILDEPFKGIDKTTEAVLVKIMKD-MQAAGKTLLIVHHNLQTLEA 206
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGhCARGGMVVLTTHQDLGLSEA 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-168 |
3.08e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldAKTVsayggvktnsiynHIA 80
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---GETV-------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQ-TSAVDWDypITVFEVVlmgtyRRLgwftRPGKRErdeaTKALQTVG-ML---DYAQRSISQLSGGQQQRVFLARA 155
Cdd:COG0488 382 YFDQhQEELDPD--KTVLDEL-----RDG----APGGTE----QEVRGYLGrFLfsgDDAFKPVGVLSGGEKARLALAKL 446
|
170
....*....|...
gi 2786564536 156 LVENQDVYILDEP 168
Cdd:COG0488 447 LLSPPNVLLLDEP 459
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-201 |
5.03e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 98.37 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVS---AYGGVKtnsiyNH 78
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRL--DGEDITklpPHERAR-----AG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVdwdYP-ITVFEVVLMGtyrrlgWFTRPG-KRERDEATKALQTVgMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:TIGR03410 77 IAYVPQGREI---FPrLTVEENLLTG------LAALPRrSRKIPDEIYELFPV-LKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 157 VENQDVYILDEPFKGIDKTteavlvkIMKDMQAA--------GKTLLIVHHNL 201
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPS-------IIKDIGRVirrlraegGMAILLVEQYL 192
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-227 |
9.12e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 98.66 E-value: 9.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDT--VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL----TLDAKTVsayggvktNSI 75
Cdd:TIGR04520 4 ENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdgldTLDEENL--------WEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 YNHIAYVPQTsavdwdyP------ITVFEVVLMGTyRRLGwFTRPGKRERdeATKALQTVGMLDYAQRSISQLSGGQQQR 149
Cdd:TIGR04520 76 RKKVGMVFQN-------PdnqfvgATVEDDVAFGL-ENLG-VPREEMRKR--VDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQA-AGKTLLIVHHNL-QTLEAyfDQVLCVNR-RLVGMGPVRD 226
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMeEAVLA--DRVIVMNKgKIVAEGTPRE 222
|
.
gi 2786564536 227 I 227
Cdd:TIGR04520 223 I 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-237 |
1.13e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.99 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 19 FQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlveGTIELTLDAKTVSAYGGvktNSIYNHIAYVPQ-TSAVdwdYPITVF 97
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLP---GQGEILLNGRPLSDWSA---AELARHRAYLSQqQSPP---FAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 98 EvvlmgtYRRLGwftRPGKRERDEATKALQTV----GMLDYAQRSISQLSGGQQQRVFLARALVE-----NQD--VYILD 166
Cdd:COG4138 88 Q------YLALH---QPAGASSEAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 167 EPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNL-QTLeAYFDQVLCVNR-RLVGMGPVRDIVGSPILDETY 237
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLnHTL-RHADRVWLLKQgKLVASGETAEVMTPENLSEVF 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-231 |
2.38e-24 |
|
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: 98.59 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY---DDTV-VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP---LVEGTIE------LTLDAKTVSAYG 68
Cdd:COG0444 5 RNLKVYFptrRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILfdgedlLKLSEKELRKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 69 GvktnsiyNHIAYVPQ--TSAVDwdyP-ITVFEVvLMGTYRRLGWFTRPGKRERdeATKALQTVGmLDYAQRSIS----Q 141
Cdd:COG0444 85 G-------REIQMIFQdpMTSLN---PvMTVGDQ-IAEPLRIHGGLSKAEARER--AIELLERVG-LPDPERRLDryphE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 142 LSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLcV--NRRL 218
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA-VmyAGRI 229
|
250
....*....|...
gi 2786564536 219 VGMGPVRDIVGSP 231
Cdd:COG0444 230 VEEGPVEELFENP 242
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-232 |
2.80e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.95 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLD-----AKTVSAYGGVktnsi 75
Cdd:PRK13537 10 FRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrARHARQRVGV----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 ynhiayVPQTSAVDWDYpiTVFEVVLM-GTYrrlgwFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLAR 154
Cdd:PRK13537 85 ------VPQFDNLDPDF--TVRENLLVfGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 155 ALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQvLCV--NRRLVGMGPVRDIVGSPI 232
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDR-LCVieEGRKIAEGAPHALIESEI 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-212 |
7.73e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.56 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAYGGVktnsiynhIAYVP 83
Cdd:PRK13539 8 LACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA--------CHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVDwdYPITVFEVVLMgtyrrlgWFTRPGKRERDeATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVY 163
Cdd:PRK13539 80 HRNAMK--PALTVAENLEF-------WAAFLGGEELD-IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2786564536 164 ILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHnlQTLEAYFDQVL 212
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH--IPLGLPGAREL 196
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-203 |
8.10e-24 |
|
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: 95.37 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTV-VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSaygGVKTNSIYNHIA 80
Cdd:cd03253 4 ENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI--LIDGQDIR---EVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypiTVFEVVLMGtyrrlgwftRPGKRERD--EATKALQ----TVGMLD-YA----QRSIsQLSGGQQQR 149
Cdd:cd03253 79 VVPQDTVLFND---TIGYNIRYG---------RPDATDEEviEAAKAAQihdkIMRFPDgYDtivgERGL-KLSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQT 203
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLST 198
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-207 |
9.79e-24 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 94.62 E-value: 9.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYD-DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIYNHI 79
Cdd:TIGR02673 4 FHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI--AGEDVNRLRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQtsavdwDYPI----TVFEVVLMgTYRRLGWftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARA 155
Cdd:TIGR02673 82 GVVFQ------DFRLlpdrTVYENVAL-PLEVRGK---KEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 156 LVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAY 207
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRV 203
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-199 |
1.04e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.16 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 8 YDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAyGGVKTNSIYNHIAYVPQTSA 87
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG--DLIVDGLKVND-PKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 88 VdwdYP-ITVFEVVLMGTYRrlgwfTRPGKRE--RDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYI 164
Cdd:PRK09493 88 L---FPhLTALENVMFGPLR-----VRGASKEeaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2786564536 165 LDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHH 199
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-238 |
1.20e-23 |
|
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: 95.10 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNsiynhIAYV 82
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI--LFGGEDATDVPVQERN-----VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 83 PQTSAVdwdYP-ITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:cd03296 80 FQHYAL---FRhMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 162 VYILDEPFKGID----KTTEAVLVKIMKDMQAAgkTLLIVHHNLQTLEAYfDQVLCVNRrlvgmGPVRDiVGSPilDETY 237
Cdd:cd03296 157 VLLLDEPFGALDakvrKELRRWLRRLHDELHVT--TVFVTHDQEEALEVA-DRVVVMNK-----GRIEQ-VGTP--DEVY 225
|
.
gi 2786564536 238 S 238
Cdd:cd03296 226 D 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-228 |
1.83e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 98.28 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGvktNSIYNHIAY 81
Cdd:COG4618 336 LTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV--RLDGADLSQWDR---EELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTsavdwdypITVFEvvlmGTYR----RLGwftrpgKRERDEATKALQTVGMLD--------YAQRsI----SQLSGG 145
Cdd:COG4618 411 LPQD--------VELFD----GTIAeniaRFG------DADPEKVVAAAKLAGVHEmilrlpdgYDTR-IgeggARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAyFDQVLCV-NRRLVGMGPv 224
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLrDGRVQAFGP- 549
|
....
gi 2786564536 225 RDIV 228
Cdd:COG4618 550 RDEV 553
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-239 |
1.90e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.72 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKA---MLGLVPL--VEGTIelTLDAKTVSAyGGVKTNSIY 76
Cdd:COG1117 15 RNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGarVEGEI--LLDGEDIYD-PDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAYVPQTSAVdwdYPITVFEVVLMGtYRRLGWftrPGKRERDEAT-KALQTVGMLDYA----QRSISQLSGGQQQRVF 151
Cdd:COG1117 92 RRVGMVFQKPNP---FPKSIYDNVAYG-LRLHGI---KSKSELDEIVeESLRKAALWDEVkdrlKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 152 LARALVENQDVYILDEPFKGID-KTT---EAVLVKIMKDMqaagkTLLIVHHNLQ--------TleAYFDqvlcvNRRLV 219
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpISTakiEELILELKKDY-----TIVIVTHNMQqaarvsdyT--AFFY-----LGELV 232
|
250 260
....*....|....*....|
gi 2786564536 220 GMGPVRDIVGSPILDETYSY 239
Cdd:COG1117 233 EFGPTEQIFTNPKDKRTEDY 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-199 |
2.18e-23 |
|
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: 93.47 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNsiynhIA 80
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI--YIGGRDVTDLPPKDRD-----IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYP-ITVFEVVLMGTyrRLGWFTRPGKRER-DEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVE 158
Cdd:cd03301 76 MVFQNYAL---YPhMTVYDNIAFGL--KLRKVPKDEIDERvREVAELLQIEHLLD---RKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 159 NQDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHH 199
Cdd:cd03301 148 EPKVFLMDEPLSNLDaKLRVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-212 |
2.53e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.00 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLV--PLVEGTIelTLDAKTVSAyggvktNSIYNHIAYVPQTSAVdw 90
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEV--LINGRPLDK------RSFRKIIGYVPQDDIL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dYP-ITVFEvvlmgtyrrlgwftrpgkrerdeatkalqtvgMLDYAQRsISQLSGGQQQRVFLARALVENQDVYILDEPF 169
Cdd:cd03213 94 -HPtLTVRE--------------------------------TLMFAAK-LRGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2786564536 170 KGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQT-LEAYFDQVL 212
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSeIFELFDKLL 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-201 |
2.66e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVS--------AYGgvkt 72
Cdd:COG3845 8 LRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI--DGKPVRirsprdaiALG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 73 nsiynhIAYVPQT-SAVDwdyPITVFEVVLMGTYRRLGWFTRPgKRERDEATKALQTVGM-LDyAQRSISQLSGGQQQRV 150
Cdd:COG3845 82 ------IGMVHQHfMLVP---NLTVAENIVLGLEPTKGGRLDR-KAARARIRELSERYGLdVD-PDAKVEDLSVGEQQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 151 FLARALVENQDVYILDEPfkgidkTteAVLV--------KIMKDMQAAGKTLLIVHHNL 201
Cdd:COG3845 151 EILKALYRGARILILDEP------T--AVLTpqeadelfEILRRLAAEGKSIIFITHKL 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-237 |
4.92e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIE-------------QGTMTAIVGPNGAGKSTLVKaMLGL-VPLVEGTIelTLDAKTVSA 66
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLK-MLGRhQPPSEGEI--LLDAQPLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 67 YggvKTNSIYNHIAYVPQT-SAVDwdyPITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGG 145
Cdd:PRK10575 78 W---SSKAFARKVAYLPQQlPAAE---GMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEA-VLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGP 223
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVdVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGgEMIAQGT 231
|
250
....*....|....
gi 2786564536 224 VRDIVGSPILDETY 237
Cdd:PRK10575 232 PAELMRGETLEQIY 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-212 |
5.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldAKTVSAYGGVKT-NSIYNHIAYVPQTSAVDWdY 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA--GYHITPETGNKNlKKLRKKVSLVFQFPEAQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PITVFEVVLMGTyRRLGwFTRpgKRERDEATKALQTVGM-LDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKG 171
Cdd:PRK13641 100 ENTVLKDVEFGP-KNFG-FSE--DEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 172 IDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVL 212
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVL 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-214 |
5.59e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.28 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtLDAKTVSayggvKTNSIYNHIAYVP 83
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV-LGVPVPA-----RARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVDWDYpiTVFEVVLMgtyrrLGWFTRPGKRERDEATKALQTVGMLDY-AQRSISQLSGGQQQRVFLARALVENQDV 162
Cdd:PRK13536 121 QFDNLDLEF--TVRENLLV-----FGRYFGMSTREIEAVIPSLLEFARLESkADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 163 YILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQvLCV 214
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDR-LCV 244
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-205 |
6.22e-23 |
|
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: 93.06 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYggvKTNSIYNHI 79
Cdd:cd03251 4 KNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI--DGHDVRDY---TLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAVDWDypiTVFEVVLMGtyrrlgwftRPGKrERDEATKALQTVGMLDYAQRSI-----------SQLSGGQQQ 148
Cdd:cd03251 79 GLVSQDVFLFND---TVAENIAYG---------RPGA-TREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQaAGKTLLIVHHNLQTLE 205
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIE 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-216 |
1.58e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDT--VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL---TLDAKTV----SAYGGVKT 72
Cdd:PRK13635 9 EHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmVLSEETVwdvrRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 73 NsiynhiayvPQTSAVDwdypITVFEVVLMGTYRRlgwftrpgKRERDEATK----ALQTVGMLDYAQRSISQLSGGQQQ 148
Cdd:PRK13635 89 N---------PDNQFVG----ATVQDDVAFGLENI--------GVPREEMVErvdqALRQVGMEDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGID-KTTEAVL--VKIMKDMQAAgkTLLIVHHNLQtlEAYF-DQVLCVNR 216
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDpRGRREVLetVRQLKEQKGI--TVLSITHDLD--EAAQaDRVIVMNK 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-176 |
1.61e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.39 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG-LVPLVEGTIELTLDAKTVSAyggVKTNSiyNHIA 80
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFSASGEVLLNGRRLTA---LPAEQ--RRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTsavDWDYP-ITVFEVVLMGTYRRLGwftRPGKRERDEAtkALQTVGMLDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:COG4136 80 ILFQD---DLLFPhLSVGENLAFALPPTIG---RAQRRARVEQ--ALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170
....*....|....*..
gi 2786564536 160 QDVYILDEPFKGIDKTT 176
Cdd:COG4136 152 PRALLLDEPFSKLDAAL 168
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-200 |
1.73e-22 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 93.95 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 8 YDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSA-------YGgvktnsiynhia 80
Cdd:TIGR03265 14 FGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTI--YQGGRDITRlppqkrdYG------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYP-ITVFEVVLMGTYRRlgwftRPGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:TIGR03265 80 IVFQSYAL---FPnLTVADNIAYGLKNR-----GMGRAEVAErVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHN 200
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHD 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
9-227 |
1.74e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.83 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSaYGGVKTNSIYNHIAYVPQTSAv 88
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI--KGEPIK-YDKKSLLEVRKTVGIVFQNPD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 DWDYPITVFEVVLMGTYRrLGWftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:PRK13639 89 DQLFAPTVEEDVAFGPLN-LGL---SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 169 FKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV-LCVNRRLVGMGPVRDI 227
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVyVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
2.08e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTI---ELTLDAKTVSayggvktnSIY 76
Cdd:PRK13648 11 KNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynNQAITDDNFE--------KLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAYVPQTSAVDWDYPITVFEVVLmgtyrRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAF-----GLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 157 VENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGK-TLLIVHHNL-QTLEAyfDQVLCVNRRLV-GMGPVRDI 227
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLsEAMEA--DHVIVMNKGTVyKEGTPTEI 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-239 |
2.17e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.02 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPL-----VEGTIELTldakTVSAYG-GVKTNS 74
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFF----NQNIYErRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 IYNHIAYV-PQTSAvdwdYPITVFEVVLMGTyRRLGWftRPGKRERDEATKALQTVGMLDYAQ----RSISQLSGGQQQR 149
Cdd:PRK14258 86 LRRQVSMVhPKPNL----FPMSVYDNVAYGV-KIVGW--RPKLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGK-TLLIVHHNLQTLE------AYFDQVLCVNRRLVGMG 222
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSrlsdftAFFKGNENRIGQLVEFG 238
|
250
....*....|....*..
gi 2786564536 223 PVRDIVGSPILDETYSY 239
Cdd:PRK14258 239 LTKKIFNSPHDSRTREY 255
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-222 |
2.60e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.17 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAY---DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGGVktnSIYNHI 79
Cdd:TIGR00958 483 DVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG--QVLLDGVPLVQYDHH---YLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQtsavdwdypitvfEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQR-----------SISQLSGGQQQ 148
Cdd:TIGR00958 558 ALVGQ-------------EPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEfpngydtevgeKGSQLSGGQKQ 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLvkiMKDMQAAGKTLLIVHHNLQTLEAYfDQVLCVNR-RLVGMG 222
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQLL---QESRSRASRTVLLIAHRLSTVERA-DQILVLKKgSVVEMG 695
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
19-201 |
3.99e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.80 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 19 FQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLD--AKTVSAYGGV----KTNSIYNHIayvpqtsavdwdy 92
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfQENNLFSHL------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 piTVFEVVLMGTYrrlgwftrPGKR----ERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:PRK10771 87 --TVAQNIGLGLN--------PGLKlnaaQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190
....*....|....*....|....*....|....
gi 2786564536 169 FKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNL 201
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVcQERQLTLLMVSHSL 190
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-237 |
4.77e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 19 FQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlveGTIELTLDAKTVSAYGGvktNSIYNHIAYVPQTSAVDWDYPitVFE 98
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLP---GSGSIQFAGQPLEAWSA---AELARHRAYLSQQQTPPFAMP--VFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 99 vvlmgtYRRLgwfTRPGKRERDEATKAL----QTVGMLDYAQRSISQLSGGQQQRVFLARALVE-------NQDVYILDE 167
Cdd:PRK03695 89 ------YLTL---HQPDKTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 168 PFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNL-QTLEaYFDQVLCVNR-RLVGMGPVRDIVGSPILDETY 237
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLnHTLR-HADRVWLLKQgKLLASGRRDEVLTPENLAQVF 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-194 |
5.04e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.09 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVK--TNSIYNHIAY 81
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI--MLDGQDITHVPAENrhVNTVFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQtsavdwdypITVFEVVLMGTyrrlgwftRPGKRERDEATK----ALQTVGMLDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:PRK09452 98 FPH---------MTVFENVAFGL--------RMQKTPAAEITPrvmeALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2786564536 158 ENQDVYILDEPFKGIDktteavlVKIMKDMQAAGKTL 194
Cdd:PRK09452 161 NKPKVLLLDESLSALD-------YKLRKQMQNELKAL 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-199 |
7.33e-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: 89.96 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 5 SVAYDD--TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL-TLDAKTVSAyggvktNSIYNHIAY 81
Cdd:cd03245 9 SFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRQLDP------ADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQtsavdwdypitvfEVVLM-GTYR-RLGWFTRPGKRERDEAtkALQTVGMLDYAQRS-------IS----QLSGGQQQ 148
Cdd:cd03245 83 VPQ-------------DVTLFyGTLRdNITLGAPLADDERILR--AAELAGVTDFVNKHpngldlqIGergrGLSGGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHH 199
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITH 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1-199 |
9.10e-22 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.50 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKtvsayggvktnsiynhIA 80
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK----------------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPqtsavdwdypitvfevvlmgtyrrlgwftrpgkrerdeatkalqtvgmldyaqrsisQLSGGQQQRVFLARALVENQ 160
Cdd:cd03221 67 YFE---------------------------------------------------------QLSGGEKMRLALAKLLLENP 89
|
170 180 190
....*....|....*....|....*....|....*....
