|
Name |
Accession |
Description |
Interval |
E-value |
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-232 |
7.02e-139 |
|
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: 388.72 E-value: 7.02e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRGANIGIVFQSFHLIPNMTALENVAVPLELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAEPVQGA 232
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-227 |
5.41e-112 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 320.45 E-value: 5.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRGANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-225 |
1.40e-106 |
|
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: 306.72 E-value: 1.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFR 89
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-233 |
2.81e-77 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 232.64 E-value: 2.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:COG2884 1 MIRFENVSKRYPG---GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQReNGLTMVLVTHDPSLAARCD-REIPVRSGRIAEPVQGAG 233
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-227 |
5.37e-77 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 231.98 E-value: 5.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RGANIGIVFQSFHLIPNMTALENVAVPLELAGR--RDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGEssRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
28-227 |
1.25e-75 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 228.39 E-value: 1.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHLIPNMT 107
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQ 185
Cdd:TIGR02211 100 ALENVAMPLLIGKksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489055174 186 IADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:TIGR02211 180 IFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
7.60e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 222.66 E-value: 7.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 1 MTEKlvGPIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQm 80
Cdd:COG1116 1 MSAA--APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 81 sedqaaafRGANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAI 158
Cdd:COG1116 78 --------PGPDRGVVFQEPALLPWLTVLDNVALGLELRGvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 159 ARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDReIPV---RSGRIAE 227
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADR-VVVlsaRPGRIVE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-227 |
1.10e-71 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 218.71 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqMSEDQAAAF 88
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVAVPLELA---GRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVkkmSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 166 PKILIADEPTGNLD-------TATGRQIAdllfakqrENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG1126 155 PKVMLFDEPTSALDpelvgevLDVMRDLA--------KEGMTMVVVTHEMGFAREvADRVVFMDGGRIVE 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-227 |
3.21e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 221.10 E-value: 3.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVAVPLELAGrrdaFDVAERELRA------VGLGERLTHYPSELSGGEQQRVAIARAL 162
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAG----VPKAEIRKRVaellelVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 163 APSPKILIADEPTGNLDTATGRQIADLLfaKQ--RENGLTMVLVTHDPSLAAR-CDReipV---RSGRIAE 227
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLL--KDinRELGLTIVLITHEMDVVRRiCDR---VavlENGRIVE 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-227 |
3.47e-71 |
|
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: 217.45 E-value: 3.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVAVPLELAGRRDAfDVAERE---LRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKA-EIEERVlelLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-227 |
1.12e-70 |
|
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: 216.59 E-value: 1.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMsedQAAAFR 89
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR---RRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GaNIGIVFQ----SFHliPNMTALENVAVPLELAGRRDAFDVAERELRAVGLGER-LTHYPSELSGGEQQRVAIARALAP 164
Cdd:COG1124 79 R-RVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVE 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-225 |
4.06e-68 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 209.91 E-value: 4.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLghaASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRgANIGIVFQSFHLIPNMTALENVavpleLAGR----------RDAFDVAERE-----LRAVGLGERLTHYPSELSGGE 152
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSVLTNV-----LAGRlgrtstwrslLGLFPPEDREraleaLERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 153 QQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-227 |
1.32e-67 |
|
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: 208.13 E-value: 1.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAf 88
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RGANIGIVFQ----SFHliPNMTALENVAVPLELAGRRDAFDVAER----ELRAVGLGE-RLTHYPSELSGGEQQRVAIA 159
Cdd:cd03257 80 RRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEavllLLVGVGLPEeVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 160 RALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-227 |
1.73e-67 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 207.32 E-value: 1.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmsedqaaafR 89
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPV--RSGRIAE 227
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLsaRPGRIVA 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-213 |
5.07e-66 |
|
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: 203.63 E-value: 5.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGhaaSSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:TIGR02673 1 MIEFHNVSKAYP---GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVAVPLELAGR--RDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKkeREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLfakQREN--GLTMVLVTHDPSLAAR 213
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLL---KRLNkrGTTVIVATHDLSLVDR 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-226 |
2.67e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 206.10 E-value: 2.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAA 86
Cdd:COG3842 3 MPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 AFRgaNIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAP 164
Cdd:COG3842 75 EKR--NVGMVFQDYALFPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDP----SLAarcDReIPV-RSGRIA 226
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQeealALA---DR-IAVmNDGRIE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-227 |
9.88e-65 |
|
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: 209.37 E-value: 9.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLT-LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAA 86
Cdd:COG1123 259 PLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 AFRGaNIGIVFQS-FH-LIPNMTALENVAVPLELAGRRDAFDVAER---ELRAVGLGERLTH-YPSELSGGEQQRVAIAR 160
Cdd:COG1123 339 ELRR-RVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSRAERRERvaeLLERVGLPPDLADrYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 161 ALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-216 |
2.44e-64 |
|
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: 200.21 E-value: 2.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG1127 4 PMIEVRNLTKSFG----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRgANIGIVFQSFHLIPNMTALENVAVPLELAGR---RDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAP 164
Cdd:COG1127 80 LR-RRIGMLFQGGALFDSLTVFENVAFPLREHTDlseAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD-PSLAARCDR 216
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADR 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-227 |
6.90e-64 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 198.13 E-value: 6.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafR 89
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gaNIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLKLRGvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-226 |
5.70e-61 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 191.63 E-value: 5.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFR 89
Cdd:cd03256 1 IEVENLSKTYPN---GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVavpleLAGRRDA----------FDVAERE-----LRAVGLGERLTHYPSELSGGEQQ 154
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENV-----LSGRLGRrstwrslfglFPKEEKQralaaLERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-227 |
6.51e-61 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 194.63 E-value: 6.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFR 89
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPLELAGRRDAfDVAER--ELRA-VGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKA-EIKARvtELLElVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
9-226 |
1.27e-60 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 190.23 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVAVPLELA---GRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALELQpnlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIA 226
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-225 |
1.03e-59 |
|
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: 188.09 E-value: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAassvHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFR 89
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPLELAGRRDA---FDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-216 |
4.25e-59 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 189.49 E-value: 4.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLE---HVDNGIVKIAGETISQMSEDQA 85
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 AAFRGANIGIVFQ----SFHliPNMTALENVAVPLEL---AGRRDAFDVAERELRAVGL---GERLTHYPSELSGGEQQR 155
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIhggLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 156 VAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDR 216
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADR 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-225 |
4.70e-59 |
|
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: 185.81 E-value: 4.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAassvHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmSEDQAAAFR 89
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAV-PLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQREnGLTMVLVTHDPSLA-ARCDREIPVRSGRI 225
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
27-218 |
4.73e-59 |
|
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: 185.51 E-value: 4.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHLIPNM 106
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENVAVPLELAGR--RDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:TIGR03608 92 TVEENLDLGLKYKKLskKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....
gi 489055174 185 QIADLLFaKQRENGLTMVLVTHDPSLAARCDREI 218
Cdd:TIGR03608 172 EVLDLLL-ELNDEGKTIIIVTHDPEVAKQADRVI 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-225 |
4.98e-59 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 186.56 E-value: 4.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 25 SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHLIP 104
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 NMTALENVAVPLELAGRR--DAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTAT 182
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489055174 183 GRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-227 |
9.79e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 183.37 E-value: 9.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RGAniGIVFQSFHLIPNMTALENVAV-PLEL--AGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:PRK09493 77 QEA--GMVFQQFYLFPHLTALENVMFgPLRVrgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 166 PKILIADEPTGNLDTATgRQIADLLFAKQRENGLTMVLVTHDPSLAARC-DREIPVRSGRIAE 227
Cdd:PRK09493 155 PKLMLFDEPTSALDPEL-RHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAE 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-227 |
5.18e-57 |
|
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: 188.96 E-value: 5.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDvhLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL---EHVDNGIVKIAGETISQMSEdq 84
Cdd:COG1123 3 PLLEVRD--LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 85 aaAFRGANIGIVFQSF--HLIPnMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIAR 160
Cdd:COG1123 79 --ALRGRRIGMVFQDPmtQLNP-VTVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 161 ALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVE 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-240 |
7.56e-56 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 188.78 E-value: 7.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRGANIGIVFQSFHLIPNMTALENVAVPLELAGrrdaFDVAERELRAV------GLGERLTHYPSELSGGEQQRVAIARA 161
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAG----LERKQRLLRAQellqrlGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLfaKQ-RENGLTMVLVTHDPSLAARCDREIPVRSGRI--------AEPVQGA 232
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAIL--HQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIvrnppaqeKVNVAGG 236
|
....*...