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQaagKTLLIVHH 199
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYP---GTVILVSH 125
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-216 |
1.24e-21 |
|
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: 89.01 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEltLDAKTVSaygGVKTNSIYNH 78
Cdd:cd03369 9 VENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE--IDGIDIS---TIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSavdwdypitvfeVVLMGTYR-RLGWFtrpGKRERDEATKALQTVGmldyaqrSISQLSGGQQQRVFLARALV 157
Cdd:cd03369 84 LTIIPQDP------------TLFSGTIRsNLDPF---DEYSDEEIYGALRVSE-------GGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 158 ENQDVYILDEPFKGIDKTTEAVLVKIMKDmQAAGKTLLIVHHNLQTLeAYFDQVLCVNR 216
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE-EFTNSTILTIAHRLRTI-IDYDKILVMDA 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-239 |
1.46e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 90.27 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPL------VEGTIELTLDAKTVSAYGGVKTNSIY 76
Cdd:PRK13547 6 HLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgARVTGDVTLNGEPLAAIDAPRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 nhiAYVPQtsAVDWDYPITVFEVVLMGTY---RRLGWFTRpgkRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLA 153
Cdd:PRK13547 86 ---AVLPQ--AAQPAFAFSAREIVLLGRYphaRRAGALTH---RDGEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 154 RALVE---------NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGK--TLLIVHH-NLQTLEAyfDQ-VLCVNRRLVG 220
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDpNLAARHA--DRiAMLADGAIVA 235
|
250
....*....|....*....
gi 2786564536 221 MGPVRDIVGSPILDETYSY 239
Cdd:PRK13547 236 HGAPADVLTPAHIARCYGF 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
1.67e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.05 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYggvKTNSIYNHI 79
Cdd:PRK13632 11 ENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI--DGITISKE---NLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTsavdwdyP------ITVFEVVLMGTYRRLgwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLA 153
Cdd:PRK13632 86 GIIFQN-------PdnqfigATVEDDIAFGLENKK----VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 154 RALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAG-KTLLIVHHNL-QTLEAyfDQVLCVNR-RLVGMGPVRDIV 228
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMdEAILA--DKVIVFSEgKLIAQGKPKEIL 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-214 |
2.08e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 88.38 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 21 IEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGG--------VKTNSIYNHIayvpqtsavdwdy 92
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASG--SIKVNDQSHTGLAPyqrpvsmlFQENNLFAHL------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 piTVFEVVLMGTyrrlgwftRPGKR----ERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:TIGR01277 86 --TVRQNIGLGL--------HPGLKlnaeQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 169 FKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCV 214
Cdd:TIGR01277 156 FSALDpLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-222 |
2.87e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 87.93 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 20 QIEQGTMTAIVGPNGAGKSTLVKAMLG-LVP-----LVEGTIELTLD--AKTVSAYggVKTNSIYNHiayvpqtsavdwd 91
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGfETPqsgrvLINGVDVTAAPpaDRPVSML--FQENNLFAH------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 ypITVFEVVLMGTYRRLgwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKG 171
Cdd:cd03298 85 --LTVEQNVGLGLSPGL----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 172 IDKTTEAVLVKIMKDMQA-AGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMG 222
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNgRIAAQG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-235 |
5.45e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyggVKTNSIYNHIAYVPQTSAv 88
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV--KVMGREVNA---ENEKWVRSKVGLVFQDPD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 DWDYPITVFEVVLMGTyRRLGwFTRPGKRERDEAtkALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:PRK13647 90 DQVFSSTVWDDVAFGP-VNMG-LDKDEVERRVEE--ALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 169 FKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSPILDE 235
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEgRVLAEGDKSLLTDEDIVEQ 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-205 |
5.94e-21 |
|
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: 87.53 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyggvktnsiYNHIAYVPQTSAVD 89
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV--LLDGKPISQ---------YEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 WDypitvfEVVLMGTYRRLGWFTRPGKrERDEATKALQTVGMLDY-----------AQRSISQLSGGQQQRVFLARALVE 158
Cdd:cd03248 95 QE------PVLFARSLQDNIAYGLQSC-SFECVKEAAQKAHAHSFiselasgydteVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAgKTLLIVHHNLQTLE 205
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVE 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
9-202 |
9.37e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.40 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGGVktnsiYNH-IAYVPQTSA 87
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG--EVLWQGEPIRRQRDE-----YHQdLLYLGHQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 88 VDWDypITVFEvvlmgtyrRLGWFTR-PGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILD 166
Cdd:PRK13538 85 IKTE--LTALE--------NLRFYQRlHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2786564536 167 EPFKGIDKTTEAVLVKIMKD-MQAAGKTLLIVHHNLQ 202
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQhAEQGGMVILTTHQDLP 191
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-227 |
9.96e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 90.16 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIA 80
Cdd:TIGR02203 335 NVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI--LLDGHDLADY---TLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypiTVFEVVLMGtyrrlgwftRPGKRERDEATKALQTVGMLDYAQRSI-----------SQLSGGQQQR 149
Cdd:TIGR02203 410 LVSQDVVLFND---TIANNIAYG---------RTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTE----AVLVKIMKdmqaaGKTLLIVHHNLQTLEAYfDQVLCVNR-RLVGMGPV 224
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESErlvqAALERLMQ-----GRTTLVIAHRLSTIEKA-DRIVVMDDgRIVERGTH 551
|
...
gi 2786564536 225 RDI 227
Cdd:TIGR02203 552 NEL 554
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
29-231 |
1.15e-20 |
|
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: 88.70 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 29 IVGPNGAGKSTLVKAMLGLVPLVEGTIELT-LDAKTVSAYggvktnsiYNHIAYVPQTSAVdwdYP-ITVFEVVLMGTYR 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDgEDVTNVPPH--------LRHINMVFQSYAL---FPhMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 107 RlgwftRPGKRERDEATK-ALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMK 185
Cdd:TIGR01187 70 R-----KVPRAEIKPRVLeALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2786564536 186 DMQ-AAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:TIGR01187 145 TIQeQLGITFVFVTHDQEEAMTMSDRIAIMRKgKIAQIGTPEEIYEEP 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-212 |
1.15e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSV-AYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP-----LVEGtIELT-LDAKtvsayggvktnS 74
Cdd:PRK11174 353 EDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKING-IELReLDPE-----------S 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 IYNHIAYVPQTSAVdwdYPITVFEVVLMGtyrrlgwftRPGKRErDEATKALQTVGM----------LDYA--QRSISqL 142
Cdd:PRK11174 421 WRKHLSWVGQNPQL---PHGTLRDNVLLG---------NPDASD-EQLQQALENAWVseflpllpqgLDTPigDQAAG-L 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 143 SGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAvlvKIMKDMQAA--GKTLLIVHHNLQTLEAYfDQVL 212
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ---LVMQALNAAsrRQTTLMVTHQLEDLAQW-DQIW 554
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-223 |
1.37e-20 |
|
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: 84.90 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDaktvsayggvktnsiyNHIA 80
Cdd:cd03223 4 ENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG----------------EDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSavdwdY-PItvfevvlmGTYRRLgwftrpgkrerdeatkalqtvgmLDYAQRSIsqLSGGQQQRVFLARALVEN 159
Cdd:cd03223 68 FLPQRP-----YlPL--------GTLREQ-----------------------LIYPWDDV--LSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDMqaaGKTLLIVHHNlQTLEAYFDQVLcvnrRLVGMGP 223
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR-PSLWKFHDRVL----DLDGEGG 165
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-173 |
1.73e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSayggvKTNSIYNHIA 80
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG--HIRFHGTDVS-----RLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypITVFEVVLMGTY---RRlgwfTRPGKRE-RDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:PRK10851 78 FVFQHYALFRH--MTVFDNIAFGLTvlpRR----ERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170
....*....|....*...
gi 2786564536 157 -VENQdVYILDEPFKGID 173
Cdd:PRK10851 152 aVEPQ-ILLLDEPFGALD 168
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-199 |
1.88e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKaMLGLVPLVE-GTIELTLDAKTVSAYGGVKT-NSIYNH 78
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMPRsGTLNIAGNHFDFSKTPSDKAiRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVdWDYpITVFEVVLMGTYRRLGwFTRPGKRERdeATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:PRK11124 84 VGMVFQQYNL-WPH-LTVQQNLIEAPCRVLG-LSKDQALAR--AEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHH 199
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-202 |
1.93e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 11 TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGGVKTNSIYNH-IAYVPQTSAVD 89
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG--DVIFNGQPMSKLSSAAKAELRNQkLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 WDYpiTVFEVVLMgtyrrlgwftrP---GKRERDEATKA----LQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDV 162
Cdd:PRK11629 100 PDF--TALENVAM-----------PlliGKKKPAEINSRalemLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 163 YILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQ 202
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-223 |
2.67e-20 |
|
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: 85.62 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDT--VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDaktvsaygGVKTNSI---- 75
Cdd:cd03244 6 KNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI--LID--------GVDISKIglhd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 -YNHIAYVPQtsavdwdypitvfEVVLM-GTYRR-LGWFtrpGKRERDEATKALQTVGMLDYAQRSI-----------SQ 141
Cdd:cd03244 76 lRSRISIIPQ-------------DPVLFsGTIRSnLDPF---GEYSDEELWQALERVGLKEFVESLPggldtvveeggEN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 142 LSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKdMQAAGKTLLIVHHNLQTLeAYFDQVLCVNR-RLVG 220
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR-EAFKDCTVLTIAHRLDTI-IDSDRILVLDKgRVVE 217
|
...
gi 2786564536 221 MGP 223
Cdd:cd03244 218 FDS 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-231 |
4.09e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVA-----YDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT-LDAKTVSAYGGV----- 70
Cdd:PRK10619 4 NKLNVIdlhkrYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgQTINLVRDKDGQlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 71 --KTNSIYNHIAYVPQTSAVdWDYpITVFEVVLMGTYRRLGwFTRPGKRERdeATKALQTVGMLDYAQ-RSISQLSGGQQ 147
Cdd:PRK10619 84 knQLRLLRTRLTMVFQHFNL-WSH-MTVLENVMEAPIQVLG-LSKQEARER--AVKYLAKVGIDERAQgKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 148 QRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNRRLV-GMGPVRD 226
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeEEGAPEQ 238
|
....*
gi 2786564536 227 IVGSP 231
Cdd:PRK10619 239 LFGNP 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-231 |
4.12e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.06 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYD----DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNH 78
Cdd:COG1135 6 NLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV--LVDGVDLTALSERELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQ-----TSAvdwdypiTVFEVV-----LMGTyrrlgwftrpGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQ 147
Cdd:COG1135 84 IGMIFQhfnllSSR-------TVAENValpleIAGV----------PKAEIRKrVAELLELVGLSDKADAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 148 QRVFLARALVENQDVYILDEPFKGID-KTTEAVL---VKIMKDMqaaGKTLLIVHHNLQTLEAYFDQVLcV--NRRLVGM 221
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDpETTRSILdllKDINREL---GLTIVLITHEMDVVRRICDRVA-VleNGRIVEQ 222
|
250
....*....|
gi 2786564536 222 GPVRDIVGSP 231
Cdd:COG1135 223 GPVLDVFANP 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-199 |
4.13e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.45 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL---------TLDAKTVSAY---- 67
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfsqKPSEKAIRLLrqkv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 68 GGVKTNsiYNHiayvpqtsavdWDYpITVFEVVLMGTYRRLGwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQ 147
Cdd:COG4161 85 GMVFQQ--YNL-----------WPH-LTVMENLIEAPCKVLG---LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 148 QRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHH 199
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH 199
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-212 |
4.26e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVA-YDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKtvsayggvktnsiynhIAY 81
Cdd:COG4178 367 DLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR----------------VLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSavdwdYpitvfevVLMGTYRRLgwFTRPGKRER---DEATKALQTVG------MLDYAQRSISQLSGGQQQRVFL 152
Cdd:COG4178 431 LPQRP-----Y-------LPLGTLREA--LLYPATAEAfsdAELREALEAVGlghlaeRLDEEADWDQVLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 153 ARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDmQAAGKTLLIV-HHnlQTLEAYFDQVL 212
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVgHR--STLAAFHDRVL 554
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-231 |
4.96e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSayggvkTNSIYNH-IAY 81
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI--FIDGEDVT------HRSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFEVVLMGtYRRLGwftRPgKRERDEATK-ALQTVGMLDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:PRK11432 83 VFQSYAL---FPhMSLGENVGYG-LKMLG---VP-KEERKQRVKeALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 160 QDVYILDEPFKGIDktteAVLVKIMKD-----MQAAGKTLLIVHHNlQTlEAYF--DQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:PRK11432 155 PKVLLFDEPLSNLD----ANLRRSMREkirelQQQFNITSLYVTHD-QS-EAFAvsDTVIVMNKgKIMQIGSPQELYRQP 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-202 |
6.19e-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: 84.79 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL------TLDAKTVSAYGGvktnsiyNHIAYVPQ- 84
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfALDEDARARLRA-------RHVGFVFQs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 -----TsavdwdypITVFEVVLMgtyrrlgwftrP----GKRE-RDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLAR 154
Cdd:COG4181 99 fqllpT--------LTALENVML-----------PlelaGRRDaRARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2786564536 155 ALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQA-AGKTLLIVHHNLQ 202
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-215 |
6.68e-20 |
|
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: 85.08 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 8 YDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLvplvegtieLTLDAKTVSAYGGVKTNSIYNHIAYVP---- 83
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL---------LQPTSGEVRVAGLVPWKRRKKFLRRIGvvfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVDWDYPITVFEVVLMGTYRrlgwfTRPG--KRERDEATKALQTVGMLDYAQRsisQLSGGQQQRVFLARALVENQD 161
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYD-----LPPArfKKRLDELSELLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVN 215
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
13-231 |
7.02e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 85.27 E-value: 7.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSaYGGVKTNSiyNHIAYVPQTSAVDWDY 92
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSG--EILINGHKLE-YGDYKYRC--KHIRMIFQDPNTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PITVFEVvLMGTYRRLGWFTRPGKRERDEATkaLQTVGML-DYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKG 171
Cdd:COG4167 103 RLNIGQI-LEEPLRLNTDLTAEEREERIFAT--LRLVGLLpEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 172 IDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:COG4167 180 LDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQgEVVEYGKTAEVFANP 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-239 |
7.68e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.96 E-value: 7.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPL-----VEGtiELTLDAKTVSAYGGVKTNSIYNH 78
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSG--EVYLDGQDIFKMDVIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQtsavdwdyPI---TVFEVVLMGTyrRLGWFTRPGKRERDEATKALQTVGMLDYAQRSI----SQLSGGQQQRVF 151
Cdd:PRK14247 87 VFQIPN--------PIpnlSIFENVALGL--KLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 152 LARALVENQDVYILDEPFKGIDKTT----EAVLVKIMKDMqaagkTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRD 226
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENtakiESLFLELKKDM-----TIVLVTHFPQQAARISDYVAFLYKgQIVEWGPTRE 231
|
250
....*....|...
gi 2786564536 227 IVGSPILDETYSY 239
Cdd:PRK14247 232 VFTNPRHELTEKY 244
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-199 |
9.31e-20 |
|
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: 84.24 E-value: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP---LVEGTIelTLDAKTVSAYGGVKtnsiynHIAYVPQTSavD 89
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQI--LFNGQPRKPDQFQK------CVAYVRQDD--I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 WDYPITVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPF 169
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 2786564536 170 KGIDKTTEAVLVKIMKDMQAAGKTLLIVHH 199
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-204 |
1.02e-19 |
|
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: 84.30 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAYGGVKTNSIYNhIAYVPQTSavd 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS-VAYAAQKP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 WDYPITVFEVVLMGTyrrlgwftrPGKRERDEATK---ALQ-TVGMLDYA------QRSISqLSGGQQQRVFLARALVEN 159
Cdd:cd03290 89 WLLNATVEENITFGS---------PFNKQRYKAVTdacSLQpDIDLLPFGdqteigERGIN-LSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVK--IMKDMQAAGKTLLIVHHNLQTL 204
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-200 |
1.15e-19 |
|
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: 84.13 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEltLDAKTVSAYggvktnSIYNH---- 78
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL--LDGQDITKL------PMHKRarlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVDWDypITVFEVVLMGtyrrLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:cd03218 77 IGYLPQEASIFRK--LTVEENILAV----LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHN 200
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN 192
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-227 |
1.24e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 87.02 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 11 TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYggvKTNSIYNHIAYVPQTsavdw 90
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL--DGADLKQW---DRETFGKHIGYLPQD----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dypITVFEVVLMGTYRRLGWFTRPgkRERDEATKALQTVGML---------DYAQRSISqLSGGQQQRVFLARALVENQD 161
Cdd:TIGR01842 401 ---VELFPGTVAENIARFGENADP--EKIIEAAKLAGVHELIlrlpdgydtVIGPGGAT-LSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAyFDQVLCVNR-RLVGMGPVRDI 227
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGC-VDKILVLQDgRIARFGERDEV 540
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-204 |
2.28e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.57 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEgtieltlDAKTVsayggvktnsIYNHIAYVPQtsaVDWDYP 93
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-------TSSVV----------IRGSVAYVPQ---VSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVFEVVLMGTyrrlgwftrpgKRERDEATKALQTVGM---LD-YAQRSISQL-------SGGQQQRVFLARALVENQDV 162
Cdd:PLN03232 693 ATVRENILFGS-----------DFESERYWRAIDVTALqhdLDlLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 163 YILDEPFKGID-KTTEAVLVKIMKDmQAAGKTLLIVHHNLQTL 204
Cdd:PLN03232 762 YIFDDPLSALDaHVAHQVFDSCMKD-ELKGKTRVLVTNQLHFL 803
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-211 |
2.95e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDD--TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLvkamLGLvpLV------EGTIelTLDAKTVSAYggvKT 72
Cdd:PRK11160 341 LNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQL--LTrawdpqQGEI--LLNGQPIADY---SE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 73 NSIYNHIAYVPQTsaVDwdypitvfevVLMGTYR---RLGwftrpGKRERDEA-TKALQTVGMLDYAQ------------ 136
Cdd:PRK11160 410 AALRQAISVVSQR--VH----------LFSATLRdnlLLA-----APNASDEAlIEVLQQVGLEKLLEddkglnawlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 137 -RsisQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTE----AVLVKIMKDmqaagKTLLIVHHNLQTLEaYFDQV 211
Cdd:PRK11160 473 gR---QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETErqilELLAEHAQN-----KTVLMITHRLTGLE-QFDRI 543
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-218 |
3.04e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 85.84 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlvEG-TIELTLdaktvsaYG-----GVKTNS 74
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGySNDLTL-------FGrrrgsGETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 IYNHIAYVpqTSAVDWDYPI--TVFEVVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDY-AQRSISQLSGGQQQRVF 151
Cdd:PRK10938 334 IKKHIGYV--SSSLHLDYRVstSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLAL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 152 LARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKT-LLIVHHNLQtleayfDQVLCVNRRL 218
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAE------DAPACITHRL 473
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
14-227 |
3.43e-19 |
|
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: 82.90 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHiayvpqtSAVDWdyp 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV--ILEGKQITEPGPDRMVVFQNY-------SLLPW--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVFEVVLMGTYRRLGWFTRPGKRERDEATkaLQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGID 173
Cdd:TIGR01184 69 LTVRENIALAVDRVLPDLSKSERRAIVEEH--IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 174 KTTEAVLV-KIMKDMQAAGKTLLIVHHNLqtleayfDQVLCVNRRLVGM--GPVRDI 227
Cdd:TIGR01184 147 ALTRGNLQeELMQIWEEHRVTVLMVTHDV-------DEALLLSDRVVMLtnGPAANI 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-176 |
5.11e-19 |
|
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: 85.37 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldAKTVsayggvktnsiynHIAY 81
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---GETV-------------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQT-SAVDWDYpiTVFEVVLMGT-YRRLGWFTRPGKrerdeatkalQTVGMLDYA----QRSISQLSGGQQQRVFLARA 155
Cdd:TIGR03719 390 VDQSrDALDPNK--TVWEEISGGLdIIKLGKREIPSR----------AYVGRFNFKgsdqQKKVGQLSGGERNRVHLAKT 457
|
170 180
....*....|....*....|.
gi 2786564536 156 LVENQDVYILDEPFKGIDKTT 176
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVET 478
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-204 |
5.38e-19 |
|
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: 85.77 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 7 AYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeltldaktvsayggvktnSIYNHIAYVPQTS 86
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------------HMKGSVAYVPQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 avdWDYPITVFEVVLMGTYrrlgwFTRPGKRERDEATKALQTVGMLDYAQRS-ISQ----LSGGQQQRVFLARALVENQD 161
Cdd:TIGR00957 709 ---WIQNDSLRENILFGKA-----LNEKYYQQVLEACALLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2786564536 162 VYILDEPFKGIDK-TTEAVLVKIMKDMQA-AGKTLLIVHHNLQTL 204
Cdd:TIGR00957 781 IYLFDDPLSAVDAhVGKHIFEHVIGPEGVlKNKTRILVTHGISYL 825
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-203 |
6.03e-19 |
|
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: 82.20 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGGVKTNSI-----YNHIAYVPQ 84
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL----------DGVDIRDLnlrwlRSQIGLVSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 TSAVdwdYPITVFEVVLMGTYRRLgwftrpgKRERDEATKA-------------LQT-VGmldyaQRSiSQLSGGQQQRV 150
Cdd:cd03249 85 EPVL---FDGTIAENIRYGKPDAT-------DEEVEEAAKKanihdfimslpdgYDTlVG-----ERG-SQLSGGQKQRI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 151 FLARALVENQDVYILDEPFKGIDKTTEAV----LVKIMKdmqaaGKTLLIVHHNLQT 203
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLvqeaLDRAMK-----GRTTIVIAHRLST 200
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-237 |
6.74e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVS-------AYGGvktnsi 75
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI--IIDDEDISllplharARRG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 ynhIAYVPQTSAVdwdypitvfevvlmgtYRRLGWFTRP----------GKRERDEATKALQTVGMLDYAQRSISQ-LSG 144
Cdd:PRK10895 80 ---IGYLPQEASI----------------FRRLSVYDNLmavlqirddlSAEQREDRANELMEEFHIEHLRDSMGQsLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 145 GQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGP 223
Cdd:PRK10895 141 GERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGT 220
|
250
....*....|....
gi 2786564536 224 VRDIVGSPILDETY 237
Cdd:PRK10895 221 PTEILQDEHVKRVY 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-173 |
6.90e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvktnSIYNH---- 78
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI--FLDGEDITHL------PMHKRarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVDWDypITVFE---VVLMgtyrrlgwFTRPGKRERDEATKALqtvgmLDY------AQRSISQLSGGQQQR 149
Cdd:COG1137 80 IGYLPQEASIFRK--LTVEDnilAVLE--------LRKLSKKEREERLEEL-----LEEfgithlRKSKAYSLSGGERRR 144
|
170 180
....*....|....*....|....
gi 2786564536 150 VFLARALVENQDVYILDEPFKGID 173
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVD 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
16-233 |
7.16e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 84.01 E-value: 7.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 16 DVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTV-SAYGGVKTNSIYNHIAYVPQTSAVdwdYP- 93
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEG--EIVLNGRTLfDSRKGIFLPPEKRRIGYVFQEARL---FPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVFEVVLMGTyrrlgWFTRPGKRERDEAtKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGID 173
Cdd:TIGR02142 90 LSVRGNLRYGM-----KRARPSERRISFE-RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 174 KTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGSPIL 233
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAGPIAEVWASPDL 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-239 |
7.77e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.52 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKA---MLGLVPlvegtieltldakTVSAYGGVKTNSiynH 78
Cdd:PRK14239 9 SDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNP-------------EVTITGSIVYNG---H 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVDW------------DYPITVFEVVLMGTyrRLGwftrpGKRER---DEAT-KALQTVGMLDYAQ----RS 138
Cdd:PRK14239 73 NIYSPRTDTVDLrkeigmvfqqpnPFPMSIYENVVYGL--RLK-----GIKDKqvlDEAVeKSLKGASIWDEVKdrlhDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 139 ISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTT----EAVLVKIMKDMqaagkTLLIVHHNLQTLEAYFDQV-LC 213
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISagkiEETLLGLKDDY-----TMLLVTRSMQQASRISDRTgFF 220
|
250 260
....*....|....*....|....*.
gi 2786564536 214 VNRRLVGMGPVRDIVGSPILDETYSY 239
Cdd:PRK14239 221 LDGDLIEYNDTKQMFMNPKHKETEDY 246
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-219 |
1.03e-18 |
|
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: 81.76 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVsayGGVKTNSIYNHIAYVPQTSav 88
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV--LVDGHDL---ALADPAWLRRQVGVVLQEN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 dwdypitvfeVVLMGTYRRLGWFTRPG-KRERDEATKAL---------------QTVGmldyaQRSISqLSGGQQQRVFL 152
Cdd:cd03252 86 ----------VLFNRSIRDNIALADPGmSMERVIEAAKLagahdfiselpegydTIVG-----EQGAG-LSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 153 ARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTleayfdqVLCVNRRLV 219
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLST-------VKNADRIIV 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-212 |
1.03e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.16 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHIAYVPQT--SAVDw 90
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV--SFRGQDLYQLDRKQRRAFRRDVQLVFQDspSAVN- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dyPITVFEVVLMGTYRRLgwfTRPGKRERDEATKA-LQTVGM-LDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:TIGR02769 103 --PRMTVRQIIGEPLRHL---TSLDESEQKARIAElLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2786564536 169 FKGIDKTTEAVLVKIMKDMQAAGKT-LLIVHHNLQTLEAYFDQVL 212
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVA 222
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
11-199 |
1.37e-18 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 80.92 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 11 TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKaMLGLV-PLVEGTieLTLDAKTVsayggvkTNSIYNH--------IAY 81
Cdd:NF038007 18 TKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLN-IIGMFdSLDSGS--LTLAGKEV-------TNLSYSQkiilrrelIGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVdwdYP-ITVFE-VVLMGTYRRLGwftrpgKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:NF038007 88 IFQSFNL---IPhLSIFDnVALPLKYRGVA------KKERIErVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 159 NQDVYILDEPFKGID-KTTEAVLVKiMKDMQAAGKTLLIVHH 199
Cdd:NF038007 159 NPALLLADEPTGNLDsKNARAVLQQ-LKYINQKGTTIIMVTH 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-215 |
2.14e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTL-DAKTVSAYGGV------------------KTN 73
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFkDEKNKKKTKEKekvleklviqktrfkkikKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 74 SIYNHIAYVPQ-------TSAVDWDypiTVFEVVLMGTyrrlgwftrPGKRERDEATKALQTVGM-LDYAQRSISQLSGG 145
Cdd:PRK13651 102 EIRRRVGVVFQfaeyqlfEQTIEKD---IIFGPVSMGV---------SKEEAKKRAAKYIELVGLdESYLQRSPFELSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVN 215
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-233 |
2.53e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.38 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDT--VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG-LVP--------LVEGTielTLDAKTV----SAY 67
Cdd:PRK13640 10 HVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddnpnskiTVDGI---TLTAKTVwdirEKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 68 GGVKTNsiynhiayvPQTSAVDwdypITVFEVVLMGTYRRlgwfTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQ 147
Cdd:PRK13640 87 GIVFQN---------PDNQFVG----ATVGDDVAFGLENR----AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 148 QRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQtlEAYF-DQVLCVNR-RLVGMGPV 224
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDID--EANMaDQVLVLDDgKLLAQGSP 227
|
....*....
gi 2786564536 225 RDIVGSPIL 233
Cdd:PRK13640 228 VEIFSKVEM 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-221 |
3.54e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP-----LVEGTIELTlDAKTvsayggvKTNSI 75
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETpsageLLAGTAPLA-EARE-------DTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 YNHIAYVPqtsavdWDypiTVFEVVLMGTyrRLGWftrpgkreRDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARA 155
Cdd:PRK11247 87 FQDARLLP------WK---KVIDNVGLGL--KGQW--------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 156 LVENQDVYILDEPFKGIDktteaVLVKI-MKDM-----QAAGKTLLIVHHNLQTLEAYFDQVLCVNRRLVGM 221
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALD-----ALTRIeMQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-216 |
5.78e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.18 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAYGGVKTNS-----I 75
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERagiviI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 YNHIAYVPQtsavdwdypITVFEVVLMGTYrrlgwFTRPGKRERDEAT-----KALQTVGM-LDYAQRSISQLSGGQQQR 149
Cdd:TIGR02633 84 HQELTLVPE---------LSVAENIFLGNE-----ITLPGGRMAYNAMylrakNLLRELQLdADNVTRPVGDYGGGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 150 VFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVlCVNR 216
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTI-CVIR 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-216 |
6.24e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.07 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGgvkTNSIYNHI 79
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG--EIRLDGRPLSSLS---HSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAVDWDypiTVFEVVLMGtyrrlgwftrpgkRERDEAT--KALQTVGMLDYAqRSISQ------------LSGG 145
Cdd:PRK10790 418 AMVQQDPVVLAD---TFLANVTLG-------------RDISEEQvwQALETVQLAELA-RSLPDglytplgeqgnnLSVG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEAVlvkIMKDMQAAGK--TLLIVHHNLQTL-EAyfDQVLCVNR 216
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQA---IQQALAAVREhtTLVVIAHRLSTIvEA--DTILVLHR 549
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-197 |
8.34e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL---TLDAKTVSAyggvktnSIYNHIAYVP-----Q 84
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdgkPVRIRSPRD-------AIRAGIAYVPedrkgE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 TSAVDWDypitVFE---VVLMGTYRRLGWFTRpgKRERDEATKALQTVGM-LDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:COG1129 340 GLVLDLS----IREnitLASLDRLSRGGLLDR--RRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190
....*....|....*....|....*....|....*..
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIV 197
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI 450
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-201 |
8.77e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 81.71 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYD-DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSaygGVKTNSIYNHI 79
Cdd:TIGR01193 476 INDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI--LLNGFSLK---DIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAVdwdYPITVFEVVLMGTYRRLgwftrpgkrERDEATKALQTVGMLDYAQR-----------SISQLSGGQQQ 148
Cdd:TIGR01193 551 NYLPQEPYI---FSGSILENLLLGAKENV---------SQDEIWAACEIAEIKDDIENmplgyqtelseEGSSISGGQKQ 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAagKTLLIVHHNL 201
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRL 669
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-200 |
1.07e-17 |
|
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: 79.37 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 21 IEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAktvsayggvktnsiynhIAYVPQTsaVDWDYPITVFEVv 100
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------------VSYKPQY--IKADYEGTVRDL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 101 LMGTYRRLGwfTRPgkRERDEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVL 180
Cdd:cd03237 82 LSSITKDFY--THP--YFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180
....*....|....*....|.
gi 2786564536 181 VKIMKDM-QAAGKTLLIVHHN 200
Cdd:cd03237 155 SKVIRRFaENNEKTAFVVEHD 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-214 |
1.09e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.71 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTieltldakTVSAYGGVktnsiynhiAYVPQTSavdWDYP 93
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA--------SVVIRGTV---------AYVPQVS---WIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVFEVVLMGTyrrlgwftrPGKRERDEatKALQTVGMldyaQRSISQL---------------SGGQQQRVFLARALVE 158
Cdd:PLN03130 693 ATVRDNILFGS---------PFDPERYE--RAIDVTAL----QHDLDLLpggdlteigergvniSGGQKQRVSMARAVYS 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 159 NQDVYILDEPFKGID-KTTEAVLVKIMKDmQAAGKTLLIVHHNLQTLeAYFDQVLCV 214
Cdd:PLN03130 758 NSDVYIFDDPLSALDaHVGRQVFDKCIKD-ELRGKTRVLVTNQLHFL-SQVDRIILV 812
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-216 |
1.30e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlvEGTI--ELTLDAKTVSAYGGVKTNS---- 74
Cdd:PRK13549 8 MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HGTYegEIIFEGEELQASNIRDTERagia 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 -IYNHIAYVPQtsavdwdypITVFEVVLMGTYrrlgwFTRPGKRERD----EATKALQTVGM-LDYAQRsISQLSGGQQQ 148
Cdd:PRK13549 86 iIHQELALVKE---------LSVLENIFLGNE-----ITPGGIMDYDamylRAQKLLAQLKLdINPATP-VGNLGLGQQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVlCVNR 216
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI-CVIR 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-216 |
1.42e-17 |
|
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: 78.63 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG---------LVPLVEGTIEL-TLDAKTVsayggvktnsIY---NH 78
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWVDLaQASPREI----------LAlrrRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYV-------PQTSAVDwdypitvfevVLMGTYRRLGWftrpgkrERDEA-TKALQTVGMLDYAQR----SISQLSGGQ 146
Cdd:COG4778 95 IGYVsqflrviPRVSALD----------VVAEPLLERGV-------DREEArARARELLARLNLPERlwdlPPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 147 QQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
10-227 |
1.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 79.32 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyGGVKTNSIYNHIAYVPQtsavd 89
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI--IIDGVDITD-KKVKLSDIRKKVGLVFQ----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 wdYP------ITVFEVVLMGTyRRLGWftrpgkrERDE----ATKALQTVGM--LDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:PRK13637 91 --YPeyqlfeETIEKDIAFGP-INLGL-------SEEEienrVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 158 ENQDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:PRK13637 161 MEPKILILDEPTAGLDpKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKgKCELQGTPREV 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-205 |
1.94e-17 |
|
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: 81.11 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 11 TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG-LVPlVEGTIELTldaktvsayggvktnsiyNHIAYVPQTSavd 89
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEP-SEGKIKHS------------------GRISFSPQTS--- 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 WDYPITVFEVVLMG-TYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISqLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:TIGR01271 497 WIMPGTIKDNIIFGlSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 169 FKGIDKTT-----EAVLVKIMkdmqaAGKTLLIVHHNLQTLE 205
Cdd:TIGR01271 576 FTHLDVVTekeifESCLCKLM-----SNKTRILVTSKLEHLK 612
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-231 |
2.41e-17 |
|
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: 80.50 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAY-----------DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlVEGTIelTLDAKTVSAYGGV 70
Cdd:COG4172 279 RDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEI--RFDGQDLDGLSRR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 71 KTNSIYNHIAYVPQtsavdwDyP-------ITVFEVVL--MGTYRRlgwftRPGKRERDE-ATKALQTVGML-DYAQRSI 139
Cdd:COG4172 356 ALRPLRRRMQVVFQ------D-PfgslsprMTVGQIIAegLRVHGP-----GLSAAERRArVAEALEEVGLDpAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 140 SQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-R 217
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDgK 503
|
250
....*....|....