gi 489055174 233 GIPETQAV 240
Cdd:PRK10535 237 TEPVVNTA 244
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-225 |
2.07e-55 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 180.65 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFR 89
Cdd:COG3839 4 LELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT----DLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gaNIGIVFQSFHLIPNMTALENVAVPLELAGRRDAfDVAER--E-LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKA-EIDRRvrEaAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 167 KILIADEPTGNLD----TATGRQIADLlfakQRENGLTMVLVTHDP----SLAarcDReIPV-RSGRI 225
Cdd:COG3839 153 KVFLLDEPLSNLDaklrVEMRAEIKRL----HRRLGTTTIYVTHDQveamTLA---DR-IAVmNDGRI 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-226 |
4.80e-55 |
|
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: 175.98 E-value: 4.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTlghAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmsEDQAAAFR 89
Cdd:COG1122 1 IELENLSFS---YPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQ-SFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:COG1122 75 -RKVGLVFQnPDDQLFAPTVEEDVAFGPENLGlpREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIV 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-224 |
1.67e-54 |
|
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: 173.14 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMsEDQAAAFR 89
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPlelagrrdafdvaerelravglgerlthypseLSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03229 76 -RRIGMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGR 224
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-224 |
6.38e-54 |
|
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: 172.65 E-value: 6.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGHAASSVhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafRG 90
Cdd:cd03225 1 ELKNLSFSYPDGARPA--LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 ANIGIVFQ-SFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:cd03225 75 RKVGLVFQnPDDQFFGPTVEEEVAFGLENLGlpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGR 224
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-225 |
9.30e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.92 E-value: 9.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFR 89
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNmTALENVAVPLELAGRRDAFDVAERELRAVGLGERLTHYP-SELSGGEQQRVAIARALAPSPKI 168
Cdd:COG4619 74 -RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 169 LIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-227 |
1.45e-53 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 176.11 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmseDQAAAFR 89
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT---NLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gaNIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:COG1118 76 --RVGFVFQHYALFPHMTVAENIAFGLRVRPpsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQ 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-236 |
2.55e-53 |
|
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: 172.83 E-value: 2.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHLIPNMTALEN 111
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 112 VAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADL 189
Cdd:cd03294 123 VAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 190 LFAKQRENGLTMVLVTHDPSLAARC-DREIPVRSGRIaepVQgAGIPE 236
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRL---VQ-VGTPE 246
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-225 |
3.93e-53 |
|
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: 170.67 E-value: 3.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVHvlkGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFR 89
Cdd:cd03292 1 IEFINVTKTYPNGTAALD---GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPLEL--AGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 168 ILIADEPTGNLDTATGRQIADlLFAKQRENGLTMVLVTHDPSLAARCD-REIPVRSGRI 225
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
9-225 |
4.97e-51 |
|
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: 166.32 E-value: 4.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGhaaSSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVavpleLAGRRDA----------FDVAERE-----LRAVGLGERLTHYPSELSGGEQ 153
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENV-----LHGRLGYkptwrsllgrFSEEDKEralsaLERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 154 QRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEI 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-226 |
9.54e-51 |
|
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: 165.99 E-value: 9.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAaf 88
Cdd:COG1120 1 MLEAENLSVGYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 rgANIGIVFQSFHLIPNMTALENVAV-------PLELAGRRDAfDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARA 161
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIV 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-211 |
1.21e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 165.74 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 1 MTEKLVgPIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsQM 80
Cdd:COG4598 1 MTDTAP-PALEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 81 SEDQAAAFRGAN----------IGIVFQSFHLIPNMTALENV-AVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSE 147
Cdd:COG4598 75 KPDRDGELVPADrrqlqrirtrLGMVFQSFNLWSHMTVLENViEAPVHVLGrpKAEAIERAEALLAKVGLADKRDAYPAH 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 148 LSGGEQQRVAIARALAPSPKILIADEPTGNLDT-------ATGRQIAdllfakqrENGLTMVLVTHDPSLA 211
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPelvgevlKVMRDLA--------EEGRTMLVVTHEMGFA 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-225 |
6.32e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.31 E-value: 6.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsqmsEDQAAAFR 89
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGlpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELL-RELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRI 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-225 |
8.31e-50 |
|
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: 162.79 E-value: 8.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAaafr 89
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gaNIGIVFQSFHLIPNMTALENVAVPLELAGRRDAfDVAER---ELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA-EIKERvaeALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRI 225
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-216 |
6.47e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.02 E-value: 6.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmsedqaaa 87
Cdd:COG1121 5 PAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 fRGANIGIVFQSFHLIPN--MTALENVA------VPLELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIA 159
Cdd:COG1121 73 -ARRRIGYVPQRAEVDWDfpITVRDVVLmgrygrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 160 RALAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDR 216
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREyFDR 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-227 |
8.42e-49 |
|
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: 167.94 E-value: 8.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKS----TLLMVLAGLEHVDNGIVKIAGETISQMSED 83
Cdd:COG4172 5 PLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 84 QAAAFRGANIGIVFQSfhliPnMTAL-------ENVAVPLEL---AGRRDAFDVAERELRAVGLGE---RLTHYPSELSG 150
Cdd:COG4172 85 ELRRIRGNRIAMIFQE----P-MTSLnplhtigKQIAEVLRLhrgLSGAAARARALELLERVGIPDperRLDAYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 151 GEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-227 |
1.07e-48 |
|
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: 170.01 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFR 89
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVAVplelaGRRDA-FDVAERELRAVGLGERLTHYP-----------SELSGGEQQRVA 157
Cdd:COG2274 549 -RQIGVVLQDVFLF-SGTIRENITL-----GDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-225 |
1.14e-48 |
|
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: 159.34 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFR 89
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT----DLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gaNIGIVFQSFHLIPNMTALENVAVPLELAGRRDAfDVAERELRA---VGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:cd03301 73 --DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKD-EIDERVREVaelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRI 225
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-227 |
1.08e-47 |
|
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: 157.34 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDvhltLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHV-----DNGIVKIAGETISQMSEDQ 84
Cdd:cd03260 1 IELRD----LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 85 AAAFRgaNIGIVFQSFHLIPnMTALENVAVPLELAGRRDAFDVAERE---LRAVGLGERL---THyPSELSGGEQQRVAI 158
Cdd:cd03260 77 LELRR--RVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVeeaLRKAALWDEVkdrLH-ALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 159 ARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREngLTMVLVTHDPSLAARC-DREIPVRSGRIAE 227
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVE 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-207 |
1.99e-47 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 157.72 E-value: 1.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmsedqaaa 87
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 fRGANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:COG4525 74 -PGADRGVVFQKDALLPWLNVLDNVAFGLRLRGvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-227 |
2.57e-47 |
|
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: 164.55 E-value: 2.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAA 86
Cdd:COG4987 331 GPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 afrgANIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDVAERE-LRAVGLGERLTHYP-----------SELSGGEQQ 154
Cdd:COG4987 409 ----RRIAVVPQRPHLF-DTTLRENLRL-----ARPDATDEELWAaLERVGLGDWLAALPdgldtwlgeggRRLSGGERR 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFA--KQRenglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEalAGR----TVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
29-225 |
3.41e-47 |
|
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: 156.35 E-value: 3.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaaaFRGANIGIVFQSFHLIPNMTA 108
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERNVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LENVAVPLELAGRRDAFDVAERELRAV---------GLGERlthYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:cd03296 92 FDNVAFGLRVKPRSERPPEAEIRAKVHellklvqldWLADR---YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 180 TATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-227 |
6.99e-47 |
|
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: 155.79 E-value: 6.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETisqmSEDQAAAFR 89
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGlfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVA 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-224 |
9.21e-47 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 152.92 E-value: 9.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaAFR 89
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE---SLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVavplelagrrdafdvaerelravglgerlthypseLSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03228 76 -KNIAYVPQDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAkqRENGLTMVLVTHDPSLAARCDREIPVRSGR 224
Cdd:cd03228 119 ILDEATSALDPETEALILEALRA--LAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-237 |
9.77e-47 |
|
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: 157.66 E-value: 9.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 44 IVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMsedqAAAFRGanIGIVFQSFHLIPNMTALENVAVPLELAGRrD 123
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV----PPHLRH--INMVFQSYALFPHMTVEENVAFGLKMRKV-P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 124 AFDVAER---ELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLT 200
Cdd:TIGR01187 74 RAEIKPRvleALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 489055174 201 MVLVTHDPSLA-ARCDREIPVRSGRIAEpvqgAGIPET 237
Cdd:TIGR01187 154 FVFVTHDQEEAmTMSDRIAIMRKGKIAQ----IGTPEE 187
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-175 |
1.05e-46 |
|
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: 152.03 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaaAFRGANIGIVFQSFHLIPNMTA 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 109 LENVAVPLELAG--RRDAFDVAERELRAVGLG----ERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPT 175
Cdd:pfam00005 77 RENLRLGLLLKGlsKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-227 |
6.71e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 150.55 E-value: 6.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 25 SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIS---QMSEDQAAAFRGaNIGIVFQSFH 101
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLRQ-KVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 102 LIPNMTALEN-VAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNL 178
Cdd:COG4161 93 LWPHLTVMENlIEAPCKVLGlsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489055174 179 DTATGRQIADLLFAKQrENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG4161 173 DPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKvASQVVYMEKGRIIE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-225 |
6.77e-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: 148.35 E-value: 6.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrg 90
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 aNIGIVFQsfhlipnmtALENVavplelagrrDAFDVAERELravglgerlthypSELSGGEQQRVAIARALAPSPKILI 170
Cdd:cd03214 74 -KIAYVPQ---------ALELL----------GLAHLADRPF-------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 171 ADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
10-225 |
7.24e-45 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 150.34 E-value: 7.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaaaFR 89
Cdd:TIGR00968 1 IEIANISKRFG----SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIPNMTALENVAVPLELAgRRDAFDVAERE---LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIR-KHPKAKIKARVeelLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRS-GRI 225
Cdd:TIGR00968 150 QVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSnGKI 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-227 |
8.89e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 153.95 E-value: 8.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaa 87
Cdd:PRK09452 13 PLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 fRGANIgiVFQSFHLIPNMTALENVAVPLELAGRRDAfDVAER---ELRAVGLGERLTHYPSELSGGEQQRVAIARALAP 164
Cdd:PRK09452 86 -RHVNT--VFQSYALFPHMTVFENVAFGLRMQKTPAA-EITPRvmeALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRIAE 227
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQ 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-240 |
1.22e-44 |
|
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: 156.77 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLT-------LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDnGIVKIAGETISQM 80
Cdd:COG4172 274 PLLEARDLKVWfpikrglFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 81 SEDQAAAFRgANIGIVFQ----SfhLIPNMTALENVAVPLELagRRDAFDVAERE------LRAVGLGERLTH-YPSELS 149
Cdd:COG4172 353 SRRALRPLR-RRMQVVFQdpfgS--LSPRMTVGQIIAEGLRV--HGPGLSAAERRarvaeaLEEVGLDPAARHrYPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 150 GGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDpsLA---ARCDREIPVRSGRIA 226
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD--LAvvrALAHRVMVMKDGKVV 505
|
250
....*....|....
gi 489055174 227 EpvQGagipETQAV 240
Cdd:COG4172 506 E--QG----PTEQV 513
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-226 |
4.86e-44 |
|
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: 147.44 E-value: 4.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIA---PGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETI--SQMSEDQAAAFRGanIGIVFQSFHLI 103
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLPPQQRK--IGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNMTALENVAVPLELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATG 183
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489055174 184 RQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-228 |
6.30e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 147.59 E-value: 6.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVhvlkgvSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafR 89
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GanIGIVFQSFHLIPNMTALENVAVPLELAGRRDAFDVAERE--LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:COG3840 72 P--VSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEqaLERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAEP 228
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAAD 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-236 |
1.01e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 150.62 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaaafR 89
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIPNMTALENVAVPLELAGRRDAFDVAERELRAVGLGE--RLTH----YPSELSGGEQQRVAIARALA 163
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEmvQLAHladrYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 164 PSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAEpvqgAGIPE 236
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQ----AGTPD 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-216 |
1.39e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.49 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL-EHVDN----GIVKIAGETISQMSE 82
Cdd:COG1117 10 PKIEVRNLNVYYG----DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPGarveGEILLDGEDIYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 83 DQAAaFRgANIGIVFQSfhliPN---MTALENVAVPLELAG---RRDAFDVAERELRAVGLGE----RLTHYPSELSGGE 152
Cdd:COG1117 86 DVVE-LR-RRVGMVFQK----PNpfpKSIYDNVAYGLRLHGiksKSELDEIVEESLRKAALWDevkdRLKKSALGLSGGQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 153 QQRVAIARALAPSPKILIADEPTGNLD-TATGRqIADLLFA-KQRengLTMVLVTHDPSLAARC-DR 216
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILElKKD---YTIVIVTHNMQQAARVsDY 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-227 |
4.38e-43 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 152.99 E-value: 4.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTlghAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafR 89
Cdd:COG4988 337 IELEDVSFS---YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----W 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLiPNMTALENVAVplelaGRRDAFDVA-ERELRAVGLGERLTHYP-----------SELSGGEQQRVA 157
Cdd:COG4988 410 RRQIAWVPQNPYL-FAGTIRENLRL-----GRPDASDEElEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLL--FAKQRenglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALrrLAKGR----TVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-225 |
4.66e-43 |
|
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: 149.03 E-value: 4.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAa 86
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFT----ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 afrgaNIGIVFQSFHLIPNMTALENVAVPLELAGRRDAfDVAERE---LRAVGLGERLTHYPSELSGGEQQRVAIARALA 163
Cdd:TIGR03265 77 -----DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRA-EVAERVaelLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 164 PSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRI 225
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-227 |
1.34e-42 |
|
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: 144.75 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAassvHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL-EHVDN----GIVKIAGETISQMSED 83
Cdd:TIGR00972 1 AIEIENLNLFYGEK----EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPGvrieGKVLFDGQDIYDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 84 qAAAFRgANIGIVFQSFHLIPnMTALENVAVPLELAGRRD---AFDVAERELRAVGLGE----RLTHYPSELSGGEQQRV 156
Cdd:TIGR00972 77 -VVELR-RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDkkeLDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 157 AIARALAPSPKILIADEPTGNLDTATGRQIADLLFaKQRENgLTMVLVTHDPSLAARC-DREIPVRSGRIAE 227
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQ-ELKKK-YTIVIVTHNMQQAARIsDRTAFFYDGELVE 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-207 |
1.49e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 146.39 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaaFR 89
Cdd:COG1125 2 IEFENVTKRYPD---GTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GaNIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGL--GERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:COG1125 76 R-RIGYVIQQIGLFPHMTVAENIATVPRLLGwdKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHD 196
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-207 |
1.67e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.80 E-value: 1.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 19 LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRgANIGIVFQ 98
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 99 ----SfhLIPNMTALENVAVPLELAGRRDAfdvAERE------LRAVGLG-ERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:COG4608 103 dpyaS--LNPRMTVGDIIAEPLRIHGLASK---AERRervaelLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-216 |
1.74e-42 |
|
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: 143.44 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaafrg 90
Cdd:cd03235 1 EVEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 anIGIVFQSFHLIPNM--TALENVAVPLELAG------RRDAFDVAERELRAVGLGErLTHYP-SELSGGEQQRVAIARA 161
Cdd:cd03235 70 --IGYVPQRRSIDRDFpiSVRDVVLMGLYGHKglfrrlSKADKAKVDEALERVGLSE-LADRQiGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDR 216
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLEyFDR 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
28-218 |
2.77e-42 |
|
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: 142.62 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsqmsEDQAAAFRgANIGIVFQSFHLIPNMT 107
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYR-RRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIA 187
Cdd:COG4133 92 VRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA 171
|
170 180 190
....*....|....*....|....*....|.
gi 489055174 188 DLLfAKQRENGLTMVLVTHDPsLAARCDREI 218
Cdd:COG4133 172 ELI-AAHLARGGAVLLTTHQP-LELAAARVL 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-207 |
3.24e-42 |
|
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: 143.60 E-value: 3.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVhvlKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaaFR 89
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVA-VP-LELAGRRDAFDVAERELRAVGLGER--LTHYPSELSGGEQQRVAIARALAPS 165
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIAlVPkLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-216 |
4.06e-42 |
|
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: 143.64 E-value: 4.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG0411 3 PLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 fRGanIGIVFQSFHLIPNMTALENVAV-----------------PLELAGRRDAFDVAERELRAVGLGERLTHYPSELSG 150
Cdd:COG0411 79 -LG--IARTFQNPRLFPELTVLENVLVaaharlgrgllaallrlPRARREEREARERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 151 GEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDR 216
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADR 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
28-225 |
5.40e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 143.66 E-value: 5.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVkIAGET-ISQMSEDqaaafrganIGIVFQSFHLIPNM 106
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTApLAEARED---------TRLMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENVAvpLELAGR-RDAfdvAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQ 185
Cdd:PRK11247 97 KVIDNVG--LGLKGQwRDA---ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489055174 186 IADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRI 225
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
28-227 |
9.98e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.58 E-value: 9.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETI--SQMSEDQAAAFRG--ANIGIVFQSFHLI 103
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQKGLIRQlrQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNMTALENVAV-PLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDT 180
Cdd:PRK11264 98 PHRTVLENIIEgPVIVKGepKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 181 -------ATGRQIAdllfakqrENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:PRK11264 178 elvgevlNTIRQLA--------QEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-242 |
1.23e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 142.90 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 16 HLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGAnIGI 95
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 96 VFQ-SFHLI-PNMTALENVAVPLELAGRRDAFDVAERE---LRAVGLG-ERLTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:PRK10419 94 VFQdSISAVnPRKTVREIIREPLRHLLSLDKAERLARAsemLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE--PVQGAGIPETQAVRA 242
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVEtqPVGDKLTFSSPAGRV 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-224 |
4.43e-41 |
|
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: 140.26 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLT-----LGHAasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNG--IVKIAGETI--S 78
Cdd:COG4778 3 TLLEVENLSKTftlhlQGGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRHDGGWVdlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 79 QMSEDQAAAFRGANIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTH-YPSELSGGEQQR 155
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGvdREEARARARELLARLNLPERLWDlPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 156 VAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREnGLTMVLVTHDPSLAAR-CDREIPVRSGR 224
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-224 |
5.43e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 5.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrg 90
Cdd:cd00267 1 EIENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 aNIGIVFQsfhlipnmtalenvavplelagrrdafdvaerelravglgerlthypseLSGGEQQRVAIARALAPSPKILI 170
Cdd:cd00267 74 -RIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 171 ADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGR 224
Cdd:cd00267 104 LDEPTSGLDPASRERLLELL-RELAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-216 |
1.49e-40 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 139.11 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfR 89
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GanIGIVFQSFHLIPNMTALENVAVPLELAGRRDAFDV------------AERELRAVGLGERLTHYPSELSGGEQQRVA 157
Cdd:cd03219 76 G--IGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLArarreerearerAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDR 216
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELI-RELRERGITVLLVEHDMDVVMSlADR 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-227 |
2.15e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.69 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaaSSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFR 89
Cdd:COG1132 340 IEFENVSFSYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVAVplelaGRRDA-FDVAERELRAVGLGERLTHYP-----------SELSGGEQQRVA 157
Cdd:COG1132 414 -RQIGVVPQDTFLF-SGTIRENIRY-----GRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLL--FAKQRenglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALerLMKGR----TTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-226 |
4.57e-40 |
|
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: 139.12 E-value: 4.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLG-HAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQsF--HLIPNMTALENVA-------VPLELAGRRdafdvAERELRAVGLGER-LTHYPSELSGGEQQRVAI 158
Cdd:TIGR04521 81 R-KKVGLVFQ-FpeHQLFEETVYKDIAfgpknlgLSEEEAEER-----VKEALELVGLDEEyLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 159 ARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPS-LAARCDREIPVRSGRIA 226
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEdVAEYADRVIVMHKGKIV 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-226 |
4.73e-40 |
|
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: 138.72 E-value: 4.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTlgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGetISQMSEDQAAAFR 89
Cdd:TIGR04520 1 IEVENVSFS--YPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQ---------------SFhlipnmtALENVAVPLELAGRRdafdVAErELRAVGLGERLTHYPSELSGGEQQ 154
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvgatveddvAF-------GLENLGVPREEMRKR----VDE-ALKLVGMEDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIA 226
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-231 |
5.72e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 137.31 E-value: 5.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRgANIGIVFQSFHLIPNMTA 108
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LENVAVPLELAGRRDAfDVAER---ELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQ 185
Cdd:PRK10908 97 YDNVAIPLIIAGASGD-DIRRRvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 186 IADlLFAKQRENGLTMVLVTHDPSLAARCD-REIPVRSGRIAEPVQG 231
Cdd:PRK10908 176 ILR-LFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHGGVGG 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
28-227 |
5.84e-40 |
|
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: 138.40 E-value: 5.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRgANIGIVFQ----SFHli 103
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFR-RDVQLVFQdspsAVN-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNMTALENVAVPLELAGRRDAFDVAERE---LRAVGL-GERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:TIGR02769 103 PRMTVRQIIGEPLRHLTSLDESEQKARIaelLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489055174 180 TATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-225 |
1.89e-39 |
|
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: 134.06 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFR 89
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GaNIGIVFQSFHLIPNMTALENVavplelagrrdafdvaerelravglgerlthypsELSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03230 73 R-RIGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 170 IADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELL-RELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-227 |
4.38e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.53 E-value: 4.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETI---SQMSEDQAAAFRgANIGIVFQSFHLIP 104
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 NMTALEN-VAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTA 181
Cdd:PRK11124 96 HLTVQQNlIEAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 182 TGRQIADLLFAKQrENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:PRK11124 176 ITAQIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-225 |
1.62e-38 |
|
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: 134.00 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAaafrgaNIGIVFQSFHLIPNMT 107
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR------DISYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAgRRDAFDVAEREL---RAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:cd03299 88 VYKNIAYGLKKR-KVDKKEIERKVLeiaEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489055174 185 QIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKL 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-213 |
1.19e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 132.27 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVD-----NGIVKIAGETIsqMSEDQ 84
Cdd:PRK14267 5 IETVNLRVYYG----SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI--YSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 85 AAAFRGANIGIVFQSFHLIPNMTALENVAVPLELAG----RRDAFDVAERELRAVGLGE----RLTHYPSELSGGEQQRV 156
Cdd:PRK14267 79 DPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvksKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 157 AIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREngLTMVLVTHDPSLAAR 213
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAAR 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-226 |
1.40e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 131.02 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfR 89
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GanIGIVFQSFHLIPNMTALENvavpLELAGRRDAFDVAERELRAV-----GLGERLTHYPSELSGGEQQRVAIARALAP 164
Cdd:cd03224 76 G--IGYVPEGRRIFPELTVEEN----LLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAI-RELRDEGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-225 |
4.61e-37 |
|
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: 128.10 E-value: 4.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafR 89
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIPNmTALENVavplelagrrdafdvaerelravglgerlthypseLSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 170 IADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-226 |
4.95e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 130.66 E-value: 4.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAassvHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRganiGIVFQSFHLIPNMTALENVA---VPLELAGRRDAfDVAERELRAVG---LGERLthYPsELSGGEQQRVAIARA 161
Cdd:PRK13548 77 RR----AVLPQHSSLSFPFTVEEVVAmgrAPHGLSRAEDD-ALVAAALAQVDlahLAGRD--YP-QLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 162 LA------PSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-207 |
5.54e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.59 E-value: 5.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmsedqaaafRGANIGIVFQSFHLIPNMT 107
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---------PGAERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQ 185
Cdd:PRK11248 87 VQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 489055174 186 IADLLFAKQRENGLTMVLVTHD 207
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-226 |
7.24e-37 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 132.53 E-value: 7.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETisqMSEDQAAAFRGA---NIGIVFQSFHLIPNMTA 108
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGIFLPPhrrRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LENvavpLELAGRRDAFDVAERELRAV----GLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:COG4148 95 RGN----LLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489055174 185 QIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVV 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-226 |
1.37e-36 |
|
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: 128.95 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG0410 2 PMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 fRGanIGIVFQSFHLIPNMTALENvavpLELAG--RRDAFDVAERELRAVG----LGERLTHYPSELSGGEQQRVAIARA 161
Cdd:COG0410 78 -LG--IGYVPEGRRIFPSLTVEEN----LLLGAyaRRDRAEVRADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 162 LAPSPKILIADEPTgnldtaTG------RQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:COG0410 151 LMSRPKLLLLDEPS------LGlaplivEEIFEII-RRLNREGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-207 |
1.37e-36 |
|
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: 128.74 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAaafrganigIVFQSFHLIPNMTA 108
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LENVAVP----LELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:TIGR01184 72 RENIALAvdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 489055174 185 QIADLLFAKQRENGLTMVLVTHD 207
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHD 174
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-226 |
1.95e-36 |
|
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: 127.87 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmseDQAAAF 88
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgaNIGIVFQSFHLIPNMTALENVAVPLELAG-RRDAFDVAERELRAV-GLGERLTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:cd03266 78 R--RLGFVSDSTGLYDRLTARENLEYFAGLYGlKGDELTARLEELADRlGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-208 |
5.07e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 126.44 E-value: 5.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGleHVDNGI-----VKIAGETISQMSEDQa 85
Cdd:COG4136 3 SLENLTITLGGRP----LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG--TLSPAFsasgeVLLNGRRLTALPAEQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 aafRgaNIGIVFQSFHLIPNMTALENVAVPL-ELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAP 164
Cdd:COG4136 76 ---R--RIGILFQDDLLFPHLSVGENLAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDP 208
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-227 |
1.47e-35 |
|
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: 126.19 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaaSSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaAFR 89
Cdd:cd03253 1 IEFENVTFAYD---PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD---SLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDVA-ERELRAVGLGERLTHYPS-----------ELSGGEQQRVA 157
Cdd:cd03253 75 -RAIGVVPQDTVLF-NDTIGYNIRY-----GRPDATDEEvIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLL--FAKQRenglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALrdVSKGR----TTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-226 |
1.51e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.77 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFR 89
Cdd:COG4559 2 LEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GanigIVFQSFHLIPNMTALENVA---VPLELAGRRDAfDVAERELRAVG---LGERltHYPsELSGGEQQRVAIARALA 163
Cdd:COG4559 78 A----VLPQHSSLAFPFTVEEVVAlgrAPHGSSAAQDR-QIVREALALVGlahLAGR--SYQ-TLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 164 -------PSPKILIADEPTGNLDTATGRQIADLL--FAKQrenGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLArqLARR---GGGVVAVLHDLNLAAQyADRILLLHQGRLV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-242 |
2.78e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG1129 3 PLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 frgANIGIVFQSFHLIPNMTALENVAVPLELAG-----RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARAL 162
Cdd:COG1129 79 ---AGIAIIHQELNLVPNLSVAENIFLGREPRRgglidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 163 APSPKILIADEPTGNLdtaTGRQIaDLLFA---KQRENGLTMVLVTHD-PSLAARCDReIPV-RSGRIAEPVQGAGIPET 237
Cdd:COG1129 156 SRDARVLILDEPTASL---TEREV-ERLFRiirRLKAQGVAIIYISHRlDEVFEIADR-VTVlRDGRLVGTGPVAELTED 230
|
....*
gi 489055174 238 QAVRA 242
Cdd:COG1129 231 ELVRL 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-226 |
4.63e-35 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 124.14 E-value: 4.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVhvlkgvSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAafr 89
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 ganIGIVFQSFHLIPNMTALENVA---VP-LEL-AGRRDAFDVAereLRAVGLGERLTHYPSELSGGEQQRVAIARALAP 164
Cdd:cd03298 72 ---VSMLFQENNLFAHLTVEQNVGlglSPgLKLtAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARC-DREIPVRSGRIA 226
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-216 |
5.11e-35 |
|
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: 124.15 E-value: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 16 HLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmseDQAAAFRgaNIGI 95
Cdd:cd03263 5 NLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---DRKAARQ--SLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 96 VFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADE 173
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489055174 174 PTGNLDTATGRQIADLLfAKQRENgLTMVLVTHDPSLAAR-CDR 216
Cdd:cd03263 160 PTSGLDPASRRAIWDLI-LEVRKG-RSIILTTHSMDEAEAlCDR 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-236 |
5.14e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 5 LVGPIIELEdvHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETisqMSEDQ 84
Cdd:PRK13635 1 MKEEIIRVE--HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 85 AAAFRgANIGIVFQSfhliPN------------MTALENVAVPLELAGRRdafdvAERELRAVGLGERLTHYPSELSGGE 152
Cdd:PRK13635 76 VWDVR-RQVGMVFQN----PDnqfvgatvqddvAFGLENIGVPREEMVER-----VDQALRQVGMEDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 153 QQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAEpvqgA 232
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE----E 221
|
....
gi 489055174 233 GIPE 236
Cdd:PRK13635 222 GTPE 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
28-225 |
5.46e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 127.53 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAaafrgaNIGIVFQSFHLIPNMT 107
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR------DICMVFQSYALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAGRRDAfDVAERELRAV------GLGERlthYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTA 181
Cdd:PRK11432 95 LGENVGYGLKMLGVPKE-ERKQRVKEALelvdlaGFEDR---YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489055174 182 TGRQIADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRI 225
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKI 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-225 |
5.48e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 124.24 E-value: 5.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaAAFR 89
Cdd:cd03245 3 IEFRNV--SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDvaERELRAV---GLGERLTHYP-----------SELSGGEQQR 155
Cdd:cd03245 77 RRNIGYVPQDVTLF-YGTLRDNITL-----GAPLADD--ERILRAAelaGVTDFVNKHPngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 156 VAIARALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-207 |
1.06e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.07 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFRGanIGIVFQSFHLIPN 105
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN----DVPPAERG--VGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVPLELAGRrdafDVAERELRA------VGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:PRK11000 90 LSVAENMSFGLKLAGA----KKEEINQRVnqvaevLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190
....*....|....*....|....*....|..
gi 489055174 180 TATGRQ----IADLlfakQRENGLTMVLVTHD 207
Cdd:PRK11000 166 AALRVQmrieISRL----HKRLGRTMIYVTHD 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
28-211 |
1.93e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.93 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqMSEDQAAAFRGAN----------IGIVF 97
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTIN-LVRDKDGQLKVADknqlrllrtrLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 98 QSFHLIPNMTALENV-AVPLELAG--RRDAFDVAERELRAVGLGERLT-HYPSELSGGEQQRVAIARALAPSPKILIADE 173
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGlsKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 489055174 174 PTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLA 211
Cdd:PRK10619 179 PTSALDPELVGEVLRIM-QQLAEEGKTMVVVTHEMGFA 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-213 |
5.18e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 122.71 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL-----EHVDNGIVKIAGETISQMseDQ 84
Cdd:PRK14247 4 IEIRDLKVSFG----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM--DV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 85 AAAFRgaNIGIVFQSFHLIPNMTALENVAVPLEL----AGRRDAFDVAERELRAVGLGE----RLTHYPSELSGGEQQRV 156
Cdd:PRK14247 78 IELRR--RVQMVFQIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 157 AIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREngLTMVLVTHDPSLAAR 213
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAAR 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-213 |
1.82e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 121.31 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETI---SQMSEDQAAAFRgANIGIVFQSFHLIP 104
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLR-KEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 NMTALENVAVPLELAG---RRDAFDVAERELRAVGLG----ERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGN 177
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGikeKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 489055174 178 LDTATGRQIADLLFAKQREngLTMVLVTHDPSLAAR 213
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVAR 217
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
16-227 |
2.28e-33 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 123.57 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 16 HLTLGHAASSVhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVD--NGIVKIAGETISQMSEDQAaafrgaNI 93
Cdd:TIGR03258 10 HLRVAYGANTV--LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAPPHKR------GL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 94 GIVFQSFHLIPNMTALENVAVPLElAGRRDAFDVAER---ELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILI 170
Cdd:TIGR03258 82 ALLFQNYALFPHLKVEDNVAFGLR-AQKMPKADIAERvadALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 171 ADEPTGNLDTATGRQIADLLFAKQRE-NGLTMVLVTHDPSLA-ARCDREIPVRSGRIAE 227
Cdd:TIGR03258 161 LDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDAlTLADKAGIMKDGRLAA 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-225 |
3.17e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 121.25 E-value: 3.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAaa 87
Cdd:PRK13632 6 VMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 fRGaNIGIVFQSfhliPN-----MTALENVAVPLE--LAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIAR 160
Cdd:PRK13632 82 -RK-KIGIIFQN----PDnqfigATVEDDIAFGLEnkKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 161 ALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-227 |
3.50e-33 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 122.53 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLeHVDNGIV----KIAGETISQMSED 83
Cdd:PRK09473 11 ALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 84 QAAAFRGANIGIVFQS--FHLIPNMTALENVAVPLEL---AGRRDAFDVAERELRAVGLGE---RLTHYPSELSGGEQQR 155
Cdd:PRK09473 90 ELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhkgMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 156 VAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPS-LAARCDREIPVRSGRIAE 227
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTME 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-227 |
1.34e-32 |
|
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: 123.76 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNgivkIAGETISQMS-------- 81
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP----TSGRIIYHVAlcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 82 -----------------EDQAAAFRGAN----------IGIVFQ-SFHLIPNMTALENVAVPLELAGR--RDAFDVAERE 131
Cdd:TIGR03269 73 erpskvgepcpvcggtlEPEEVDFWNLSdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYegKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 132 LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLA 211
Cdd:TIGR03269 153 IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVI 232
|
250
....*....|....*..
gi 489055174 212 AR-CDREIPVRSGRIAE 227
Cdd:TIGR03269 233 EDlSDKAIWLENGEIKE 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-226 |
1.50e-32 |
|
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: 117.86 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmsedQAAAFRgANIGIVFQSFHLIPNMTA 108
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVR-RRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQI 186
Cdd:cd03265 91 WENLYIHARLYGvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489055174 187 ADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRIA 226
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRII 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-206 |
1.66e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.21 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG3845 4 PALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 frgANIGIVFQSFHLIPNMTALENVAVPLE-LAGRRDAFDVAERELRAV----GLGERLTHYPSELSGGEQQRVAIARAL 162
Cdd:COG3845 80 ---LGIGMVHQHFMLVPNLTVAENIVLGLEpTKGGRLDRKAARARIRELseryGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 163 APSPKILIADEPTGNLdTAtgrQIADLLFA---KQRENGLTMVLVTH 206
Cdd:COG3845 157 YRGARILILDEPTAVL-TP---QEADELFEilrRLAAEGKSIIFITH 199
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
25-207 |
2.48e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 118.40 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 25 SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsqmsEDQAAAFRGANIGIVFQ----SF 100
Cdd:COG4167 25 QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL----EYGDYKYRCKHIRMIFQdpntSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 101 HliPNMTALENVAVPLELAGRRDAfdvAERE------LRAVGL-GERLTHYPSELSGGEQQRVAIARALAPSPKILIADE 173
Cdd:COG4167 101 N--PRLNIGQILEEPLRLNTDLTA---EEREerifatLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190
....*....|....*....|....*....|....