gi 2786564536 218 LVGMGPVRDIVGSP 231
Cdd:COG4172 504 VVEQGPTEQVFDAP 517
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-239 |
3.02e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLvplvegtIELTLDAKTvsaYGGVKtnsIYNHIAYVP 83
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRL-------LELNEEARV---EGEVR---LFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVD--------WDYP-----ITVFEVVLMGTyrRLGWFTRPgKRERDEATK-ALQTVGMLDYAQRSI----SQLSGG 145
Cdd:PRK14267 77 DVDPIEvrrevgmvFQYPnpfphLTIYDNVAIGV--KLNGLVKS-KKELDERVEwALKKAALWDEVKDRLndypSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGID----KTTEAVLVKIMKDMqaagkTLLIVHHNLQTLEAYFDQVLCVNR-RLVG 220
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDpvgtAKIEELLFELKKEY-----TIVLVTHSPAQAARVSDYVAFLYLgKLIE 228
|
250
....*....|....*....
gi 2786564536 221 MGPVRDIVGSPILDETYSY 239
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKY 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-202 |
3.57e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.15 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKaMLGLVP-------LVEGTIELTLDAKTVSAYGGVKTNSIYNHIAY 81
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDkptsgtyRVAGQDVATLDADALAQLRREHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDwdypitvfEVVLMGTYRRLGwftRPGKRERdeATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:PRK10535 98 LSHLTAAQ--------NVEVPAVYAGLE---RKQRLLR--AQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQ 202
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ 205
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-204 |
4.44e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.81 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVsayggvKTNSIYNHIAYVP 83
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI--DGKTA------TRGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVDWDypitvfevvlMGTYRRLGWFTR-PGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDV 162
Cdd:PRK13543 89 HLPGLKAD----------LSTLENLHFLCGlHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 163 YILDEPFKGIDKTTEAVLVKIMK-DMQAAGKTLLIVHHNLQTL 204
Cdd:PRK13543 159 WLLDEPYANLDLEGITLVNRMISaHLRGGGAALVTTHGAYAAP 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-201 |
4.65e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGGVKTNSIYNHIAYVP 83
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG--EILFDGENIPAMSRSRLYTVRKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVDWDypITVFEVVL--MGTYRRLgwftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:PRK11831 91 QSGALFTD--MNVFDNVAypLREHTQL-----PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNL 201
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDV 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-231 |
4.94e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT-LDAKTVSAYGGvKTNSIYNHIAY 81
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQR-PINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQtsavdwdypITVFEVVLMGTYR-RLgwftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:PRK11607 103 FPH---------MTVEQNIAFGLKQdKL-----PKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 161 DVYILDEPFKGIDKT-TEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:PRK11607 169 KLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHP 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-211 |
7.14e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 7 AYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGGVKTNsiynhIAYVPQTS 86
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG--DLFIGEKRMNDVPPAERG-----VGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 AVdwdYP-ITVFEVVLMGTYrrlgwFTRPGKRERD----EATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQD 161
Cdd:PRK11000 85 AL---YPhLSVAENMSFGLK-----LAGAKKEEINqrvnQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 162 VYILDEPFKGIDktteAVL-----VKIMKDMQAAGKTLLIVHHnlqtleayfDQV 211
Cdd:PRK11000 154 VFLLDEPLSNLD----AALrvqmrIEISRLHKRLGRTMIYVTH---------DQV 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-239 |
7.71e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEG---TIELTLDAKTVSAYGGVKtnSIYNHI 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrySGDVLLGGRSIFNYRDVL--EFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAvdwDYPITVFEVVLMGTYRRLgwfTRPGKRERDEATKALQTVGMLDYAQRSIS----QLSGGQQQRVFLARA 155
Cdd:PRK14271 104 GMLFQRPN---PFPMSIMDNVLAGVRAHK---LVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 156 LVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEAYFDQ-VLCVNRRLVGMGPVRDIVGSPILD 234
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRaALFFDGRLVEEGPTEQLFSSPKHA 256
|
....*
gi 2786564536 235 ETYSY 239
Cdd:PRK14271 257 ETARY 261
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-216 |
9.14e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.13 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIE---LTLDAKTVSayggvktnsiyNHIAYVPQTSAVDW 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvddITITHKTKD-----------KYIRPVRKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 DYPIT-VFE-----VVLMGTYRrlgwFTRPGKRERDEATKALQTVGM-LDYAQRSISQLSGGQQQRVFLARALVENQDVY 163
Cdd:PRK13646 92 QFPESqLFEdtverEIIFGPKN----FKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 164 ILDEPFKGIDKTTEAVLVKIMKDMQA-AGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-202 |
1.04e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.74 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKA---MLGLVP--LVEGTIEL--------TLDAKTVSAYGGV 70
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgfRVEGKVTFhgknlyapDVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 71 ---KTN----SIYNHIAYVPQTSAvdwdYPITVFEVVLMGTYRRLGWftrpgkrerDEATKALQTVGMldyaqrsisQLS 143
Cdd:PRK14243 96 vfqKPNpfpkSIYDNIAYGARING----YKGDMDELVERSLRQAALW---------DEVKDKLKQSGL---------SLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 144 GGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAgKTLLIVHHNLQ 202
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQ 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-227 |
1.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldAKTVsayggVKTNSIYNHIAYVPQTSAVDWDYP 93
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV---GDIV-----VSSTSKQKEIKPVRKKVGVVFQFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVF--EVVLMGTYRRLGWFTRPGKRERDEATKALQTVGML-DYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:PRK13643 94 ESQLfeETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDV 231
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-168 |
1.35e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.39 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKtvsayggvktnsiynhIAYVP 83
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN----------------IGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVDWDYPITVFEvvlmgtyrrlgWFTRPGKRERDEatkalQTV-GML-------DYAQRSISQLSGGQQQRVFLARA 155
Cdd:PRK15064 389 QDHAYDFENDLTLFD-----------WMSQWRQEGDDE-----QAVrGTLgrllfsqDDIKKSVKVLSGGEKGRMLFGKL 452
|
170
....*....|...
gi 2786564536 156 LVENQDVYILDEP 168
Cdd:PRK15064 453 MMQKPNVLVMDEP 465
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-239 |
1.39e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.77 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP------LVEGTIELTLDAKTVSAYGGVKTNSIYNHIAYVPQTSA 87
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEptrgqvLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 88 VDwdypITVFEVVLMGTyrrlgwftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDE 167
Cdd:PRK10070 124 LD----NTAFGMELAGI---------NAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 168 PFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGSPILDETYSY 239
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-205 |
1.77e-16 |
|
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: 76.43 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldaktvsayggvktnsiyNHIAYVPQTSavdWDY 92
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS------------------GRISFSSQFS---WIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PITVFEVVLMGT----YRRLGwFTRPGKRERDEATKALQTVGMLdyAQRSISqLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:cd03291 111 PGTIKENIIFGVsydeYRYKS-VVKACQLEEDITKFPEKDNTVL--GEGGIT-LSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 169 FKGIDKTTE-----AVLVKIMkdmqaAGKTLLIVHHNLQTLE 205
Cdd:cd03291 187 FGYLDVFTEkeifeSCVCKLM-----ANKTRILVTSKMEHLK 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-197 |
2.73e-16 |
|
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: 74.01 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYddtvVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggVKTNSIYNHIAYV 82
Cdd:cd03215 9 GLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI--TLDGKPVTRR--SPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 83 PqtsavdwdypitvfevvlmgtyrrlgwftrpgkRERdeatkalQTVGMLDyaQRSI-------SQLSGGQQQRVFLARA 155
Cdd:cd03215 81 P---------------------------------EDR-------KREGLVL--DLSVaenialsSLLSGGNQQKVVLARW 118
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 156 LVENQDVYILDEPFKGID-KTTEAVLvKIMKDMQAAGKTLLIV 197
Cdd:cd03215 119 LARDPRVLILDEPTRGVDvGAKAEIY-RLIRELADAGKAVLLI 160
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
20-201 |
3.51e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 20 QIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDaktvsayggvktnsiynhIAYVPQTsaVDWDYPITVfEV 99
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK------------------ISYKPQY--IKPDYDGTV-ED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 100 VLMGTYRRLG--WFtrpgkreRDEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGID---- 173
Cdd:PRK13409 420 LLRSITDDLGssYY-------KSEIIKPLQLERLLD---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqr 489
|
170 180
....*....|....*....|....*....
gi 2786564536 174 -KTTEAvlvkIMKDMQAAGKTLLIVHHNL 201
Cdd:PRK13409 490 lAVAKA----IRRIAEEREATALVVDHDI 514
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-231 |
3.98e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHIAYVPQTSAVDWDYP 93
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI--IFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVFEVVlMGTYRRLGWFtrPGKRERDEATKALQTVGML-DYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGI 172
Cdd:PRK10261 418 QTVGDSI-MEPLRVHGLL--PGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 173 DKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLgQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-212 |
4.05e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDD-TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTV--SAYGGVKTNSIYNHI 79
Cdd:PRK13636 10 ELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG--RILFDGKPIdySRKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAvdwdYPITVFEVVLMGTYRrlgwFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:PRK13636 88 FQDPDNQL----FSASVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVL 212
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVF 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-239 |
4.56e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL------------TLDAKTVSAYG 68
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyfgkdifQIDAIKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 69 GV---KTN-----SIYNHIAYVPQTSAVDWDYPItvfEVVLMGTYRRLGWFTRPGKRERDEAtkalqtvgmldyaqrsiS 140
Cdd:PRK14246 93 GMvfqQPNpfphlSIYDNIAYPLKSHGIKEKREI---KKIVEECLRKVGLWKEVYDRLNSPA-----------------S 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 141 QLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAgKTLLIVHHNLQTLEAYFDQV-LCVNRRLV 219
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVaFLYNGELV 231
|
250 260
....*....|....*....|
gi 2786564536 220 GMGPVRDIVGSPILDETYSY 239
Cdd:PRK14246 232 EWGSSNEIFTSPKNELTEKY 251
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-202 |
6.86e-16 |
|
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: 76.36 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 20 QIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDaktvsayggvktnsiynhIAYVPQTsaVDWDYPITVFEV 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK------------------ISYKPQY--ISPDYDGTVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 100 VLMGTYRRLG--WFtrpgkreRDEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTE 177
Cdd:COG1245 422 LRSANTDDFGssYY-------KTEIIKPLGLEKLLD---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180
....*....|....*....|....*.
gi 2786564536 178 AVLVKIMKD-MQAAGKTLLIVHHNLQ 202
Cdd:COG1245 492 LAVAKAIRRfAENRGKTAMVVDHDIY 517
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-214 |
7.06e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYD--DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIA 80
Cdd:PRK11176 346 NVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI--LLDGHDLRDY---TLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypiTVFEVVlmgTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSI-----SQLSGGQQQRVFLARA 155
Cdd:PRK11176 421 LVSQNVHLFND---TIANNI---AYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVigengVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 156 LVENQDVYILDEPFKGIDKTTE----AVLVKIMKDmqaagKTLLIVHHNLQTLEAYfDQVLCV 214
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESEraiqAALDELQKN-----RTSLVIAHRLSTIEKA-DEILVV 551
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
9.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.38 E-value: 9.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYD---DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTvsayggvKTN--SI 75
Cdd:PRK13650 7 VKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT-------EENvwDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 YNHIAYV---PQTSAVDwdypITVFEVVLMGTYRRlgwfTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFL 152
Cdd:PRK13650 80 RHKIGMVfqnPDNQFVG----ATVEDDVAFGLENK----GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 153 ARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLqtleayfDQVLCVNRRLV 219
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDL-------DEVALSDRVLV 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-212 |
1.10e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 15 KDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVktNSIYNHIAYVP---QTSAVDWD 91
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI--MLNGKEINALSTA--QRLARGLVYLPedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 YPITVFEVVLmgTYRRLGWFTRPgKRERDEATKALQTVGM-LDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:PRK15439 356 APLAWNVCAL--THNRRGFWIKP-ARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVL 212
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVL 474
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-233 |
1.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.25 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT-LDAKTVSAYGGVKtnSIYNH 78
Cdd:PRK13644 4 LENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgIDTGDFSKLQGIR--KLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSAVDWdypiTVFEVVLMGTYRrlgwFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVE 158
Cdd:PRK13644 82 VFQNPETQFVGR----TVEEDLAFGPEN----LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 159 NQDVYILDEPFKGID-KTTEAVLVKImKDMQAAGKTLLIVHHNLQTLEAYfDQVLCVNR-RLVGMGPVRDIVGSPIL 233
Cdd:PRK13644 154 EPECLIFDEVTSMLDpDSGIAVLERI-KKLHEKGKTIVYITHNLEELHDA-DRIIVMDRgKIVLEGEPENVLSDVSL 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-168 |
1.50e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldAKTVsayggvktnsiynHIAY 81
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---GETV-------------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQT-SAVDWDYpiTVFEVVLMGT-YRRLgwftrpGKRErdeaTKALQTVGMLDYA----QRSISQLSGGQQQRVFLARA 155
Cdd:PRK11819 392 VDQSrDALDPNK--TVWEEISGGLdIIKV------GNRE----IPSRAYVGRFNFKggdqQKKVGVLSGGERNRLHLAKT 459
|
170
....*....|...
gi 2786564536 156 LVENQDVYILDEP 168
Cdd:PRK11819 460 LKQGGNVLLLDEP 472
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-211 |
1.55e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 15 KDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT-LDAKTVSAYGGVKtnsiyNHIAYVPQTSAVDWDYP 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgKDISPRSPLDAVK-----KGMAYITESRRDNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 -------ITVFEVVLMGTYR-RLGWFTRPGKRERDEATKALQTVGMLDYAQrSISQLSGGQQQRVFLARALVENQDVYIL 165
Cdd:PRK09700 355 nfsiaqnMAISRSLKDGGYKgAMGLFHEVDEQRTAENQRELLALKCHSVNQ-NITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2786564536 166 DEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-231 |
1.63e-15 |
|
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: 75.11 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDD----TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP----LVEGTIE------LTLDAKTVSAY 67
Cdd:COG4172 10 EDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILfdgqdlLGLSERELRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 68 GGvktnsiyNHIAYV---PQTS--AVdwdYPI--TVFEVVLMgtYRRLGwftrpGKRERDEATKALQTVGMLDYAQRSIS 140
Cdd:COG4172 90 RG-------NRIAMIfqePMTSlnPL---HTIgkQIAEVLRL--HRGLS-----GAAARARALELLERVGIPDPERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 141 ---QLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVlCVNR 216
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRV-AVMR 231
|
250
....*....|....*..
gi 2786564536 217 --RLVGMGPVRDIVGSP 231
Cdd:COG4172 232 qgEIVEQGPTAELFAAP 248
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
2.63e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDT-----VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldaktvSAYGGVKTNSIY 76
Cdd:PRK13631 25 KNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG------DIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAYVPQ----------TSAVDWDYP------ITVFEVVLMGTYRrLGwftRPGKRERDEATKALQTVGM-LDYAQRSI 139
Cdd:PRK13631 99 LITNPYSKkiknfkelrrRVSMVFQFPeyqlfkDTIEKDIMFGPVA-LG---VKKSEAKKLAKFYLNKMGLdDSYLERSP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 140 SQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-203 |
2.81e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 74.47 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYD-DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyggVKTNSIYNHIAY 81
Cdd:COG5265 362 NVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI--LIDGQDIRD---VTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWDypiTVFEVVLMGtyrrlgwftRPGKRERD--EATKALQ--------------TVGmldyaQRSIsQLSGG 145
Cdd:COG5265 437 VPQDTVLFND---TIAYNIAYG---------RPDASEEEveAAARAAQihdfieslpdgydtRVG-----ERGL-KLSGG 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQT 203
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLST 555
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-215 |
3.30e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 17 VFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT------LDAKTVSAYGGVKTnsiYNHIAYVPQtsavdw 90
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhiegLPGHQIARMGVVRT---FQHVRLFRE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dypITVFEVVLMGTYRRL------GWFTRPGKR--ERDEATKA---LQTVGMLDYAQRSISQLSGGQQQRVFLARALVEN 159
Cdd:PRK11300 95 ---MTVIENLLVAQHQQLktglfsGLLKTPAFRraESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 160 QDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVN 215
Cdd:PRK11300 172 PEILMLDEPAAGLNpKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-202 |
4.55e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGlvplvegtiELTLDAKTVsaYGGVKTNsiynhIA 80
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG---------QLQADSGRI--HCGTKLE-----VA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAvDWDYPITVF--------EVVLMGTYRR-LGW---FTRPGKRERdEATKAlqtvgmldyaqrsisqLSGGQQQ 148
Cdd:PRK11147 386 YFDQHRA-ELDPEKTVMdnlaegkqEVMVNGRPRHvLGYlqdFLFHPKRAM-TPVKA----------------LSGGERN 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAagkTLLIVHHNLQ 202
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG---TVLLVSHDRQ 498
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-199 |
4.65e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDD--TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlvegtieltldAKTVSAYGGVKTNSIYnh 78
Cdd:COG2401 31 LEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-----------GTPVAGCVDVPDNQFG-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 iayvPQTSAVDWDYPITVFevvlmgtyrrlgwftrpgkrerDEATKALQTVGMLDYA--QRSISQLSGGQQQRVFLARAL 156
Cdd:COG2401 98 ----REASLIDAIGRKGDF----------------------KDAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2786564536 157 VENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHH 199
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-212 |
6.10e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHIAYVPQTS--AVDw 90
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV--SWRGEPLAKLNRAQRKAFRRDIQMVFQDSisAVN- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dyPITVFEVVLMGTYRRLgwfTRPGKRERDEATKA-LQTVGMLD-YAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:PRK10419 104 --PRKTVREIIREPLRHL---LSLDKAERLARASEmLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2786564536 169 FKGIDKTTEAVLVKIMKDMQAAGKT-LLIVHHNLQTLEAYFDQVL 212
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVM 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-211 |
7.10e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY----DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP-----------LVEGTIELTLDAKTVS 65
Cdd:PRK15134 8 IENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvypsgdiRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 66 AYGGvktnsiyNHIAYVPQTSAVDWDyPITVFEVVLmgtYRRLGwFTRPGKRE--RDEATKALQTVGMLDYAQRSIS--- 140
Cdd:PRK15134 88 GVRG-------NKIAMIFQEPMVSLN-PLHTLEKQL---YEVLS-LHRGMRREaaRGEILNCLDRVGIRQAAKRLTDyph 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 141 QLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRV 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-231 |
7.62e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTI---ELTLDA-KTVSAYGGVkTNSIYNHI 79
Cdd:PRK11264 9 LVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgDITIDTaRSLSQQKGL-IRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAVdwdYP-ITVFEVVLMGTyrrlgwfTRPGKRERDEAT----KALQTVGMLDYAQRSISQLSGGQQQRVFLAR 154
Cdd:PRK11264 88 GFVFQNFNL---FPhRTVLENIIEGP-------VIVKGEPKEEATararELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 155 ALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQgRIVEQGPAKALFADP 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-199 |
7.99e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 71.37 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTI-----ELTL-----------DAKTVsayggvktNSIY 76
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIrvggeEIRLkpdrdgelvpaDRRQL--------QRIR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAYVPQtSAVDWDYpITVFEVVLMGTYRRLGwftRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:COG4598 95 TRLGMVFQ-SFNLWSH-MTVLENVIEAPVHVLG---RPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 157 VENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHH 199
Cdd:COG4598 170 AMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-220 |
9.67e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAY-DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldAKTVSAYGGVKTNSIYNHIAY 81
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS--GHDITRLKNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVDWDYpiTVFEVVLMgtyrRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQD 161
Cdd:PRK10908 84 IFQDHHLLMDR--TVYDNVAI----PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 162 VYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVG 220
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDgHLHG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-201 |
1.01e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTV-------SAYGGVKTnsIYNHIAYVPQts 86
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI--LIDGQEMrfasttaALAAGVAI--IYQELHLVPE-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 avdwdypITVFEVVLMGTY-RRLGWFTRpgKRERDEATKALQTVGM-LDyAQRSISQLSGGQQQRVFLARALVENQDVYI 164
Cdd:PRK11288 94 -------MTVAENLYLGQLpHKGGIVNR--RLLNYEAREQLEHLGVdID-PDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 2786564536 165 LDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNL 201
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-216 |
1.14e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 8 YDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAYGGVktnSIYNHIAYVPQtsa 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL---ALRQQVATVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 88 vDWDYPI--TVFEVVLMGTYRRLGWFTRPGKRERDEAtkaLQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYIL 165
Cdd:PRK13638 85 -DPEQQIfyTDIDSDIAFSLRNLGVPEAEITRRVDEA---LTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 166 DEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQ 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-236 |
1.58e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSaYG--GVKTNSIyNHIAYVPQTSAVDWD 91
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG--ELLIDDHPLH-FGdySYRSQRI-RMIFQDPSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 YPITVFEVVLmgtyrRLGWFTRPGKRERdEATKALQTVGML-DYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:PRK15112 105 RISQILDFPL-----RLNTDLEPEQREK-QIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGSPILDET 236
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMhQGEVVERGSTADVLASPLHELT 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-201 |
1.69e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 71.30 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 16 DVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHIAYV---PQTS------ 86
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEI--LFDGQDITGLSGRELRPLRRRMQMVfqdPYASlnprmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 ---AVDwdYPITVFEVVlmgtyrrlgwftrPGKRERDEATKALQTVGML-DYAQRSISQLSGGQQQRVFLARALVENQDV 162
Cdd:COG4608 114 vgdIIA--EPLRIHGLA-------------SKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2786564536 163 YILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNL 201
Cdd:COG4608 179 IVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDL 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
16-173 |
2.12e-14 |
|
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: 71.29 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 16 DVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtldaktvsayGG---VKTNSIYN------HIAYVPQTS 86
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL----------GGevlQDSARGIFlpphrrRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 AVdwdYP-ITVFEVVLMGtYRRLGwfTRPGKRERDEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQDVYIL 165
Cdd:COG4148 87 RL---FPhLSVRGNLLYG-RKRAP--RAERRISFDEVVELLGIGHLLD---RRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
....*...