gi 489055174 174 PTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:COG4167 176 ALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
28-216 |
1.39e-31 |
|
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: 121.24 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaaFRGANIGIVFQSFHLIPNmT 107
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD----SWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVplelaGRRDAFDVAERE-LRAVGLGERLTHYP-----------SELSGGEQQRVAIARALAPSPKILIADEPT 175
Cdd:TIGR02857 412 IAENIRL-----ARPDASDAEIREaLERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489055174 176 GNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDR 216
Cdd:TIGR02857 487 AHLDAETEAEVLEAL--RALAQGRTVLLVTHRLALAALADR 525
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-208 |
1.55e-31 |
|
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: 120.93 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVHLtlGHAASSVhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAA 86
Cdd:TIGR02868 332 KPTLELRDLSA--GYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 afrgANIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDV-AERELRAVGLGERLTHYP-----------SELSGGEQQ 154
Cdd:TIGR02868 409 ----RRVSVCAQDAHLF-DTTVRENLRL-----ARPDATDEeLWAALERVGLADWLRALPdgldtvlgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKqrENGLTMVLVTHDP 208
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHHL 530
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-207 |
1.97e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.89 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 23 ASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRgANIGIVFQS--F 100
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 101 HLIPNMTALENVAVPLEL-AGRRDAFDVAEReLRA----VGLGERLTH-YPSELSGGEQQRVAIARALAPSPKILIADEP 174
Cdd:PRK15079 110 SLNPRMTIGEIIAEPLRTyHPKLSRQEVKDR-VKAmmlkVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190
....*....|....*....|....*....|...
gi 489055174 175 TGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-213 |
3.53e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.26 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 1 MTEklvgPIIELEDVHLTLGHAASsvhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVdNGIVKIAGETIsqm 80
Cdd:PRK14239 1 MTE----PILQVSDLSVYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDL-NPEVTITGSIV--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 81 sedqaaaFRGAN--------------IGIVFQSFHLIPnMTALENVAVPLELAGRRD--AFDVA-ERELRAVGLGE---- 139
Cdd:PRK14239 69 -------YNGHNiysprtdtvdlrkeIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDkqVLDEAvEKSLKGASIWDevkd 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 140 RLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREngLTMVLVTHDPSLAAR 213
Cdd:PRK14239 141 RLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASR 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-225 |
4.50e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.11 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASsvhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGI---VKIAGETIsQMSEDQA 85
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTV-QREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 AAFRG--ANIGIVFQSFHLIPNMTALENVAV------PL-ELAGRRDAFDVAERELRA---VGLGERLTHYPSELSGGEQ 153
Cdd:PRK09984 79 RDIRKsrANTGYIFQQFNLVNRLSVLENVLIgalgstPFwRTCFSWFTREQKQRALQAltrVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 154 QRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
26-207 |
5.27e-31 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 117.25 E-value: 5.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaAAFRGanIGIVFQSFHLIPN 105
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE----PADRD--IAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVPLELAGrrdaFDVAERELR------AVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:PRK11650 91 MSVRENMAYGLKIRG----MPKAEIEERvaeaarILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190
....*....|....*....|....*....|...
gi 489055174 180 tATGR-----QIADLlfakQRENGLTMVLVTHD 207
Cdd:PRK11650 167 -AKLRvqmrlEIQRL----HRRLKTTSLYVTHD 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-227 |
7.25e-31 |
|
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: 113.86 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaAAFR 89
Cdd:cd03254 3 IEFENVNFSYDE---KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR---KSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNmTALENVAVPLELAgRRDAFDVAERELRAVGLGERLT----HYPSE----LSGGEQQRVAIARA 161
Cdd:cd03254 77 -SMIGVVLQDTFLFSG-TIMENIRLGRPNA-TDEEVIEAAKEAGAHDFIMKLPngydTVLGEnggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEAL--EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-236 |
7.68e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.12 E-value: 7.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIS-QMSEDQAAAFRgANIGIVFQsF--HLIPN 105
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLR-KKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVA-------VPLELAGRRdafdvAERELRAVGLGER-LTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGN 177
Cdd:PRK13634 101 ETVEKDICfgpmnfgVSEEDAKQK-----AREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 178 LDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIaepvQGAGIPE 236
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTV----FLQGTPR 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-209 |
8.07e-31 |
|
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: 112.64 E-value: 8.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVH--VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL--EHVDNGIVKIAGETISQMSedqa 85
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRS---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 aaFRGAnIGIVFQSFHLIPNMTALENVAVPLELAGrrdafdvaerelravglgerlthypseLSGGEQQRVAIARALAPS 165
Cdd:cd03213 80 --FRKI-IGYVPQDDILHPTLTVRETLMFAAKLRG---------------------------LSGGERKRVSIALELVSN 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLL--FAKQrenGLTMVLVTHDPS 209
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLrrLADT---GRTIICSIHQPS 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-227 |
8.08e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 8.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 2 TEKLVGPIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIaGETI---- 77
Cdd:COG0488 308 PERLGKKVLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVkigy 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 78 -SQMSEDqaaafrganigivfqsfhLIPNMTALENVavplelagRRDAFDVAERELRAVgL------GERLTHYPSELSG 150
Cdd:COG0488 383 fDQHQEE------------------LDPDKTVLDEL--------RDGAPGGTEQEVRGY-LgrflfsGDDAFKPVGVLSG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 151 GEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL--FAkqrenGlTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALddFP-----G-TVLLVSHDRYFLDRvATRILEFEDGGVRE 509
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
31-227 |
1.03e-30 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 113.62 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 31 GVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLehVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQS----FHLIPNM 106
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGL--LPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprtaFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 T--ALENVAVPLELAgrRDAFDVAERELRAVGL--GERLTH-YPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTA 181
Cdd:TIGR02770 82 GnhAIETLRSLGKLS--KQARALILEALEAVGLpdPEEVLKkYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 182 TGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRS-GRIAE 227
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDdGRIVE 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-225 |
1.40e-30 |
|
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: 112.35 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGHAASsvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmsedqaAAFRG 90
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 ANIGIVFQS--FHLIPNmTALENVAVPLELAGrrDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKI 168
Cdd:cd03226 71 KSIGYVMQDvdYQLFTD-SVREELLLGLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 169 LIADEPTGNLDTATGRQIADlLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGE-LIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
1.50e-30 |
|
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: 118.37 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 2 TEKLVG-PIIELEDVHltlGHAAS----SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKI-AGE 75
Cdd:TIGR03269 271 CEVEVGePIIKVRNVS---KRYISvdrgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 76 TISQMSeDQAAAFRG---ANIGIVFQSFHLIPNMTALENV--AVPLELA---GRRDAFDVaereLRAVGLGER-----LT 142
Cdd:TIGR03269 348 EWVDMT-KPGPDGRGrakRYIGILHQEYDLYPHRTVLDNLteAIGLELPdelARMKAVIT----LKMVGFDEEkaeeiLD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 143 HYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVR 221
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMR 502
|
....
gi 489055174 222 SGRI 225
Cdd:TIGR03269 503 DGKI 506
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-225 |
1.72e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.06 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLghaASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaaF 88
Cdd:PRK13647 4 IIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RGaNIGIVFQSfhliPN-----MTALENVAV-PLELAGRRDAFDV-AERELRAVGLGERLTHYPSELSGGEQQRVAIARA 161
Cdd:PRK13647 78 RS-KVGLVFQD----PDdqvfsSTVWDDVAFgPVNMGLDKDEVERrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-207 |
2.15e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.86 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 12 LEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAgetisqmsedqaaafRGA 91
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 92 NIGIVFQSFHLIPNMTALENV-------------------------AVPLELAGRRDAFDV-----AERELRAV----GL 137
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaeleeleaklaepdEDLERLAELQEEFEAlggweAEARAEEIlsglGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 138 GERLTHYP-SELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENglTMVLVTHD 207
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL--KNYPG--TVLVVSHD 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-219 |
2.48e-30 |
|
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: 112.87 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHvdngivKIAGETISQMSEDqaaa 87
Cdd:COG1119 2 PLLELRNVTVRRG----GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP------PTYGNDVRLFGER---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 fRG--------ANIGIVFQSFH--LIPNMTALENV-----AVPlelaGRRDAFDVAERE-----LRAVGLGERLTHYPSE 147
Cdd:COG1119 68 -RGgedvwelrKRIGLVSPALQlrFPRDETVLDVVlsgffDSI----GLYREPTDEQRErarelLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 148 LSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL--FAKQREngLTMVLVTHDPSlaarcdrEIP 219
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGA--PTLVLVTHHVE-------EIP 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-207 |
3.01e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.87 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHA-ASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FrganIGIVFQ------SfhliPNMTALENVAvpleLAGRRD-------AFDVAERE-----LRAVGLG--ERLTHYPSE 147
Cdd:COG1101 81 Y----IGRVFQdpmmgtA----PSMTIEENLA----LAYRRGkrrglrrGLTKKRRElfrelLATLGLGleNRLDTKVGL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 148 LSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-226 |
4.07e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.32 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 2 TEKLVGPIIELEDvhltLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMS 81
Cdd:PRK11607 12 TRKALTPLLEIRN----LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 82 EDQAAafrganIGIVFQSFHLIPNMTALENVAVPLE---LAGRRDAFDVAEReLRAVGLGERLTHYPSELSGGEQQRVAI 158
Cdd:PRK11607 88 PYQRP------INMMFQSYALFPHMTVEQNIAFGLKqdkLPKAEIASRVNEM-LGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 159 ARALAPSPKILIADEPTGNLDTA----TGRQIADLLfakqRENGLTMVLVTHDpslaarcDREIPVRSGRIA 226
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDIL----ERVGVTCVMVTHD-------QEEAMTMAGRIA 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-225 |
5.12e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 111.15 E-value: 5.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaassVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafr 89
Cdd:cd03268 1 LKTNDLTKTYGK----KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPLELAGRRDAfdVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03268 72 -RRIGALIEAPGFYPNLTARENLRLLARLLGIRKK--RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKqRENGLTMVLVTHDPS-LAARCDREIPVRSGRI 225
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSeIQKVADRIGIINKGKL 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-226 |
5.21e-30 |
|
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: 116.77 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 17 LTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafRGANIGIV 96
Cdd:COG4618 336 LTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE----LGRHIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 97 FQSFHLIPNmTALENVAvplelagrRdaFDVAEREL-----RAVGLGERLTHYP-----------SELSGGEQQRVAIAR 160
Cdd:COG4618 412 PQDVELFDG-TIAENIA--------R--FGDADPEKvvaaaKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 161 ALAPSPKILIADEPTGNLDT----ATGRQIADLlfakqRENGLTMVLVTHDPSLAARCDREIPVRSGRIA 226
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDegeaALAAAIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-226 |
9.51e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.83 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 33 SLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAafrganIGIVFQSFHLIPNMTALENV 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 113 AVPLELAGRRDAFDVAERELRA--VGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL 190
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIArqMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 489055174 191 FAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-218 |
1.20e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.63 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGetisqmsedqaaafrGANIGIVFQSFHLIPNM- 106
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 -TALENVAV----PLELAGR--RDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:NF040873 72 lTVRDLVAMgrwaRRGLWRRltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 180 TATGRQIADLLfAKQRENGLTMVLVTHDPSLAARCDREI 218
Cdd:NF040873 152 AESRERIIALL-AEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-227 |
1.35e-29 |
|
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: 116.07 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVHLtlGHAASSVhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaA 86
Cdd:COG5265 355 GGEVRFENVSF--GYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ---A 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 AFRGAnIGIVFQS---FhlipNMTALENVAVplelaGRRDAfdvAERELRAV-----------GL--------GER-Lth 143
Cdd:COG5265 429 SLRAA-IGIVPQDtvlF----NDTIAYNIAY-----GRPDA---SEEEVEAAaraaqihdfieSLpdgydtrvGERgL-- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 144 ypsELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL--FAKQRenglTMVLVTHDPSLAARCDREIPVR 221
Cdd:COG5265 494 ---KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALreVARGR----TTLVIAHRLSTIVDADEILVLE 566
|
....*.
gi 489055174 222 SGRIAE 227
Cdd:COG5265 567 AGRIVE 572
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-227 |
1.62e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.97 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 12 LEDVHLTLGhaassvhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGA 91
Cdd:PRK10070 35 LEKTGLSLG--------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 92 NIGIVFQSFHLIPNMTALENVAVPLELAG------RRDAFDVaereLRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGinaeerREKALDA----LRQVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARC-DREIPVRSGRIAE 227
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQ 245
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
38-236 |
1.73e-29 |
|
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: 112.90 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 38 PGQSV-GIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHLIPNMTALENVavpl 116
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNL---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 117 eLAGRRDAfDVAERE------LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL 190
Cdd:TIGR02142 97 -RYGMKRA-RPSERRisfervIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 191 FAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRiaepVQGAGIPE 236
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGR----VAAAGPIA 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-227 |
2.65e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.92 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASsvHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaAAFR 89
Cdd:PRK11160 339 LTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVAVPLELAGRRDAFDVaereLRAVGLGERLTHYPS----------ELSGGEQQRVAIA 159
Cdd:PRK11160 414 -QAISVVSQRVHLF-SATLRDNLLLAAPNASDEALIEV----LQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 160 RAL---APspkILIADEPTGNLDTATGRQIADLL--FAKQRenglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PRK11160 488 RALlhdAP---LLLLDEPTEGLDAETERQILELLaeHAQNK----TVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-226 |
4.18e-29 |
|
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: 107.13 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfr 89
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQsfhlipnmtalenvavplelagrrdafdvaerelravglgerlthypseLSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03216 75 -AGIAMVYQ-------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 170 IADEPTGNLdtaTGRQIADLL--FAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:cd03216 105 ILDEPTAAL---TPAEVERLFkvIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-209 |
7.78e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.82 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 19 LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGAnIGIVFQ 98
Cdd:PRK11308 21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQK-IQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 99 SFH--LIPNMTALENVAVPLELAGRRDAfdvAERELRA------VGL-GERLTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:PRK11308 100 NPYgsLNPRKKVGQILEEPLLINTSLSA---AERREKAlammakVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPS 209
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLS 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-227 |
1.00e-28 |
|
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: 108.47 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFR 89
Cdd:cd03251 1 VEFKNV--TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDVA-ERELRAVGLGERLTHYP-----------SELSGGEQQRVA 157
Cdd:cd03251 76 -RQIGLVSQDVFLF-NDTVAENIAY-----GRPGATREEvEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLL--FAKQRenglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALerLMKNR----TTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-231 |
1.42e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.88 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVkIAGETISQMSEDQAAAFRgANIGIVFQSFH--LIP 104
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIW-FDGQPLHNLNRRQLLPVR-HRIQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 NMTALENVAVPLELagRRDAFDVAERELRA------VGLGERLTH-YPSELSGGEQQRVAIARALAPSPKILIADEPTGN 177
Cdd:PRK15134 378 RLNVLQIIEEGLRV--HQPTLSAAQREQQViavmeeVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 178 LDTATGRQIADLLFAKQRENGLTMVLVTHDPSLA-ARCDREIPVRSGRIAEpvQG 231
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEVVE--QG 508
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-238 |
2.10e-28 |
|
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: 107.23 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGHAassvHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrg 90
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 ANIGIVFQSFHLIPNMTALENVAVPLELAGRRDAFDVAE-RELRAVgLGERLTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEiYELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARC-DREIPVRSGRIAEPVQGAGIPETQ 238
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELaDRYYVMERGRVVASGAGDELDEDK 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
9-211 |
2.62e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASsvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqMSEDQAAAF 88
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSfhliPN-----MTALENVAV-PLELAGRRDafDVAER---ELRAVGLGERLTHYPSELSGGEQQRVAIA 159
Cdd:PRK13639 77 R-KTVGIVFQN----PDdqlfaPTVEEDVAFgPLNLGLSKE--EVEKRvkeALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489055174 160 RALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREnGLTMVLVTHDPSLA 211
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLV 200
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
29-206 |
4.86e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQ-SFHLIPNMT 107
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAG--RRDAFDVAERELRAVGLGERL-THYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTAtGR 184
Cdd:PRK13649 103 VLKDVAFGPQNFGvsQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK-GR 181
|
170 180
....*....|....*....|..
gi 489055174 185 QIADLLFAKQRENGLTMVLVTH 206
Cdd:PRK13649 182 KELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-226 |
7.34e-28 |
|
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: 105.35 E-value: 7.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAassvHVLKGVSLHIAPGQSvGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaaAFR 89
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GAnIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFLDYIAWLKGipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLfAKQRENgLTMVLVTHDPS-LAARCDREIPVRSGRIA 226
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLL-SELGED-RIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-226 |
1.07e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.94 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAafr 89
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAV---PLElAGRRDAFDVA--ERELRAVGLGErLTH-YPSELSGGEQQRVAIARALA 163
Cdd:COG4604 75 -KRLAILRQENHINSRLTVRELVAFgrfPYS-KGRLTAEDREiiDEAIAYLDLED-LADrYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 164 PSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-227 |
1.57e-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: 103.55 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHaaSSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfr 89
Cdd:cd03247 1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 ganIGIVFQSFHLIpNMTALENVavplelaGRRdafdvaerelravglgerlthypseLSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03247 77 ---ISVLNQRPYLF-DTTLRNNL-------GRR-------------------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-237 |
2.48e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmseDQAAA 87
Cdd:PRK13648 6 SIIVFKNV--SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRgANIGIVFQSfhliPNMT------------ALENVAVPLELAGRRdafdVAErELRAVGLGERLTHYPSELSGGEQQR 155
Cdd:PRK13648 81 LR-KHIGIVFQN----PDNQfvgsivkydvafGLENHAVPYDEMHRR----VSE-ALKQVDMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 156 VAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAEpvqgAGIP 235
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK----EGTP 226
|
..
gi 489055174 236 ET 237
Cdd:PRK13648 227 TE 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-227 |
3.05e-27 |
|
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: 104.49 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEdvHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMsedqAAAFR 89
Cdd:cd03252 1 ITFE--HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA----DPAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSfHLIPNMTALENVAVPLELAGRRDAFDVAE--------RELRAvGLGERLTHYPSELSGGEQQRVAIARA 161
Cdd:cd03252 75 RRQVGVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKlagahdfiSELPE-GYDTIVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNM--HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
33-226 |
3.13e-27 |
|
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: 103.79 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 33 SLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAafrganIGIVFQSFHLIPNMTALENV 112
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 113 AVPLELAGRRDAFDVAERE--LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL 190
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVdaAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 489055174 191 FAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIK 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-227 |
5.05e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKS-TLLMVLAGLEH----VDNGIVKIAGETISQMSE 82
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 83 DQAAAFRGANIGIVFQS--FHLIPNMTALENVAVPLEL-------AGRRDAFDVAERelraVGL---GERLTHYPSELSG 150
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhrgmrreAARGEILNCLDR----VGIrqaAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 151 GEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVE 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-225 |
5.92e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEdvHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL---EHVDNGIVKIAGETisqMSEDQA 85
Cdd:PRK13640 5 IVEFK--HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGIT---LTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 AAFRgANIGIVFQSfhliPNMT------------ALENVAVPlelagRRDAFDVAERELRAVGLGERLTHYPSELSGGEQ 153
Cdd:PRK13640 80 WDIR-EKVGIVFQN----PDNQfvgatvgddvafGLENRAVP-----RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 154 QRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-227 |
1.23e-26 |
|
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: 103.00 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFR 89
Cdd:cd03249 1 IEFKNVSFRYP-SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR----DLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDV-AERELRAVGLGERLTHYP-----------SELSGGEQQRVA 157
Cdd:cd03249 76 RSQIGLVSQEPVLF-DGTIAENIRY-----GKPDATDEeVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEAL--DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
32-240 |
1.43e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 104.82 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL----EHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSfhlipNMT 107
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQD-----PMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENV---------AVPLELAGRRdafdvAERELRAVGL---------GERLTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:PRK11022 101 SLNPCytvgfqimeAIKVHQGGNK-----KTRRQRAIDLlnqvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREI-------PVRSGRIAEPVQGAGIPETQAV 240
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIivmyagqVVETGKAHDIFRAPRHPYTQAL 253
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-218 |
1.46e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTL--GHAassvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL-EHVDNGIVKIAGETI---SQMSed 83
Cdd:COG4178 363 LALEDLTLRTpdGRP-----LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRIARPAGARVlflPQRP-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 84 qaaafrganigivfqsfhLIPNMTALENVAVPlelaGRRDAFDVAE-RE-LRAVGLG---ERL---THYPSELSGGEQQR 155
Cdd:COG4178 436 ------------------YLPLGTLREALLYP----ATAEAFSDAElREaLEAVGLGhlaERLdeeADWDQVLSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 156 VAIARALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREI 218
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-227 |
1.73e-26 |
|
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: 102.23 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGetisqmsedQAAAFRGANIGivfqsFHliPN 105
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------RVSSLLGLGGG-----FN--PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVPLELAGRRDAfDVAERELRAV---GLGERLtHYP-SELSGGEQQRVAIARALAPSPKILIADEPTGNLDTA 181
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRK-EIDEKIDEIIefsELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 182 TGRQIADlLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:cd03220 177 FQEKCQR-RLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-207 |
1.77e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.19 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDN-----GIVKIAGETISQMSEDQAAAFRgaNIGIVFQSFHL 102
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLRR--QVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 IPnMTALENVAVPLELAGRRDAF---DVAERELRAVGLGERLTH--YPS--ELSGGEQQRVAIARALAPSPKILIADEPT 175
Cdd:PRK14258 100 FP-MSVYDNVAYGVKIVGWRPKLeidDIVESALKDADLWDEIKHkiHKSalDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190
....*....|....*....|....*....|..