gi 2786564536 166 DEPFKGID 173
Cdd:COG4148 158 DEPLAALD 165
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-211 |
2.17e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 21 IEQGTMTAIVGPNGAGKSTLVKAMLG-LVP-LVEGTIELTLDaKTVSAYGGvktNSIYNH----------IAYVPQtsav 88
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGeLIPnLGDYEEEPSWD-EVLKRFRG---TELQNYfkklyngeikVVHKPQ---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 dwdYpITVFEVVLMGTYRRLgwFTRPGKRER-DEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQDVYILDE 167
Cdd:PRK13409 168 ---Y-VDLIPKVFKGKVREL--LKKVDERGKlDEVVERLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2786564536 168 PFKGIDKTTEAVLVKIMKDMqAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNV 281
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-224 |
2.32e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP---LVEGTIELT---LDAKTVSAYGgvktnsiynhiAYVPQtsa 87
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNgmpIDAKEMRAIS-----------AYVQQ--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 88 VDWDYP-ITVFEVVLMGTYRRLG-WFTRPGKRERDEATkaLQTVGMLDYAQRSISQ------LSGGQQQRVFLARALVEN 159
Cdd:TIGR00955 107 DDLFIPtLTVREHLMFQAHLRMPrRVTKKEKRERVDEV--LQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKT-LLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPV 224
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTiICTIHQPSSELFELFDKIILMAEgRVAYLGSP 251
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-211 |
4.19e-14 |
|
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: 70.97 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 22 EQGTMTAIVGPNGAGKSTLVKAMLG-LVP-LveGTIELTLDAKTV-SAYGGvktNSIYNH----------IAYVPQtsAV 88
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGeLKPnL--GDYDEEPSWDEVlKRFRG---TELQDYfkklangeikVAHKPQ--YV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 DwdypitVFEVVLMGTYRRLgwFTRPGKRER-DEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQDVYILDE 167
Cdd:COG1245 170 D------LIPKVFKGTVREL--LEKVDERGKlDELAEKLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2786564536 168 PFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-228 |
4.44e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 8 YDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldaKTVSA---YGGvktnsiynhiAYVPQ 84
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN---GRVSAlleLGA----------GFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 TSAVDwdypitvfEVVLMGtyRRLGwFTRPGKRERDEATKALQTVGmlDYAQRSISQLSGGQQQRVFLARALVENQDVYI 164
Cdd:COG1134 103 LTGRE--------NIYLNG--RLLG-LSRKEIDEKFDEIVEFAELG--DFIDQPVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 165 LDE-------PF--KGIDKtteavlvkiMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIV 228
Cdd:COG1134 170 VDEvlavgdaAFqkKCLAR---------IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKgRLVMDGDPEEVI 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-204 |
5.81e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeltLDAKTvsayggvktnsiynhIAYVPQTSavdWD 91
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---WAERS---------------IAYVPQQA---WI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 YPITVFEVVLMGTYR---RLGWFTRPGKRERDEATKA--LQTvgmlDYAQRSISqLSGGQQQRVFLARALVENQDVYILD 166
Cdd:PTZ00243 733 MNATVRGNILFFDEEdaaRLADAVRVSQLEADLAQLGggLET----EIGEKGVN-LSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 167 EPFKGIDKtteAVLVKIMKDM---QAAGKTLLIVHHNLQTL 204
Cdd:PTZ00243 808 DPLSALDA---HVGERVVEECflgALAGKTRVLATHQVHVV 845
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-205 |
8.19e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.55 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGL--VPLVEGTIELtldaktvsayggvKTNSIYNhi 79
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILF-------------KGEDITD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 ayvpqtsavdwdypITVFEVVLMGTYrrLGwFTRPgkrerdeatKALQTVGMLDYAqRSISQ-LSGGQQQRVFLARALVE 158
Cdd:cd03217 69 --------------LPPEERARLGIF--LA-FQYP---------PEIPGVKNADFL-RYVNEgFSGGEKKRNEILQLLLL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLE 205
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLD 168
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-168 |
9.14e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 8 YD-DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVsayggvktnsiyNH-------I 79
Cdd:PRK11650 13 YDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI--GGRVV------------NElepadrdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAVdwdYP-ITVFEVvlMGtY----RRLGwftRPGKRER-DEATKALQTVGMLDyaqRSISQLSGGQQQRVFLA 153
Cdd:PRK11650 79 AMVFQNYAL---YPhMSVREN--MA-YglkiRGMP---KAEIEERvAEAARILELEPLLD---RKPRELSGGQRQRVAMG 146
|
170
....*....|....*
gi 2786564536 154 RALVENQDVYILDEP 168
Cdd:PRK11650 147 RAIVREPAVFLFDEP 161
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-212 |
9.37e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 15 KDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKTNSIYNHIAYVPQTSAVDWDYPI 94
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV--AWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 95 TVFEVVL--MGTYrrlgwFTRPGKRERDEATKALQT-VGML-DYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:PRK15079 116 TIGEIIAepLRTY-----HPKLSRQEVKDRVKAMMLkVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVL 212
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVL 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-173 |
9.95e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLvkamLGLVP----LVEGTIElTLDAKTVSAyggVKTNSIYNH 78
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIAgarkIQQGRVE-VLGGDMADA---RHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQtsavdwdYP-ITVFEvvlmgtyrRLGWFTR---PGKRER----DEATKAlqtVGMLDYAQRSISQLSGGQQQRV 150
Cdd:NF033858 78 IAYMPQglg-knlYPtLSVFE--------NLDFFGRlfgQDAAERrrriDELLRA---TGLAPFADRPAGKLSGGMKQKL 145
|
170 180
....*....|....*....|...
gi 2786564536 151 FLARALVENQDVYILDEPFKGID 173
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVD 168
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-233 |
1.19e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTvsayggvKTN--SIYNHIAYVPQTSAvDW 90
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT-------KENirEVRKFVGLVFQNPD-DQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 DYPITVFEVVLMGtyrrlgwftrPGKRERDEAT------KALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYI 164
Cdd:PRK13652 91 IFSPTVEQDIAFG----------PINLGLDEETvahrvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 165 LDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSPIL 233
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIFLQPDL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-227 |
1.43e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.51 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAygGVKTN---SIYNHIAYVPQtsavdw 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--TIGERVITA--GKKNKklkPLRKKVGIVFQ------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dYP------ITVFEVVLMGTYRrlgwFTRPGKRERDEATKALQTVGM-LDYAQRSISQLSGGQQQRVFLARALVENQDVY 163
Cdd:PRK13634 93 -FPehqlfeETVEKDICFGPMN----FGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 164 ILDEPFKGIDKTTEavlvKIMKDM-----QAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:PRK13634 168 VLDEPTAGLDPKGR----KEMMEMfyklhKEKGLTTVLVTHSMEDAARYADQIVVMHKgTVFLQGTPREI 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-231 |
1.68e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlVEGtiELTLDAKTVSAYGGVKTNSIYNHIAYVPQTSAV 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQG--EIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 DWDYPITVFEVVLMGTyrRLGWFTRPGKRERDEATKALQTVGmLDYA--QRSISQLSGGQQQRVFLARALVENQDVYILD 166
Cdd:PRK15134 374 SLNPRLNVLQIIEEGL--RVHQPTLSAAQREQQVIAVMEEVG-LDPEtrHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 167 EPFKGIDKTTEAVLVKIMKDMQAAGK-TLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQgEVVEQGDCERVFAAP 517
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-219 |
1.71e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.19 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 11 TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL----TLDAKTV----SAYGGVKTNSIYNHIAYV 82
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldTSDEENLwdirNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 83 pqtsavdwdypitVFEVVLMGTyRRLGWftrPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDV 162
Cdd:PRK13633 103 -------------VEEDVAFGP-ENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 163 YILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHnlqtleaYFDQVLCVNRRLV 219
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITH-------YMEEAVEADRIIV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-222 |
1.72e-13 |
|
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: 67.17 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldaKTVSAYGGVktnsiynhiayvpqtsAVDWDY 92
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR---GRVSSLLGL----------------GGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PITVFE-VVLMGTYrrLGWfTRPGKRERDEATKALQTVGmlDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKG 171
Cdd:cd03220 98 ELTGREnIYLNGRL--LGL-SRKEIDEKIDEIIEFSELG--DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 172 IDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMG 222
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKgKIRFDG 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-167 |
2.39e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNHIA 80
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL--LFEGEDISTL---KPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypiTVFEVVLmgtyrrLGWFTRPGKRERDEATKALQTVGMLDYA-QRSISQLSGGQQQRVFLARALVEN 159
Cdd:PRK10247 85 YCAQTPTLFGD---TVYDNLI------FPWQIRNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFM 155
|
....*...
gi 2786564536 160 QDVYILDE 167
Cdd:PRK10247 156 PKVLLLDE 163
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-202 |
2.92e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 24 GTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTldAKTVSAYG-------GVKTnsIYNHIAYVPQtsavdwdypITV 96
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYL--GKEVTFNGpkssqeaGIGI--IHQELNLIPQ---------LTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 97 FEVVLMG-----TYRRLGWftrpgKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKG 171
Cdd:PRK10762 97 AENIFLGrefvnRFGRIDW-----KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190
....*....|....*....|....*....|.
gi 2786564536 172 IDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQ 202
Cdd:PRK10762 172 LTDTETESLFRVIRELKSQGRGIVYISHRLK 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-227 |
3.20e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELT------LDAKtVSAYGGVKTns 74
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkLDHK-LAAQLGIGI-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 IYNHIayvpqtSAVDwdyPITVFEVVLMG---TYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVF 151
Cdd:PRK09700 85 IYQEL------SVID---ELTVLENLYIGrhlTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 152 LARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDI 227
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMkDGSSVCSGMVSDV 232
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
14-223 |
4.21e-13 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 66.13 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLglvpLVEGT---IEltldakTVSAYG----GVKTNSIYNHIAYVPQTS 86
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTI----YAEGQrryVE------SLSAYArqflGQMDKPDVDSIEGLSPAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 AVDWDYP-----ITVFEVVLMGTYRRLgWFTRPGKRERdeaTKALQTVGmLDY--AQRSISQLSGGQQQRVFLARALVEN 159
Cdd:cd03270 81 AIDQKTTsrnprSTVGTVTEIYDYLRL-LFARVGIRER---LGFLVDVG-LGYltLSRSAPTLSGGEAQRIRLATQIGSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 160 QD--VYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYfDQVlcvnrrlVGMGP 223
Cdd:cd03270 156 LTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAA-DHV-------IDIGP 213
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-206 |
4.69e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 66.52 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG--LVPLVEGTIEL----TLDAKT--VSAYG----- 68
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFkgqdLLELEPdeRARAGlflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 69 -------GVkTNSIYNHIAYVPQTSAVDWDyPITVFEVvlmgtyrrlgwftrpgkreRDEATKALQTVGM-LDYAQRSIS 140
Cdd:TIGR01978 84 qypeeipGV-SNLEFLRSALNARRSARGEE-PLDLLDF-------------------EKLLKEKLALLDMdEEFLNRSVN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 141 Q-LSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEA 206
Cdd:TIGR01978 143 EgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNY 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-198 |
6.30e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLD--------------AKTVSA 66
Cdd:PRK11147 6 IHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvEGTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 67 Y--GGVKTNS----IYNHIAYVPQTSAVDwdypitvfevVLMGTYRRL--------GWftrpgkRERDEATKALQTVGmL 132
Cdd:PRK11147 86 FvaEGIEEQAeylkRYHDISHLVETDPSE----------KNLNELAKLqeqldhhnLW------QLENRINEVLAQLG-L 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 133 DyAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQaaGKTLLIVH 198
Cdd:PRK11147 149 D-PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFISH 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-229 |
7.08e-13 |
|
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: 67.13 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 17 VFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTV-------------SAYGGV--KTNSIYNHIAY 81
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVdmtkpgpdgrgraKRYIGIlhQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQ-TSAVDWDYPitvFEVVLMgtyrrlgwftrpgkrerdEATKALQTVGMLDYAQRSI-----SQLSGGQQQRVFLARA 155
Cdd:TIGR03269 383 LDNlTEAIGLELP---DELARM------------------KAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQV 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 156 LVENQDVYILDEPFKGIDKTTE-AVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV-LCVNRRLVGMGPVRDIVG 229
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKvDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAaLMRDGKIVKIGDPEEIVE 517
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-200 |
8.17e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYggvKTNSIYNH-I 79
Cdd:PRK11614 8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI--VFDGKDITDW---QTAKIMREaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAVdwDYPITVFEVVLMGtyrrlGWFT-RPGKRERDEATKALQTVGMLDYAQRSiSQLSGGQQQRVFLARALVE 158
Cdd:PRK11614 83 AIVPEGRRV--FSRMTVEENLAMG-----GFFAeRDQFQERIKWVYELFPRLHERRIQRA-GTMSGGEQQMLAIGRALMS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHN 200
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQN 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-231 |
9.19e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKaMLGLV-PLVEGtiELTLDAKTVSAYGGVKTNSIYNHIAYVPQTsavdwdy 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLAR-LLTMIeTPTGG--ELYYQGQDLLKADPEAQKLLRQKIQIVFQN------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PI-----------TVFEVVLMGTYrrlgwFTRPGKRERdeATKALQTVGML-DYAQRSISQLSGGQQQRVFLARALVENQ 160
Cdd:PRK11308 101 PYgslnprkkvgqILEEPLLINTS-----LSAAERREK--ALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 161 DVYILDEPFKGIDKTTEAVLVKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSP 231
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLgRCVEKGTKEQIFNNP 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-202 |
1.06e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSaygGVKTNSIYNHIAYVPQ---- 84
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI--LIDGKDVT---KLPEYKRAKYIGRVFQdpmm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 -TSAvdwdyPITVFEVVLM----GTYRRLGWftRPGKRERDEATKALQTVGM-----LDYAqrsISQLSGGQQQRVFLAR 154
Cdd:COG1101 92 gTAP-----SMTIEENLALayrrGKRRGLRR--GLTKKRRELFRELLATLGLglenrLDTK---VGLLSGGQRQALSLLM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2786564536 155 ALVENQDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIVHHNLQ 202
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDpKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-212 |
1.48e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAmlglvplVEGTIELTLDAKTVSAYGGVKTNSIYNHIAYVPQTsavDWDY 92
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNA-------LAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQD---DILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 P-ITVFEVVLMGTYRRLgwftrPGKRERDEATKALQTV----GMLD-----YAQRSISQLSGGQQQRVFLARALVENQDV 162
Cdd:PLN03211 153 PhLTVRETLVFCSLLRL-----PKSLTKQEKILVAESViselGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 163 YILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLI-VHHNLQTLEAYFDQVL 212
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVL 278
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
10-231 |
1.94e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPL-VEGTI-ELTLDAKTVSAyGGVKTnsiyNHIAYVPQTsa 87
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgVRQTAgRVLLDGKPVAP-CALRG----RKIATIMQN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 88 vdwdyPITVFEVVL-MGTYRRLGWFTRPGKRERDEATKALQTVGmLDYAQRSIS----QLSGGQQQRVFLARALVENQDV 162
Cdd:PRK10418 88 -----PRSAFNPLHtMHTHARETCLALGKPADDATLTAALEAVG-LENAARVLKlypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 163 YILDEPFKGIDKTTEA-VLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGMGPVRDIVGSP 231
Cdd:PRK10418 162 IIADEPTTDLDVVAQArILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMsHGRIVEQGDVETLFNAP 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-200 |
2.02e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.70 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGL--VPLVEGTIelTLDAKTV--------SAYG--- 68
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSI--LLDGEDIlelspderARAGifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 69 ---------GVkTNSIYNHIAYvpqtSAVDwDYPITVFEVvlmgtyrrlgwftrpgkreRDEATKALQTVGM-LDYAQRS 138
Cdd:COG0396 82 afqypveipGV-SVSNFLRTAL----NARR-GEELSAREF-------------------LKLLKEKMKELGLdEDFLDRY 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 139 ISQ-LSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHN 200
Cdd:COG0396 137 VNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-227 |
2.24e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.21 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTI-----ELT-LDAKTVSAYggvktnsiYNHIAYVPQ--- 84
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqDLTaLSEKELRKA--------RRQIGMIFQhfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 --TSAvdwdypiTVFEVV-----LMGTyrrlgwftrpGKRERDE-ATKALQTVGMLDYAQRSISQLSGGQQQRVFLARAL 156
Cdd:PRK11153 93 llSSR-------TVFDNValpleLAGT----------PKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786564536 157 VENQDVYILDEPFKGID-KTTEAVLvKIMKDMQAA-GKTLLIVHHNLQTLEAYFDQVlCV--NRRLVGMGPVRDI 227
Cdd:PRK11153 156 ASNPKVLLCDEATSALDpATTRSIL-ELLKDINRElGLTIVLITHEMDVVKRICDRV-AVidAGRLVEQGTVSEV 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-222 |
2.40e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTV-VLKDVFFQIEQGTMTAIVGPNGAGKSTLVkAMLGLV--PlVEGTIelTLDAKTVSaygGVKTNSIYNH 78
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVfdP-QSGRI--LIDGTDIR---TVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAyvpqtsavdwdypiTVF-EVVLMG-TYR---RLGwftRPGKRErDEATKALQTVGMLDYAQRSI-----------SQL 142
Cdd:PRK13657 411 IA--------------VVFqDAGLFNrSIEdniRVG---RPDATD-EEMRAAAERAQAHDFIERKPdgydtvvgergRQL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 143 SGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAvLVKIMKDMQAAGKTLLIVHHNLQTL-EAyfDQVLCV-NRRLVG 220
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEA-KVKAALDELMKGRTTFIIAHRLSTVrNA--DRILVFdNGRVVE 549
|
..