gi 489055174 176 GNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-225 |
3.03e-26 |
|
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: 102.03 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 25 SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFRgANIGIVF-QSFHLI 103
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW----KRRKKFL-RRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNMTALENVAVplelagRRDAFDVAERELRA--------VGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPT 175
Cdd:cd03267 108 WDLPVIDSFYL------LAAIYDLPPARFKKrldelselLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489055174 176 GNLDTATGRQIADLLFAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-227 |
6.00e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 105.71 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRgANIGIVFQSFH--LI 103
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPYasLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNMTALENVAVPLELAGRRDAFDVAERE---LRAVGL-GERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPGKAAAARVawlLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489055174 180 TATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRS-GRIAE 227
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYlGQIVE 544
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-207 |
8.89e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 8.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETI-SQMSEDQAAAFRgANIGIVFQ--SFHLIPN 105
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQfpEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 mTALENVAV-PLEL-AGRRDAFDVAERELRAVGLGERL-THYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTAT 182
Cdd:PRK13641 102 -TVLKDVEFgPKNFgFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180
....*....|....*....|....*
gi 489055174 183 GRQIADLLFAKQREnGLTMVLVTHD 207
Cdd:PRK13641 181 RKEMMQLFKDYQKA-GHTVILVTHN 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-225 |
9.95e-26 |
|
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: 99.66 E-value: 9.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafr 89
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 ganIGIVFQSFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:cd03269 72 ---IGYLPEERGLYPKMKVIDQLVYLAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAkQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-225 |
1.63e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.96 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGEtisQMSEDQAAAF 88
Cdd:PRK13650 4 IIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSfhliPN-----MTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARA 161
Cdd:PRK13650 80 R-HKIGMVFQN----PDnqfvgATVEDDVAFGLENKGipHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
9-225 |
2.36e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGEtisQMSEDQAAAF 88
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQS-FHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:PRK13642 80 R-RKIGMVFQNpDNQFVGATVEDDVAFGMENQGipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-227 |
2.72e-25 |
|
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: 103.64 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 12 LEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFRgA 91
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR-R 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 92 NIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDVA--ERELRAVGLGERLTHYP-----------SELSGGEQQRVAI 158
Cdd:TIGR02203 407 QVALVSQDVVLF-NDTIANNIAY-----GRTEQADRAeiERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 159 ARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRenGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-227 |
3.65e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.62 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 19 LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGET-----ISQMSEDQAAAFRGANI 93
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAERRRLLRTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 94 GIVFQsfH----LIPNMTALENVAVPLELAGRR---DAFDVAERELRAVGLG-ERLTHYPSELSGGEQQRVAIARALAPS 165
Cdd:PRK11701 92 GFVHQ--HprdgLRMQVSAGGNIGERLMAVGARhygDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDpsLA-AR--CDREIPVRSGRIAE 227
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHD--LAvARllAHRLLVMKQGRVVE 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-225 |
3.79e-25 |
|
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: 97.50 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 12 LEDVHLTLGHAassvhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrga 91
Cdd:cd03215 5 LEVRGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 92 nIGIVF-----QSFHLIPNMTALENVAVPlelagrrdafdvaerelravglgerlthypSELSGGEQQRVAIARALAPSP 166
Cdd:cd03215 75 -AGIAYvpedrKREGLVLDLSVAENIALS------------------------------SLLSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAkQRENGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-208 |
4.17e-25 |
|
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: 98.50 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVD---NGIVKIAGEtisQMSEDQa 85
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 aaFRgANIGIVFQSFHLIPNMTALE------NVAVPLELAGRRDAFDVAERELRAVGLgERLTH-YPSELSGGEQQRVAI 158
Cdd:cd03234 79 --FQ-KCVAYVRQDDILLPGLTVREtltytaILRLPRKSSDAIRKKRVEDVLLRDLAL-TRIGGnLVKGISGGERRRVSI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489055174 159 ARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLtmVLVT-HDP 208
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRI--VILTiHQP 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
10-216 |
4.61e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 99.14 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTlghaassvHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHvDNGIVKIAGETISQMSEDQAAAFR 89
Cdd:COG4138 1 LQLNDVAVA--------GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 G---------ANIGiVFQ--SFHLIPNMTALENVAVPLELAGRrdafdvaerelraVGLGERLTHYPSELSGGEQQRVAI 158
Cdd:COG4138 72 AylsqqqsppFAMP-VFQylALHQPAGASSEAVEQLLAQLAEA-------------LGLEDKLSRPLTQLSGGEWQRVRL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 159 ARALA-------PSPKILIADEPTGNLDTAtgRQIA-DLLFAKQRENGLTMVLVTHDPSLAAR-CDR 216
Cdd:COG4138 138 AAVLLqvwptinPEGQLLLLDEPMNSLDVA--QQAAlDRLLRELCQQGITVVMSSHDLNHTLRhADR 202
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-227 |
4.83e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 99.00 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 30 KGVSLHIAPGQSVGIVGPSGSGKStlLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQ----SFHLIPN 105
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQnprsAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MT--ALENVAVplelAGRRDAFDVAERELRAVGLGER---LTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDT 180
Cdd:PRK10418 98 MHthARETCLA----LGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 181 ATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRS-GRIAE 227
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMShGRIVE 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
9-225 |
6.52e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLtlgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqMSEDQAAAF 88
Cdd:PRK13636 5 ILKVEELNY---NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQS-FHLIPNMTALENVAV-PLELAGRRDAF-DVAERELRAVGLgERLTHYPSE-LSGGEQQRVAIARALAP 164
Cdd:PRK13636 81 R-ESVGMVFQDpDNQLFSASVYQDVSFgAVNLKLPEDEVrKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAA-RCDREIPVRSGRI 225
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-174 |
6.74e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.18 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaaAFRGANIGI--------VFQs 99
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP-----MHKRARLGIgylpqeasIFR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 fhlipNMTALENVAVPLELAGRrdafDVAERELRAVGLGE--RLTH----YPSELSGGEQQRVAIARALAPSPKILIADE 173
Cdd:COG1137 92 -----KLTVEDNILAVLELRKL----SKKEREERLEELLEefGITHlrksKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
.
gi 489055174 174 P 174
Cdd:COG1137 163 P 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-227 |
7.91e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmsedQAAA 87
Cdd:PRK13537 6 APIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRGANIGIVFQSFHLIPNMTALENvavpLELAGRRDAFDVAERELRAVGLGE--RLTHYP----SELSGGEQQRVAIARA 161
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVREN----LLVFGRYFGLSAAAARALVPPLLEfaKLENKAdakvGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 162 LAPSPKILIADEPTGNLDTatgrQIADLLFAKQRE---NGLTMVLVTHDPSLAAR-CDREIPVRSGR-IAE 227
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDP----QARHLMWERLRSllaRGKTILLTTHFMEEAERlCDRLCVIEEGRkIAE 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
10-226 |
8.10e-25 |
|
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: 102.04 E-value: 8.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAaafr 89
Cdd:TIGR01842 317 LSVENV--TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIPNMTAlENVAVPLELAGRRDAFDVAerelRAVGLGERLTHYP-----------SELSGGEQQRVAI 158
Cdd:TIGR01842 391 GKHIGYLPQDVELFPGTVA-ENIARFGENADPEKIIEAA----KLAGVHELILRLPdgydtvigpggATLSGGQRQRIAL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 159 ARALAPSPKILIADEPTGNLDTAtGRQ--IADLLFAKQRenGLTMVLVTHDPSLAARCDREIPVRSGRIA 226
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEE-GEQalANAIKALKAR--GITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-216 |
1.32e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 99.59 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLeHVDNGIVK-----IAGETISQMSEDQAAAFRGANIGIVFQ-- 98
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTadrfrWNGIDLLKLSPRERRKIIGREIAMIFQep 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 99 SFHLIPNMTALENV--AVP-LELAGR-----RDAFDVAERELRAVGLGER---LTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:COG4170 99 SSCLDPSAKIGDQLieAIPsWTFKGKwwqrfKWRKKRAIELLHRVGIKDHkdiMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD-PSLAARCDR 216
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADT 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-218 |
2.18e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.10 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGEtisqmsedqaaafrGANIGIVFQSFHLI---- 103
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG--------------DIDDPDVAEACHYLghrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 ---PNMTALENVAVPLELAGRRDAFdvAERELRAVGLGeRLTHYP-SELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:PRK13539 83 amkPALTVAENLEFWAAFLGGEELD--IAAALEAVGLA-PLAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 180 TATGRQIADLLFAKQRENGLtMVLVTHDPsLAARCDREI 218
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGI-VIAATHIP-LGLPGAREL 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
10-227 |
2.24e-24 |
|
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: 101.35 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASsvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaaafr 89
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID-------- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 ganIGIVFQSFHLIPNM------TALENvavpLELAGRRD--------AFDVAER----ELRAVGLGERLTHYPSELSGG 151
Cdd:TIGR01193 543 ---RHTLRQFINYLPQEpyifsgSILEN----LLLGAKENvsqdeiwaACEIAEIkddiENMPLGYQTELSEEGSSISGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 152 EQQRVAIARALAPSPKILIADEPTGNLDTATGRQIAD-LLFAKQRenglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNnLLNLQDK----TIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-227 |
3.18e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.57 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaaAFR 89
Cdd:TIGR00958 479 IEFQDVSFSYP-NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH----HYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVFQSFHLIpNMTALENVAVPLELAGRRDAFDVAERELRAVGLGERLTHYPSE-------LSGGEQQRVAIARAL 162
Cdd:TIGR00958 554 HRQVALVGQEPVLF-SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 163 APSPKILIADEPTGNLDTatgrQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:TIGR00958 633 VRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-227 |
3.41e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 97.47 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 15 VHLTLGHAASSVhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLE-----HVDNGIVKIAGETISQMSEdqAAAFR 89
Cdd:PRK14271 25 VNLTLGFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIFNYRD--VLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPnMTALENVAVPL---ELAGRRDAFDVAERELRAVGL----GERLTHYPSELSGGEQQRVAIARAL 162
Cdd:PRK14271 101 -RRVGMLFQRPNPFP-MSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 163 APSPKILIADEPTGNLDTATGRQIADllFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEE--FIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-218 |
3.78e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVhltlGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaA 87
Cdd:PRK10247 6 PLLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRgANIGIVFQSFHLIPNmTALENVAVPLELAGRRDAFDVAERELRAVGLGER-LTHYPSELSGGEQQRVAIARALAPSP 166
Cdd:PRK10247 79 YR-QQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489055174 167 KILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREI 218
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
28-225 |
4.59e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIV----------KIAGETISQMSED--QAAAFRGAN--- 92
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLviQKTRFKKIKkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 93 -----IGIVFQ--SFHLIPNmTALENVAV-PLELA-GRRDAFDVAERELRAVGLGER-LTHYPSELSGGEQQRVAIARAL 162
Cdd:PRK13651 102 eirrrVGVVFQfaEYQLFEQ-TIEKDIIFgPVSMGvSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 163 APSPKILIADEPTGNLDTATGRQIADlLFAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKI 243
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
32-227 |
5.87e-24 |
|
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: 96.44 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGET-----ISQMSEDQAAAFRGANIGIVFQSFH--LIP 104
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQNPRdgLRM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 NMTALENVAVPLELAGRRDAFDV---AERELRAVGLGE-RLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDT 180
Cdd:TIGR02323 102 RVSAGANIGERLMAIGARHYGNIratAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDV 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 181 ATGRQIADLLFAKQRENGLTMVLVTHDPSLAA-RCDREIPVRSGRIAE 227
Cdd:TIGR02323 182 SVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVE 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-227 |
6.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.77 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQsfhlIPNMTA 108
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LE-NVAVPLELAGRRDAFDVAERELRA----VGLG-ER--LTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDT 180
Cdd:PRK13646 99 FEdTVEREIIFGPKNFKMNLDEVKNYAhrllMDLGfSRdvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 181 ATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPV-RSGRIAE 227
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVmKEGSIVS 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-224 |
6.59e-24 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 94.84 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVH-VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGeTISQMSEdqaaaf 88
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVSQ------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 rganigivfQSFhlIPNMTALENVavpleLAGRRdaFDVA--ERELRAVGL---------------GER-LThypseLSG 150
Cdd:cd03250 74 ---------EPW--IQNGTIRENI-----LFGKP--FDEEryEKVIKACALepdleilpdgdlteiGEKgIN-----LSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 151 GEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGR 224
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-227 |
7.05e-24 |
|
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: 95.25 E-value: 7.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAaafRgANIGIVFQSFHLIP--- 104
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---R-SRISIIPQDPVLFSgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 --NM--------TALENVavpLELAGRRDAFdvaerELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEP 174
Cdd:cd03244 95 rsNLdpfgeysdEELWQA---LERVGLKEFV-----ESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 175 TGNLDTATGRQIADLLfakqREN--GLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03244 167 TASVDPETDALIQKTI----REAfkDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-242 |
9.35e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVhltlghaaSSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:COG1129 255 VVLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FrganiGIVF-----QSFHLIPNMTALENVAVP-LELAGRRDAFDVAERELRAVGLGERL---THYP----SELSGGEQQ 154
Cdd:COG1129 327 A-----GIAYvpedrKGEGLVLDLSIRENITLAsLDRLSRGGLLDRRRERALAEEYIKRLrikTPSPeqpvGNLSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRIAEPVQGAG 233
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLI-RELAAEGKAVIVISSElPELLGLSDRILVMREGRIVGELDREE 480
|
....*....