gi 2786564536 221 MG 222
Cdd:PRK13657 550 SG 551
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-227 |
3.00e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVK-TNSIYNHIAYVPQ--TSAVdw 90
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV--RVDDTLITSTSKNKdIKQIRKKVGLVFQfpESQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dYPITVFEVVLMGTYRrlgwFTRPGKRERDEATKALQTVGML-DYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPF 169
Cdd:PRK13649 99 -FEETVLKDVAFGPQN----FGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 170 KGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDI 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-221 |
3.44e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 19 FQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSayggVKT--NSIYNHIAYVPQTSAVDWDYPI-T 95
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAG--QVYLDGKPID----IRSprDAIRAGIMLCPEDRKAEGIIPVhS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 96 VFEVVLMGTYR---RLGWFTRPgKRERDEATK-----ALQTVGmldyAQRSISQLSGGQQQRVFLARALVENQDVYILDE 167
Cdd:PRK11288 348 VADNINISARRhhlRAGCLINN-RWEAENADRfirslNIKTPS----REQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 168 PFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQtleayfdQVLCVNRRLVGM 221
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLP-------EVLGVADRIVVM 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-227 |
6.91e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGlvplvegtiELTLdaktvsaYGGVKTNSiYNHIA--------- 80
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG---------ELPL-------LSGERQSQ-FSHITrlsfeqlqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQT---------SAVDWDYPITVFEVVLMGTYrrlgwftrpgKRER-DEATKALQTVGMLDyaqRSISQLSGGQQQRV 150
Cdd:PRK10938 78 LVSDEwqrnntdmlSPGEDDTGRTTAEIIQDEVK----------DPARcEQLAQQFGITALLD---RRFKYLSTGETRKT 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 151 FLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV-LCVNRRLVGMGPVRDI 227
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAgVLADCTLAETGEREEI 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-214 |
7.77e-12 |
|
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: 64.08 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 16 DVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP-LVEGTIelTLDAKTVSAYGGVKtnSIYNHIAYVPQTSAVDWDYPI 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNV--FINGKPVDIRNPAQ--AIRAGIAMVPEDRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 95 tvfevVLMGTYRRLGWFTRPGKRERDEATKALQTVGmlDYAQR----------SISQLSGGQQQRVFLARALVENQDVYI 164
Cdd:TIGR02633 354 -----LGVGKNITLSVLKSFCFKMRIDAAAELQIIG--SAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2786564536 165 LDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCV 214
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-205 |
1.08e-11 |
|
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: 63.67 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGL--VPLVEGTIeltldaktvsayggvktnsIYnHIAY 81
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRI-------------------IY-HVAL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 82 VPQTSAVD-----------------------WDYPITVF--------------------EVVLMGTYRRLGWFTRPGKRE 118
Cdd:TIGR03269 66 CEKCGYVErpskvgepcpvcggtlepeevdfWNLSDKLRrrirkriaimlqrtfalygdDTVLDNVLEALEEIGYEGKEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 119 RDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGID-KTTEAVLVKIMKDMQAAGKTLLIV 197
Cdd:TIGR03269 146 VGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGISMVLT 225
|
....*...
gi 2786564536 198 HHNLQTLE 205
Cdd:TIGR03269 226 SHWPEVIE 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-214 |
1.25e-11 |
|
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: 62.38 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 24 GTMTAIVGPNGAGKSTLVKAMLG-LVP-LVEGTIELTLDaKTVSAYGGVKTNSIYNHI-------AYVPQTsaVDwDYPI 94
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPnLGKFDDPPDWD-EILDEFRGSELQNYFTKLlegdvkvIVKPQY--VD-LIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 95 TVfevvlMGTYRRLgwFTRPGKRER-DEATKALQTVGMLDyaqRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGID 173
Cdd:cd03236 102 AV-----KGKVGEL--LKKKDERGKlDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 174 KTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCV 214
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-201 |
1.53e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELtlDAKTVSAYGGVKTNSIYNHIAYVPQTSAVD 89
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI--DGELLTAENVWNLRRKIGMVFQNPDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 wdypITVFEVVLMGTYRRlgwfTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPF 169
Cdd:PRK13642 97 ----ATVEDDVAFGMENQ----GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190
....*....|....*....|....*....|...
gi 2786564536 170 KGIDKTTEAVLVKIMKDMQAAGK-TLLIVHHNL 201
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDL 201
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-212 |
1.53e-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: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTL--VKAMLGLVPLVEGTIeltldakTVSAYGGVKTNSIYnhIAYVPQtsaVDWD 91
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLldVLAGRKTAGVITGEI-------LINGRPLDKNFQRS--TGYVEQ---QDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 YP-ITVFEVVLMGTYRRlgwftrpgkrerdeatkalqtvgmldyaqrsisQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:cd03232 91 SPnLTVREALRFSALLR---------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAAGKTLLI-VHHNLQTLEAYFDQVL 212
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLL 180
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-211 |
1.59e-11 |
|
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: 63.42 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYD-DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKtvsayggvktnsiynhI 79
Cdd:TIGR03719 7 MNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIK----------------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 80 AYVPQTSAVDWDypITVFEVVLMGTYRRLGWFTR----------PGK------RERDEATKALQTVGMLDYAQR------ 137
Cdd:TIGR03719 71 GYLPQEPQLDPT--KTVRENVEEGVAEIKDALDRfneisakyaePDAdfdklaAEQAELQEIIDAADAWDLDSQleiamd 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 138 ---------SISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAagkTLLIVHHnlqtlEAYF 208
Cdd:TIGR03719 149 alrcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTH-----DRYF 220
|
....
gi 2786564536 209 -DQV 211
Cdd:TIGR03719 221 lDNV 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-211 |
2.02e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPL--VEGTIEltLDAKTVsAYGGVKTNS------IYNHIAYVPQT 85
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEIL--FDGEVC-RFKDIRDSEalgiviIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 86 SavdwdypitVFEVVLMGTYR-RLGWFTRPgkRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYI 164
Cdd:NF040905 94 S---------IAENIFLGNERaKRGVIDWN--ETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 165 LDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-197 |
2.10e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 16 DVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP-LVEGTIelTLDAKTVSayggVKT--NSIYNHIAYVPQTSAVDWDY 92
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEI--FIDGKPVK----IRNpqQAIAQGIAMVPEDRKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PI-TVFEVVLMGTYRRlgwFTRPGK-RERDEATKALQTVGMLDYAQRS----ISQLSGGQQQRVFLARALVENQDVYILD 166
Cdd:PRK13549 354 PVmGVGKNITLAALDR---FTGGSRiDDAAELKTILESIQRLKVKTASpelaIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190
....*....|....*....|....*....|.
gi 2786564536 167 EPFKGIDKTTEAVLVKIMKDMQAAGKTLLIV 197
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-209 |
2.12e-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: 62.89 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 21 IEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL---TLDAKTVSAYGgvktnsiyNHIayvpqtSAVDWDYpiTVF 97
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLdgqPVTADNREAYR--------QLF------SAVFSDF--HLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 98 EvvlmgtyRRLGwftRPGKRERDEATKALQTVGM---LDYAQRSIS--QLSGGQQQRVFLARALVENQDVYILDE----- 167
Cdd:COG4615 419 D-------RLLG---LDGEADPARARELLERLELdhkVSVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEwaadq 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2786564536 168 --PFKGIDKTTeavlvkIMKDMQAAGKTLLIVHHNlqtlEAYFD 209
Cdd:COG4615 489 dpEFRRVFYTE------LLPELKARGKTVIAISHD----DRYFD 522
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-216 |
5.25e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 23 QGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGT-------IELTLDAKTVSAYGGVKTNSIYNHIayvpqtsavdwdypiT 95
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTvlvggkdIETNLDAVRQSLGMCPQHNILFHHL---------------T 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 96 VFEVVLMgtYRRLGwfTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKT 175
Cdd:TIGR01257 1020 VAEHILF--YAQLK--GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2786564536 176 TEAVLVKIMKDMQaAGKTLLIVHHNLQTLEAYFDQVLCVNR 216
Cdd:TIGR01257 1096 SRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQ 1135
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-204 |
5.68e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTI--------ELTLDA-----KTVSAYGGVKTNSIY 76
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltKLQLDSwrsrlAVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAY-VPQTSAVDWDYPI---TVFEVVLmgtyrRL--GWFTRPGKRerdeatkalqtvGMLdyaqrsisqLSGGQQQRV 150
Cdd:PRK10789 407 NNIALgRPDATQQEIEHVArlaSVHDDIL-----RLpqGYDTEVGER------------GVM---------LSGGQKQRI 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786564536 151 FLARALVENQDVYILDEPFKGIDKTTEAvlvKIMKDMQ--AAGKTLLIVHHNLQTL 204
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEH---QILHNLRqwGEGRTVIISAHRLSAL 513
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-201 |
7.61e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDA--KTVSAYggvktnsiYNHIA 80
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikKDLCTY--------QKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDypITVFEVVLMGTYrrlgwfTRPGKRERDEATKALQTVGMLDYaqrSISQLSGGQQQRVFLARALVENQ 160
Cdd:PRK13540 78 FVGHRSGINPY--LTLRENCLYDIH------FSPGAVGITELCRLFSLEHLIDY---PCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2786564536 161 DVYILDEPFKGIDK-TTEAVLVKIMKDMQAAGKTLLIVHHNL 201
Cdd:PRK13540 147 KLWLLDEPLVALDElSLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
14-201 |
9.94e-11 |
|
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: 59.94 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLglVPLVEGtiELTLDAKTVSAYGGVKTNSIYNHIAYVPQ--------- 84
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTL--YPALAR--RLHLKKEQPGNHDRIEGLEHIDKVIVIDQspigrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 85 -----TSAVDwdyPI-------------------------TVFEVVLMGTYRRLGWFTRPGKRERdeATKALQTVGmLDY 134
Cdd:cd03271 87 npatyTGVFD---EIrelfcevckgkrynretlevrykgkSIADVLDMTVEEALEFFENIPKIAR--KLQTLCDVG-LGY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 135 AQ--RSISQLSGGQQQRVFLARALVE---NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNL 201
Cdd:cd03271 161 IKlgQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
13-202 |
2.03e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.64 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL------TLDAKTVSAYGGVKTNSIYNHIAYVPQTS 86
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhQMDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 AVDwdypitvfEVVLMGTYRrlgwftrpGKRERDEATKALQTVGMLDYAQRSI---SQLSGGQQQRVFLARALVENQDVY 163
Cdd:PRK10584 105 ALE--------NVELPALLR--------GESSRQSRNGAKALLEQLGLGKRLDhlpAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2786564536 164 ILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQ 202
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-206 |
2.18e-10 |
|
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: 60.41 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 21 IEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAyggvKTNSIYNHIAYVPQTSAVDwdypitvfevV 100
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG--DATVAGKSILT----NISDVHQNMGYCPQFDAID----------D 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 101 LMGTYRRLGWFTR----PGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTT 176
Cdd:TIGR01257 2026 LLTGREHLYLYARlrgvPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190
....*....|....*....|....*....|
gi 2786564536 177 EAVLVKIMKDMQAAGKTLLIVHHNLQTLEA 206
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTSHSMEECEA 2135
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-231 |
2.35e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVpLVEGTIELTLDAKTVSAYGGVK-TNSIYNHIAYVPQTSAVDWdY 92
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISETGQTIVGDYAIPANLKKIKeVKRLRKEIGLVFQFPEYQL-F 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 PITVFEVVLMGTYRrLGwftrpgkRERDEATKALQTVGML-----DYAQRSISQLSGGQQQRVFLARALVENQDVYILDE 167
Cdd:PRK13645 105 QETIEKDIAFGPVN-LG-------ENKQEAYKKVPELLKLvqlpeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 168 PFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLqtleayfDQVLCVNRRLVGM--GPVRDIvGSP 231
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNM-------DQVLRIADEVIVMheGKVISI-GSP 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-229 |
2.38e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 8 YD---DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL--TLDAKTV------SAYGGVK----- 71
Cdd:PTZ00265 392 YDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndSHNLKDInlkwwrSKIGVVSqdpll 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 72 -TNSIYNHIAYvPQTSAVDWDYpitvfevvLMGTYRRLGWFTRPGKRERD-----------------------EATKALQ 127
Cdd:PTZ00265 472 fSNSIKNNIKY-SLYSLKDLEA--------LSNYYNEDGNDSQENKNKRNscrakcagdlndmsnttdsneliEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 128 TVG---MLDYAQRSI--------------------SQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIM 184
Cdd:PTZ00265 543 TIKdseVVDVSKKVLihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2786564536 185 KDMQA-AGKTLLIVHHNLQTLEaYFDQVLCVNRRLVGMGPVRDIVG 229
Cdd:PTZ00265 623 NNLKGnENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIG 667
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-233 |
2.61e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 57.72 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAmlglvplvegtielTLDAKTVSAYGGVKTNSIYNHIAYVPQTSAVdwdyp 93
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--------------GLYASGKARLISFLPKFSRNKLIFIDQLQFL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 itvfevVLMG-TYRRLGwftrpgkrerdeatkalqtvgmldyaqRSISQLSGGQQQRVFLARALVENQD--VYILDEPFK 170
Cdd:cd03238 72 ------IDVGlGYLTLG---------------------------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLqtleayfdQVLCVNRRLVGMGPVRDIVGSPIL 233
Cdd:cd03238 119 GLHQQDINQLLEVIKGLIDLGNTVILIEHNL--------DVLSSADWIIDFGPGSGKSGGKVV 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-227 |
2.67e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDD-TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGgvkTNSIYNH-IA 80
Cdd:COG3845 262 NLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI--RLDGEDITGLS---PRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQ----TSAVDwDYPITvfEVVLMGTYRRLGwFTRPG---KRERDEATKALqtvgMLDY------AQRSISQLSGGQQ 147
Cdd:COG3845 337 YIPEdrlgRGLVP-DMSVA--ENLILGRYRRPP-FSRGGfldRKAIRAFAEEL----IEEFdvrtpgPDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 148 QRVFLARALVENQDVYILDEPFKGID-KTTEAVLVKIMkDMQAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVR 225
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDvGAIEFIHQRLL-ELRDAGAAVLLISEDLDEILALSDRIAVMYEgRIVGEVPAA 487
|
..
gi 2786564536 226 DI 227
Cdd:COG3845 488 EA 489
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-199 |
4.27e-10 |
|
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: 58.99 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLvegtieltldaktvsaYGGVKTNSIYNHIAYVPQ----TSA 87
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV----------------YGGRLTKPAKGKLFYVPQrpymTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 88 VDWD---YPITVFEvvlmgtyrrlgwFTRPGKRERDeATKALQTVGMLDYAQRSIS---------QLSGGQQQRVFLARA 155
Cdd:TIGR00954 530 TLRDqiiYPDSSED------------MKRRGLSDKD-LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2786564536 156 LVENQDVYILDEpfkgidkTTEAVLV----KIMKDMQAAGKTLLIVHH 199
Cdd:TIGR00954 597 FYHKPQFAILDE-------CTSAVSVdvegYMYRLCREFGITLFSVSH 637
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-173 |
6.16e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSayggvkTNS----IYNHIAYVPQTSAVD 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSG--YVTLDGHEVV------TRSpqdgLANGIVYISEDRKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 90 wdypitvfEVVL-------MgTYRRLGWFTRPGKRERDEATKalQTVGmlDYAQ----------RSISQLSGGQQQRVFL 152
Cdd:PRK10762 340 --------GLVLgmsvkenM-SLTALRYFSRAGGSLKHADEQ--QAVS--DFIRlfniktpsmeQAIGLLSGGNQQKVAI 406
|
170 180
....*....|....*....|.
gi 2786564536 153 ARALVENQDVYILDEPFKGID 173
Cdd:PRK10762 407 ARGLMTRPKVLILDEPTRGVD 427
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-219 |
6.65e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG-LVPlVEGTIEltldaktVSAYGGVKtnsiyNHIAYVPQTSAV---- 88
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVR-------VLGYVPFK-----RRKEFARRIGVVfgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 ---DWDYPitvfevvLMGTYRRLG--------WFtrpgKRERDEATKALqtvGMLDYAQRSISQLSGGQQQRVFLARALV 157
Cdd:COG4586 105 sqlWWDLP-------AIDSFRLLKaiyripdaEY----KKRLDELVELL---DLGELLDTPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 158 ENQDVYILDEPFKGIDktteaVLVKIM-----KDMQAA-GKTLLIVHHNLQTLEAyfdqvLCvnRRLV 219
Cdd:COG4586 171 HRPKILFLDEPTIGLD-----VVSKEAireflKEYNRErGTTILLTSHDMDDIEA-----LC--DRVI 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-212 |
1.55e-09 |
|
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: 55.73 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPL---VEGTIEltldaktvsaYGGV---KTNSIYNH-IAYVPQTs 86
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIH----------YNGIpykEFAEKYPGeIIYVSEE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 87 avDWDYP-ITVFEVVlmgtyrrlgwftrpgkrerDEATKALqtvgmldyAQRSISQLSGGQQQRVFLARALVENQDVYIL 165
Cdd:cd03233 92 --DVHFPtLTVRETL-------------------DFALRCK--------GNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2786564536 166 DEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHhnLQT-LEAY--FDQVL 212
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMaDVLKTTTFVSL--YQAsDEIYdlFDKVL 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-211 |
1.72e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEltLDAKTVSAYGGVKTNS--IYnhia 80
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE--IGGNPCARLTPAKAHQlgIY---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVdwdYP-ITVFEVVLMGTYRrlgwftRPGKRERDEA-TKALQTVGMLDYaqrSISQLSGGQQQRVFLARALVE 158
Cdd:PRK15439 90 LVPQEPLL---FPnLSVKENILFGLPK------RQASMQKMKQlLAALGCQLDLDS---SAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 159 NQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-204 |
1.96e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGgvkTNSIYNHIAYVPQTSavdwdy 92
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG--RIMIDDCDVAKFG---LTDLRRVLSIIPQSP------ 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 pitvfeVVLMGTYRrlgwFTRPGKRERDEAT--KALQTVGMLDYAQRSISQL-----------SGGQQQRVFLARALVEN 159
Cdd:PLN03232 1320 ------VLFSGTVR----FNIDPFSEHNDADlwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRR 1389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKDmQAAGKTLLIVHHNLQTL 204
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTI 1433
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-216 |
3.45e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 9 DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLveGTIelTLDAKTVSayGGVKTNSIYNHIAYVPQTsav 88
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTT--GVI--TGGDRLVN--GRPLDSSFQRSIGYVQQQ--- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 DWDYP-ITVFEVVLMGTYRRlgwftRPG---KRERDE-ATKALQTVGMLDYAQRSI----SQLSGGQQQRVFLARALVEN 159
Cdd:TIGR00956 845 DLHLPtSTVRESLRFSAYLR-----QPKsvsKSEKMEyVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAK 919
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 160 QDVYI-LDEPFKGIDKTTEAVLVKIMKDMQAAGKTLL-IVHHNLQTLEAYFDQVLCVNR 216
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILcTIHQPSAILFEEFDRLLLLQK 978
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-204 |
4.16e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 55.63 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDD--TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlVEGTIELTldaktvsaygGVKTNSI-----Y 76
Cdd:cd03289 8 LTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQID----------GVSWNSVplqkwR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 NHIAYVPQtsavdwdypiTVFevVLMGTYRRLgwFTRPGKRERDEATKALQTVGMLDYAQRSISQ-----------LSGG 145
Cdd:cd03289 77 KAFGVIPQ----------KVF--IFSGTFRKN--LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 146 QQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKdmQA-AGKTLLIVHHNLQTL 204
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAfADCTVILSEHRIEAM 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-204 |
4.55e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY--DDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlVEGTIELTldaktvsaygGVKTNSIY-- 76
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID----------GVSWNSVTlq 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 ---NHIAYVPQtsavdwdypiTVFevVLMGTYRRlgwFTRPGKRERDEAT-KALQTVGMldyaQRSISQ----------- 141
Cdd:TIGR01271 1289 twrKAFGVIPQ----------KVF--IFSGTFRK---NLDPYEQWSDEEIwKVAEEVGL----KSVIEQfpdkldfvlvd 1349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 142 ----LSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKdmQA-AGKTLLIVHHNLQTL 204
Cdd:TIGR01271 1350 ggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK--QSfSNCTVILSEHRVEAL 1415
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-216 |
7.40e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP--LVEGTIELTldaktvsayGGVKTNSIYNH 78
Cdd:PLN03140 883 MKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRIS---------GFPKKQETFAR 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IA-YVPQTsavDWDYP-ITVFEVVLMGTYRRLGwfTRPGKRER----DEATKALQTVGMLD--YAQRSISQLSGGQQQRV 150
Cdd:PLN03140 954 ISgYCEQN---DIHSPqVTVRESLIYSAFLRLP--KEVSKEEKmmfvDEVMELVELDNLKDaiVGLPGVTGLSTEQRKRL 1028
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 151 FLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHH--NLQTLEAyFDQVLCVNR 216
Cdd:PLN03140 1029 TIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEA-FDELLLMKR 1095
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-210 |
9.35e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.98 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLvkAML--GLVPLVEGtiELTLDAKTVSAYggvktnsiyNHIAYVPQTSAVDWD 91
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSG--EILLDGKPVTAE---------QPEDYRKLFSAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 YPItvFEvvlmgtyRRLGwftrPGKRERDEA--TKALQTVGM-----LDYAQRSISQLSGGQQQRVFLARALVENQDVYI 164
Cdd:PRK10522 406 FHL--FD-------QLLG----PEGKPANPAlvEKWLERLKMahkleLEDGRISNLKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 165 LDEPFKGIDKTTEAVLV-KIMKDMQAAGKTLLIVHHNlqtlEAYFDQ 210
Cdd:PRK10522 473 LDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHD----DHYFIH 515
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-231 |
1.07e-08 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 54.07 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeltldakTVSAYGGVKTNSIYNHIA 80
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA-------TYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 YVPQTSAVDWDYpitVFEVVLMGTYRRLGWFTRPGKRE-----------RDEATKALQTVGM-LDYAQRSISQLSGGQQQ 148
Cdd:TIGR02323 79 ERRRLMRTEWGF---VHQNPRDGLRMRVSAGANIGERLmaigarhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRD 226
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQgRVVESGLTDQ 235
|
....*
gi 2786564536 227 IVGSP 231
Cdd:TIGR02323 236 VLDDP 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-168 |
1.45e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYD-DTVVLKDV---FFQieqGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKtvsayggvktnsiy 76
Cdd:PRK11819 9 MNRVSKVVPpKKQILKDIslsFFP---GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIK-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 77 nhIAYVPQTSAVDWDYpiTVFEVVLMGTYRRLGWFTR----------P-----------GK--------------RERDE 121
Cdd:PRK11819 72 --VGYLPQEPQLDPEK--TVRENVEEGVAEVKAALDRfneiyaayaePdadfdalaaeqGElqeiidaadawdldSQLEI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2786564536 122 ATKALQtvgmLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:PRK11819 148 AMDALR----CPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
27-217 |
1.46e-08 |
|
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: 52.99 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 27 TAIVGPNGAGKSTLVKAML----GLVPLveGTIELTLDAKTVsaygGVKTNSIYNHIAYvpqTSAVDWDYPIT----VFE 98
Cdd:cd03240 25 TLIVGQNGAGKTTIIEALKyaltGELPP--NSKGGAHDPKLI----REGEVRAQVKLAF---ENANGKKYTITrslaILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 99 VVLmgtYRRLGWFTRPGKRERDeatkalqtvgmldyaqrsisQLSGGQQQ------RVFLARALVENQDVYILDEPFKGI 172
Cdd:cd03240 96 NVI---FCHQGESNWPLLDMRG--------------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2786564536 173 DK-TTEAVLVKIMKDMQAAGKTLLIV--HHnlQTLEAYFDQVLCVNRR 217
Cdd:cd03240 153 DEeNIEESLAEIIEERKSQKNFQLIVitHD--EELVDAADHIYRVEKD 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-224 |
2.74e-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: 51.59 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 24 GTMTAIVGPNGAGKSTLVKAMlGLVplvegtieLTLDAKTVSAYGGVKTNSIynhIAYVpqtsavdwdypitvfEVVLMG 103
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDAI-GLA--------LGGAQSATRRRSGVKAGCI---VAAV---------------SAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 104 TyrrlgwftrpgkrerdeatkalqtvgmldyaqrsISQLSGGQQQRVFLARAL----VENQDVYILDEPFKGIDKTTEAV 179
Cdd:cd03227 74 T----------------------------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2786564536 180 LVKIMKDMQAAGKTLLIVHHNLQTLEAYfdqvlcvnRRLVGMGPV 224
Cdd:cd03227 120 LAEAILEHLVKGAQVIVITHLPELAELA--------DKLIHIKKV 156
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-223 |
4.09e-08 |
|
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: 53.48 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 126 LQTVGmLDY--AQRSISQLSGGQQQRVFLARAL------VenqdVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIV 197
Cdd:TIGR00630 472 LIDVG-LDYlsLSRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVV 546
|
90 100
....*....|....*....|....*.
gi 2786564536 198 HHNLQTLEAyfdqvlcvNRRLVGMGP 223
Cdd:TIGR00630 547 EHDEDTIRA--------ADYVIDIGP 564
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-199 |
4.20e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLvP---------LVEGTIELTLDAKTVSAYG------ 68
Cdd:CHL00131 13 LHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykilegdiLFKGESILDLEPEERAHLGiflafq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 69 ------GVkTNSIYNHIAY-----VPQTSAVDwdyPITVFEVVlmgtyrrlgwftrpgkrerdeaTKALQTVGMLD-YAQ 136
Cdd:CHL00131 92 ypieipGV-SNADFLRLAYnskrkFQGLPELD---PLEFLEII----------------------NEKLKLVGMDPsFLS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 137 RSISQ-LSGGQQQR-VFLARALVENQdVYILDEPFKGID----KTTEAVLVKIMKDMQAAgktLLIVHH 199
Cdd:CHL00131 146 RNVNEgFSGGEKKRnEILQMALLDSE-LAILDETDSGLDidalKIIAEGINKLMTSENSI---ILITHY 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
110-211 |
4.69e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.50 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 110 WFTRPGKRERdEATKALQTVGMLDY--AQRSIS-QLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKD 186
Cdd:PRK15093 125 WWQRFGWRKR-RAIELLHRVGIKDHkdAMRSFPyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTR 203
|
90 100
....*....|....*....|....*.
gi 2786564536 187 M-QAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:PRK15093 204 LnQNNNTTILLISHDLQMLSQWADKI 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-207 |
4.94e-08 |
|
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: 53.03 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGgvkTNSIYNHIAYVPQTSavdwd 91
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG--EIIIDGLNIAKIG---LHDLRFKITIIPQDP----- 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 ypitvfeVVLMGTYR-RLGWFtrpGKRERDEATKALQTVGMLDYAQ-----------RSISQLSGGQQQRVFLARALVEN 159
Cdd:TIGR00957 1370 -------VLFSGSLRmNLDPF---SQYSDEEVWWALELAHLKTFVSalpdkldhecaEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVKIMKdMQAAGKTLLIVHHNLQTLEAY 207
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDY 1486
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-211 |
6.94e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTI-----ELTLDAKTVSAYGGVKTnsI 75
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkEIDFKSSKEALENGISM--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 76 YNHIAYVPQTSAVD--WdypitvfevvlMGTYRRLGWFTRPGKRERDeaTKALQTVGMLDYAQR-SISQLSGGQQQRVFL 152
Cdd:PRK10982 79 HQELNLVLQRSVMDnmW-----------LGRYPTKGMFVDQDKMYRD--TKAIFDELDIDIDPRaKVATLSVSQMQMIEI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 153 ARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQV 211
Cdd:PRK10982 146 AKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEI 204
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-231 |
7.85e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAY-DDTVVLKDV---FFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPL----------VEGTIELTLDAKTVSA 66
Cdd:PRK11022 6 VDKLSVHFgDESAPFRAVdriSYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrvmaekleFNGQDLQRISEKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 67 YGGVKTNSIYNHiayvPQTS---AVDWDYPITVFEVVLMGTYRRlgwfTRpgkreRDEATKALQTVGMLDYAQR---SIS 140
Cdd:PRK11022 86 LVGAEVAMIFQD----PMTSlnpCYTVGFQIMEAIKVHQGGNKK----TR-----RQRAIDLLNQVGIPDPASRldvYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 141 QLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQ-AAGKTLLIVHHNLQTL-EAYFDQVLCVNRRL 218
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
250
....*....|...
gi 2786564536 219 VGMGPVRDIVGSP 231
Cdd:PRK11022 233 VETGKAHDIFRAP 245
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-233 |
1.11e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 136 QRSISQLSGGQQQRVFLARAL-VENQDV-YILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNlqtleayfDQVLC 213
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLgAELIGItYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQMIS 542
|
90 100
....*....|....*....|
gi 2786564536 214 VNRRLVGMGPVRDIVGSPIL 233
Cdd:PRK00635 543 LADRIIDIGPGAGIFGGEVL 562
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-205 |
1.15e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTI-----ELTLDAKTVSAYGGVKTNSI----YNHIAYVP 83
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHivfknEHTNDMTNEQDYQGDEEQNVgmknVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAVD------------------WDYPI----TVFEVVL-------MGTYRRLGWftrpGKRE--RDEATKALQTVGML 132
Cdd:PTZ00265 1263 EGGSGEdstvfknsgkilldgvdiCDYNLkdlrNLFSIVSqepmlfnMSIYENIKF----GKEDatREDVKRACKFAAID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 133 DYAQRSISQ-----------LSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQ-AAGKTLLIVHHN 200
Cdd:PTZ00265 1339 EFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHR 1418
|
....*
gi 2786564536 201 LQTLE 205
Cdd:PTZ00265 1419 IASIK 1423
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
124-201 |
1.52e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.57 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 124 KALQTVGmLDYAQ--RSISQLSGGQQQRVFLARALVENQD---VYILDEP-----FKGIDKtteavLVKIMKDMQAAGKT 193
Cdd:COG0178 808 QTLQDVG-LGYIKlgQPATTLSGGEAQRVKLASELSKRSTgktLYILDEPttglhFHDIRK-----LLEVLHRLVDKGNT 881
|
....*...
gi 2786564536 194 LLIVHHNL 201
Cdd:COG0178 882 VVVIEHNL 889
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-187 |
2.70e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGlvplveGTIELTLDAKTVSAYGGVKTNSIYNH----IAYVPQTsav 88
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS------NTDGFHIGVEGVITYDGITPEEIKKHyrgdVVYNAET--- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 89 DWDYP-ITVFEvVLMGTYRRLGWFTRPGKRERDEATKALQTVGMLDYAQRS----------ISQLSGGQQQRVFLARALV 157
Cdd:TIGR00956 147 DVHFPhLTVGE-TLDFAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHtrntkvgndfVRGVSGGERKRVSIAEASL 225
|
170 180 190
....*....|....*....|....*....|
gi 2786564536 158 ENQDVYILDEPFKGIDKTTEAVLVKIMKDM 187
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTS 255
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-197 |
3.04e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 3.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 138 SISQ----LSGGQQQRVFLARALVENQDVYILDEPFKGIDktteaVLVK-----IMKDMQAAGKTLLIV 197
Cdd:NF040905 397 SVFQkvgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID-----VGAKyeiytIINELAAEGKGVIVI 460
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-216 |
4.39e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.52 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 1 MNHLSVAYDDTV--VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAyggVKTNSIYNH 78
Cdd:cd03288 22 IHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI--VIDGIDISK---LPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 79 IAYVPQTSavdwdypitvfeVVLMGTYRrlgWFTRPGKRERD----EATKALQTVGM-------LD-YAQRSISQLSGGQ 146
Cdd:cd03288 97 LSIILQDP------------ILFSGSIR---FNLDPECKCTDdrlwEALEIAQLKNMvkslpggLDaVVTEGGENFSVGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786564536 147 QQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMkdMQA-AGKTLLIVHHNLQT-LEAyfDQVLCVNR 216
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAfADRTVVTIAHRVSTiLDA--DLVLVLSR 229
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-201 |
4.55e-07 |
|
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: 50.01 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 124 KALQTVGmLDYAQ--RSISQLSGGQQQRVFLARAL---VENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVH 198
Cdd:TIGR00630 811 QTLCDVG-LGYIRlgQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIE 889
|
...
gi 2786564536 199 HNL 201
Cdd:TIGR00630 890 HNL 892
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
18-215 |
5.15e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.80 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 18 FFQIEQGTMTAIVGPNGAGKSTLvkamlglvplvegtieltLDAKTVSAYGGV----KTNSIYNHIAYVPQTSAVDWDYP 93
Cdd:cd03279 22 FTGLDNNGLFLICGPTGAGKSTI------------------LDAITYALYGKTprygRQENLRSVFAPGEDTAEVSFTFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITvfevvlMGTYRrlgwFTRPGKRERDEATKALqtvgML------DYAQRSISQLSGGQQQRVFLARAL-----VENQ-- 160
Cdd:cd03279 84 LG------GKKYR----VERSRGLDYDQFTRIV----LLpqgefdRFLARPVSTLSGGETFLASLSLALalsevLQNRgg 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 161 ---DVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHnLQTLEAYFDQVLCVN 215
Cdd:cd03279 150 arlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH-VEELKERIPQRLEVI 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-221 |
6.16e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGGVKtnSIYNHIAYVPQ---TSAVDW 90
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI--TLHGKKINNHNANE--AINHGFALVTEerrSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 DYPITVFEVVL-MGTYRRlGWFTRPGKRERDEATKALQTVGMLDYAQR-SISQLSGGQQQRVFLARALVENQDVYILDEP 168
Cdd:PRK10982 340 YLDIGFNSLISnIRNYKN-KVGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2786564536 169 FKGIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAYFDQVLCV-NRRLVGM 221
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMsNGLVAGI 472
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-201 |
6.25e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 121 EATKALQTVGmLDYAQ--RSISQLSGGQQQRVFLARAL---VENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLL 195
Cdd:PRK00635 788 EKIHALCSLG-LDYLPlgRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVV 866
|
....*.
gi 2786564536 196 IVHHNL 201
Cdd:PRK00635 867 IIEHNM 872
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-204 |
7.57e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 13 VLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIelTLDAKTVSAYGgvkTNSIYNHIAYVPQTSavdwdy 92
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI--LIDGCDISKFG---LMDLRKVLGIIPQAP------ 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 93 pitvfeVVLMGTYRrlgwFTRPGKRERDEAT--KALQTVGMLDYAQRSISQL-----------SGGQQQRVFLARALVEN 159
Cdd:PLN03130 1323 ------VLFSGTVR----FNLDPFNEHNDADlwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRR 1392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2786564536 160 QDVYILDEPFKGIDKTTEAVLVK-IMKDMQAAgkTLLIVHHNLQTL 204
Cdd:PLN03130 1393 SKILVLDEATAAVDVRTDALIQKtIREEFKSC--TMLIIAHRLNTI 1436
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
21-214 |
9.80e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 21 IEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAktvsayggvktnsiynhIAYVPQTSavdwdypitvfevv 100
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-----------------PVYKPQYI-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 101 lmgtyrrlgwftrpgkrerdeatkalqtvgmldyaqrsisQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVL 180
Cdd:cd03222 71 ----------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA 110
|
170 180 190
....*....|....*....|....*....|....*
gi 2786564536 181 VKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQVLCV 214
Cdd:cd03222 111 ARAIRRLsEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-231 |
1.05e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 20 QIEQGTMTAIVGPNGAGKSTLVKAMLGLVPlvegtieltlDAKTVSA----YGGV---------KTNSIYNHIAYV---P 83
Cdd:COG4170 29 TLNEGEIRGLVGESGSGKSLIAKAICGITK----------DNWHVTAdrfrWNGIdllklspreRRKIIGREIAMIfqeP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 84 QTSAvdwDYPITVF----EVVLMGTYRRLgWFTRPGKRERdEATKALQTVGMLDYAQ--RSIS-QLSGGQQQRVFLARAL 156
Cdd:COG4170 99 SSCL---DPSAKIGdqliEAIPSWTFKGK-WWQRFKWRKK-RAIELLHRVGIKDHKDimNSYPhELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786564536 157 VENQDVYILDEPFKGIDKTTEAVLVKIMKDM-QAAGKTLLIVHHNLQTLEAYFDQ--VL-CvnRRLVGMGPVRDIVGSP 231
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTitVLyC--GQTVESGPTEQILKSP 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-231 |
1.07e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 10 DTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVP---------LVEGTIELTLDAKTVSAYGGVKTNSIYNHia 80
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangriggsaTFNGREILNLPEKELNKLRAEQISMIFQD-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 yvPQTSavdwdypitvfevvlMGTYRRLG--------WFTRPGKRER-DEATKALQTVGMLDyAQRSIS----QLSGGQQ 147
Cdd:PRK09473 106 --PMTS---------------LNPYMRVGeqlmevlmLHKGMSKAEAfEESVRMLDAVKMPE-ARKRMKmyphEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 148 QRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLI-VHHNLQTLEAYFDQVLCVNR-RLVGMGPVR 225
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAgRTMEYGNAR 247
|
....*.
gi 2786564536 226 DIVGSP 231
Cdd:PRK09473 248 DVFYQP 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-231 |
1.13e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 4 LSVAYDD----TVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIE-------------LTLDAKTVSA 66
Cdd:PRK10261 18 LNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvIELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 67 YGGVKTNSIynhiAYVPQTSAVDWDYPITVFEVVLMGTYRRLGWftrPGKRERDEATKALQTVGMLDyAQRSIS----QL 142
Cdd:PRK10261 98 MRHVRGADM----AMIFQEPMTSLNPVFTVGEQIAESIRLHQGA---SREEAMVEAKRMLDQVRIPE-AQTILSryphQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 143 SGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLLI-VHHNLQTLEAYFDQVLCVNR-RLVG 220
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQgEAVE 249
|
250
....*....|.
gi 2786564536 221 MGPVRDIVGSP 231
Cdd:PRK10261 250 TGSVEQIFHAP 260
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
116-227 |
2.67e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 116 KRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAAGKTLL 195
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVL 198
|
90 100 110
....*....|....*....|....*....|...
gi 2786564536 196 IVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDI 227
Cdd:NF000106 199 LTTQYMEEAEQLAHELTVIDRgRVIADGKVDEL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
23-201 |
4.82e-06 |
|
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: 45.06 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 23 QGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIeLTLDAktvsayggvktnsiynhiayvpqtsavdwdypitvfevvlm 102
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-IYIDG----------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 103 gtyrrlgwftrpgkrerDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVK 182
Cdd:smart00382 39 -----------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180
....*....|....*....|....
gi 2786564536 183 I-----MKDMQAAGKTLLIVHHNL 201
Cdd:smart00382 102 LeelrlLLLLKSEKNLTVILTTND 125
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-201 |
6.84e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.69 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 2 NHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTL-DAKTVSAYGgvKTNSIYNHIA 80
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrDGQLRDLYA--LSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 81 -----YVPQTSAVDWDYPITVFEVV---LMGtyrrLGWftRPGKRERDEATKALQTV----GMLDYAQRSisqLSGGQQQ 148
Cdd:PRK11701 88 rtewgFVHQHPRDGLRMQVSAGGNIgerLMA----VGA--RHYGDIRATAGDWLERVeidaARIDDLPTT---FSGGMQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 149 RVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMK----DMQAAgktLLIVHHNL 201
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRglvrELGLA---VVIVTHDL 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-212 |
8.83e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLvkamlglvplvegtieLTLDAKTVSAYGGVKTNSIYNHIAYVPQ-TSAVDw 90
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTL----------------LALLKNEISADGGSYTFPGNWQLAWVNQeTPALP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 91 dypITVFEVVLMG--TYRRLgwftrpgKRERDEATK-----ALQTV-GMLDYAQ-----------------------RSI 139
Cdd:PRK10636 78 ---QPALEYVIDGdrEYRQL-------EAQLHDANErndghAIATIhGKLDAIDawtirsraasllhglgfsneqleRPV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786564536 140 SQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTTEAVLVKIMKDMQAagkTLLIVHHNLQTLEAYFDQVL 212
Cdd:PRK10636 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKII 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-201 |
9.07e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAYGGVKTnsiynhiayvpQTSAVDwdyp 93
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSG-----------QLTGIE---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 94 ITVFEVVLMGtyrrlgwFTRpgKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGID 173
Cdd:PRK13546 105 NIEFKMLCMG-------FKR--KEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180
....*....|....*....|....*....
gi 2786564536 174 KT-TEAVLVKIMkDMQAAGKTLLIVHHNL 201
Cdd:PRK13546 176 QTfAQKCLDKIY-EFKEQNKTIFFVSHNL 203
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
126-223 |
1.23e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 126 LQTVGmLDYA--QRSISQLSGGQQQRVFLARA----LVenqDV-YILDEPFKG-----IDKtteavLVKIMKDMQAAGKT 193
Cdd:COG0178 469 LVDVG-LDYLtlDRSAGTLSGGEAQRIRLATQigsgLV---GVlYVLDEPSIGlhqrdNDR-----LIETLKRLRDLGNT 539
|
90 100 110
....*....|....*....|....*....|.
gi 2786564536 194 LLIVHHNLQT-LEAyfDqvlcvnrRLVGMGP 223
Cdd:COG0178 540 VIVVEHDEDTiRAA--D-------YIIDIGP 561
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-173 |
1.44e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 3 HLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKaML-GLVPLVEGTIEL---TLDAKTVSAYGGV----KTNS 74
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMK-MLtGLLPASEGEAWLfgqPVDAGDIATRRRVgymsQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 75 IYNHiayvpqtsavdwdypITVFE-VVLmgtYRRLgwFTRPGKRERDEATKALQTVGMLDYAQRSISQLSGGQQQRVFLA 153
Cdd:NF033858 350 LYGE---------------LTVRQnLEL---HARL--FHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA 409
|
170 180
....*....|....*....|
gi 2786564536 154 RALVENQDVYILDEPFKGID 173
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVD 429
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-233 |
4.75e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.71 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 27 TAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL---TLdaktVSAYGGVKTNSIYNHIAYVPQtsavdwdypitvfEVVLMG 103
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLngrVL----FDAEKGICLPPEKRRIGYVFQ-------------DARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 104 TYRRLGWFtRPGKRERDEAtKALQTVGMLDYA---QRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGID----KTT 176
Cdd:PRK11144 90 HYKVRGNL-RYGMAKSMVA-QFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786564536 177 EAVLVKIMKDMQAAgktLLIVHHNLQTLEAYFDQVLCVNR-RLVGMGPVRDIVGSPIL 233
Cdd:PRK11144 168 LPYLERLAREINIP---ILYVSHSLDEILRLADRVVVLEQgKVKAFGPLEEVWASSAM 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-57 |
4.98e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 4.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIEL 57
Cdd:PRK10636 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-231 |
5.10e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGtiELTLDAKTVSAYGgvkTNSIYNHIAYVPQTSavdwd 91
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGG--EIRVNGREIGAYG---LRELRRQFSMIPQDP----- 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 ypitvfeVVLMGTYRR-LGWFTRPGKrerDEATKALQTVGMLDY-----------AQRSISQLSGGQQQRVFLARALVEN 159
Cdd:PTZ00243 1394 -------VLFDGTVRQnVDPFLEASS---AEVWAALELVGLRERvasesegidsrVLEGGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 160 QDVYIL-DEPFKGIDKTTEavlvkimKDMQA------AGKTLLIVHHNLQTLeAYFDQVLCVNRRLVG-MGPVRDIVGSP 231
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALD-------RQIQAtvmsafSAYTVITIAHRLHTV-AQYDKIIVMDHGAVAeMGSPRELVMNR 1535
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
14-207 |
7.73e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 14 LKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGLVPLVEGTIELTLDAKTVSAYGGV--KTNSIYNhiayvpqtsavdwd 91
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLngQLTGIEN-------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 ypiTVFEVVLMGTyrrlgwftrpGKRERDEAT-KALQTVGMLDYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:PRK13545 106 ---IELKGLMMGL----------TKEKIKEIIpEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAAGKTLLIVHHNLQTLEAY 207
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSF 209
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
124-201 |
1.40e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 124 KALQTVGmLDYAQ--RSISQLSGGQQQRVFLARALVEN---QDVYILDEP-----FKGIDKtteavLVKIMKDMQAAGKT 193
Cdd:PRK00349 812 QTLVDVG-LGYIKlgQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPttglhFEDIRK-----LLEVLHRLVDKGNT 885
|
....*...
gi 2786564536 194 LLIVHHNL 201
Cdd:PRK00349 886 VVVIEHNL 893
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-215 |
1.71e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 12 VVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLGlvplvegtiELTLDAKTVSAYGGVKTNSIYNHIAYVPQTSAVDWD 91
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG---------ELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 92 YPITVFEVVLMGTYR-RLGWFTRPGkrerdeaTKALQtvgmldyaqrSISQLSGGQQQRVFLARALVENQDVYILDEPFK 170
Cdd:PLN03073 594 YMMRCFPGVPEQKLRaHLGSFGVTG-------NLALQ----------PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2786564536 171 GIDKTTEAVLVKIMKDMQAAgktLLIVHHNLQTLEAYFDQVLCVN 215
Cdd:PLN03073 657 HLDLDAVEALIQGLVLFQGG---VLMVSHDEHLISGSVDELWVVS 698
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-46 |
1.90e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 1.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2786564536 1 MNHLSVAYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAMLG 46
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
21-49 |
4.93e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 4.93e-04
10 20 30
....*....|....*....|....*....|
gi 2786564536 21 IEQGTMTAIVGPNGAGKSTLVKAMLG-LVP 49
Cdd:pfam13555 19 IDPRGNTLLTGPSGSGKSTLLDAIQTlLVP 48
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
14-44 |
6.36e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 6.36e-04
10 20 30
....*....|....*....|....*....|.
gi 2786564536 14 LKDVFFQIEQGtMTAIVGPNGAGKSTLVKAM 44
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
19-45 |
6.75e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.37 E-value: 6.75e-04
10 20
....*....|....*....|....*..
gi 2786564536 19 FQIEQGtMTAIVGPNGAGKSTLVKAML 45
Cdd:cd03278 18 IPFPPG-LTAIVGPNGSGKSNIIDAIR 43
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-44 |
1.29e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.26 E-value: 1.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2786564536 2 NHLSvaYDDTVVLKDVFFQIEQGTMTAIVGPNGAGKSTLVKAM 44
Cdd:COG1106 9 NFRS--FKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEAL 49
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
14-44 |
1.35e-03 |
|
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: 39.22 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|.
gi 2786564536 14 LKDVFFQIEQGtMTAIVGPNGAGKSTLVKAM 44
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEAL 43
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
26-45 |
1.71e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.18 E-value: 1.71e-03
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-47 |
1.75e-03 |
|
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: 38.91 E-value: 1.75e-03
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-43 |
1.80e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 1.80e-03
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-45 |
1.82e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 1.82e-03
10 20
....*....|....*....|....*..
gi 2786564536 19 FQIEQGtMTAIVGPNGAGKSTLVKAML 45
Cdd:COG1196 20 IPFEPG-ITAIVGPNGSGKSNIVDAIR 45
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
27-167 |
2.71e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 27 TAIVGPNGAGKSTLVKAmlglvplvegtIELTLDAKTVSayggvkTNSIYNHIAYVPQTSA---VDWDYPITVFEVV--- 100
Cdd:COG0419 26 NLIVGPNGAGKSTILEA-----------IRYALYGKARS------RSKLRSDLINVGSEEAsveLEFEHGGKRYRIErrq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 101 --------------------LMGTyRRLGWFTRPGKRERDEATKALQTVGMLDYAQR----------SISQLSGGQQQRV 150
Cdd:COG0419 89 gefaefleakpserkealkrLLGL-EIYEELKERLKELEEALESALEELAELQKLKQeilaqlsgldPIETLSGGERLRL 167
|
170
....*....|....*..
gi 2786564536 151 FLARALVENQDVYILDE 167
Cdd:COG0419 168 ALADLLSLILDFGSLDE 184
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
23-45 |
4.03e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 37.38 E-value: 4.03e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-220 |
4.42e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 133 DYAQRSISQLSGGQQQRVFLARALVENQDVYILDEPFKGIDKTT----EAVLVKimkdmqaAGKTLLIVHHNLQTLEAYF 208
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAvlwlETYLLK-------WPKTFIVVSHAREFLNTVV 408
|
90
....*....|...
gi 2786564536 209 DQVLCV-NRRLVG 220
Cdd:PLN03073 409 TDILHLhGQKLVT 421
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
26-43 |
7.21e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.22 E-value: 7.21e-03
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
26-44 |
7.44e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.90 E-value: 7.44e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
24-49 |
7.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.20 E-value: 7.52e-03
10 20
....*....|....*....|....*..
gi 2786564536 24 GTMTAIVGPNGAGKSTLVKAML-GLVP 49
Cdd:COG4913 24 GRGTLLTGDNGSGKSTLLDAIQtLLVP 50
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
27-45 |
7.68e-03 |
|
ATP-binding cassette domain of eukaryotic SMC4 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: 213241 [Multi-domain] Cd Length: 212 Bit Score: 36.51 E-value: 7.68e-03
|
| COG4185 |
COG4185 |
Predicted ABC-type ATPase or kinase [General function prediction only]; |
22-45 |
8.10e-03 |
|
Predicted ABC-type ATPase or kinase [General function prediction only];
Pssm-ID: 443339 Cd Length: 197 Bit Score: 36.40 E-value: 8.10e-03
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
23-49 |
8.21e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 36.20 E-value: 8.21e-03
10 20
....*....|....*....|....*..
gi 2786564536 23 QGTMTAIVGPNGAGKSTLVKAMLGLVP 49
Cdd:COG0194 1 RGKLIVLSGPSGAGKTTLVKALLERDP 27
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
28-67 |
8.32e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 36.42 E-value: 8.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2786564536 28 AIVGPNGAGKSTLVKAMLGLVPLVE--GTIEltlDAKTVSAY 67
Cdd:cd04170 3 ALVGHSGSGKTTLAEALLYATGAIDrlGRVE---DGNTVSDY 41
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
126-206 |
9.05e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 36.97 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786564536 126 LQTVGmLDY--AQRSISQLSGGQQQRVFLA----RALVenqDV-YILDEPFKGI-----DKtteavLVKIMKDMQAAGKT 193
Cdd:PRK00349 473 LVDVG-LDYltLSRSAGTLSGGEAQRIRLAtqigSGLT---GVlYVLDEPSIGLhqrdnDR-----LIETLKHLRDLGNT 543
|
90
....*....|...
gi 2786564536 194 LLIVHHNLQTLEA 206
Cdd:PRK00349 544 LIVVEHDEDTIRA 556
|
|
| |