gi 489055174 234 IPETQAVRA 242
Cdd:COG1129 481 ATEEAIMAA 489
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-227 |
1.35e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVHvlkGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaAAFR 89
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR---ASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVAVplelaGRRDAFDV-----AER-------ELRAVGL----GERlthyPSELSGGEQ 153
Cdd:PRK13657 409 -RNIAVVFQDAGLF-NRSIEDNIRV-----GRPDATDEemraaAERaqahdfiERKPDGYdtvvGER----GRQLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 154 QRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRenGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-238 |
1.67e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTlghAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAA 87
Cdd:COG3845 256 VVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRGANIGIVFQSFH---LIPNMTALENVAV------PL------------ELAGRR-DAFDVaerelRAVGLGERLthyp 145
Cdd:COG3845 330 RRRLGVAYIPEDRLgrgLVPDMSVAENLILgryrrpPFsrggfldrkairAFAEELiEEFDV-----RTPGPDTPA---- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 146 SELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAkQRENGLTMVLVTHDPS-LAARCDREIPVRSGR 224
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDeILALSDRIAVMYEGR 479
|
250
....*....|....
gi 489055174 225 IAEPVQGAGIPETQ 238
Cdd:COG3845 480 IVGEVPAAEATREE 493
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-206 |
2.29e-23 |
|
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: 93.36 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLE--HVDNGIVKIAGETISQMSEDQAAA 87
Cdd:cd03217 1 LEIKDLHVSVG----GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 frgANIGIVFQSfhlipnmtalenvavPLELAGRRDAFdvaerELRAVGLGerlthypseLSGGEQQRVAIARALAPSPK 167
Cdd:cd03217 77 ---LGIFLAFQY---------------PPEIPGVKNAD-----FLRYVNEG---------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTH 206
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVI-NKLREEGKSVLIITH 162
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-225 |
2.50e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmsedQAAAFRgANIGIVF-QSFHLIP 104
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK----RRKEFA-RRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 NMTALENvavpLELAGR-----RDAFDVAERELRAV-GLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNL 178
Cdd:COG4586 110 DLPAIDS----FRLLKAiyripDAEYKKRLDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 179 DTATGRQIADLLFAKQRENGLTMVLVTHDPS-LAARCDREIPVRSGRI 225
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEALCDRVIVIDHGRI 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-236 |
3.02e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaA 86
Cdd:PRK09536 1 MPMIDVSDLSVEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 AFRGANIGIVFQSFHLIPNMTALENVAV----------PLELAGRRdafdVAERELRAVGLGERLTHYPSELSGGEQQRV 156
Cdd:PRK09536 73 RAASRRVASVPQDTSLSFEFDVRQVVEMgrtphrsrfdTWTETDRA----AVERAMERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 157 AIARALAPSPKILIADEPTGNLDtaTGRQIADL-LFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRiaepVQGAGI 234
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLD--INHQVRTLeLVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGR----VRAAGP 222
|
..
gi 489055174 235 PE 236
Cdd:PRK09536 223 PA 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-227 |
4.09e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.67 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFR 89
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP----ARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVplelAGRRdaFDVAERELRAV--------GLGERLTHYPSELSGGEQQRVAIARA 161
Cdd:PRK13536 114 -ARIGVVPQFDNLDLEFTVRENLLV----FGRY--FGMSTREIEAVipsllefaRLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLFAkQRENGLTMVLVTHDPSLAAR-CDREIPVRSGR-IAE 227
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRS-LLARGKTILLTTHFMEEAERlCDRLCVLEAGRkIAE 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-227 |
4.95e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLT--LGHAASS----------------VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIV 70
Cdd:COG1134 4 MIEVENVSKSyrLYHEPSRslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 71 KIAGETisqmsedqaAAFRGANIGivfqsFHliPNMTALENVavplELAGRrdAFDVAERELRAV--------GLGERLT 142
Cdd:COG1134 84 EVNGRV---------SALLELGAG-----FH--PELTGRENI----YLNGR--LLGLSRKEIDEKfdeivefaELGDFID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 143 ----HYPSelsgGEQQRVAIARALAPSPKILIADEPtgnldTATGrqiaDLLFAKQ--------RENGLTMVLVTHDPSL 210
Cdd:COG1134 142 qpvkTYSS----GMRARLAFAVATAVDPDILLVDEV-----LAVG----DAAFQKKclarirelRESGRTVIFVSHSMGA 208
|
250
....*....|....*...
gi 489055174 211 AAR-CDREIPVRSGRIAE 227
Cdd:COG1134 209 VRRlCDRAIWLEKGRLVM 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-206 |
5.40e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.56 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 31 GVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSED--QAAAFRGANIGIVfqsfhliPNMTA 108
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLLYLGHQPGIK-------TELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LENVAVPLELAGRRDAFDVAErELRAVGLGERLtHYP-SELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIA 187
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWE-ALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170
....*....|....*....
gi 489055174 188 DlLFAKQRENGLTMVLVTH 206
Cdd:PRK13538 170 A-LLAQHAEQGGMVILTTH 187
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-232 |
5.67e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 16 HLTLGHAASSVhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrgaNIGI 95
Cdd:PRK10253 12 QLTLGYGKYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 96 VFQSFHLIPNMTALENVA------VPLELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:PRK10253 86 LAQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAepVQGA 232
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIV--AQGA 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-242 |
6.76e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.02 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMsedQAAA 87
Cdd:PRK11614 4 VMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRGANIGIVFQSFHLIPNMTALENVAVPLELAGRRDafdVAERELRAVGL----GERLTHYPSELSGGEQQRVAIARALA 163
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQ---FQERIKWVYELfprlHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 164 PSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAEPVQGAGIPETQAVRA 242
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTI-EQLREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAVRS 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
27-179 |
6.82e-23 |
|
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: 92.99 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAafrGANIGIVFQSFHLIPNM 106
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA---RLGIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 107 TALENVAVPLELAGrrdaFDVAERELRAVGLGE--RLTH----YPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:cd03218 91 TVEENILAVLEIRG----LSKKEREEKLEELLEefHITHlrksKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-227 |
7.37e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.85 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGE----------TIS 78
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 79 QMSEDQAAAFRGANIGIVFQS--FHLIPNMTALENVAVPLEL---AGRRDAFDVAERELRAVGLGER---LTHYPSELSG 150
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhqgASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 151 GEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIAE 227
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-212 |
7.54e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 24 SSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFrganIGIVFQ-SFHL 102
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVFQnPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 IPNMTALENVAV-PLELAgrRDAFDVAER---ELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNL 178
Cdd:PRK13652 91 IFSPTVEQDIAFgPINLG--LDEETVAHRvssALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190
....*....|....*....|....*....|....
gi 489055174 179 DTATGRQIADLLFAKQRENGLTMVLVTHDPSLAA 212
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-225 |
7.74e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.02 E-value: 7.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmseDQAAAF 88
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 ------RGanigivfqsfhLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIAR 160
Cdd:COG4152 74 gylpeeRG-----------LYPKMKVGEQLVYLARLKGlsKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 161 ALAPSPKILIADEPTGNLDTATGRQIADLLFAkQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEElCDRIVIINKGRK 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
28-225 |
9.11e-23 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 92.72 E-value: 9.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaafRGANIGIVF--QSFHLIPN 105
Cdd:TIGR04406 16 VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMH-----ERARLGIGYlpQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVPLELAGRRDAfdvAERELRAVGLGERL--THYPSE----LSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:TIGR04406 91 LTVEENIMAVLEIRKDLDR---AEREERLEALLEEFqiSHLRDNkamsLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489055174 180 TATGRQIADLL-FAKQRENGltmVLVT-HDpslaAR-----CDREIPVRSGRI 225
Cdd:TIGR04406 168 PIAVGDIKKIIkHLKERGIG---VLITdHN----VRetldiCDRAYIISDGKV 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
29-213 |
1.86e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.54 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGI-----VKIAGETISQMSEDQAAAFRgaNIGIVFQSFHLI 103
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLYAPDVDPVEVRR--RIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNmTALENVAVPLELAGRRDAFD-VAERELRAVGL----GERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNL 178
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGDMDeLVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190
....*....|....*....|....*....|....*
gi 489055174 179 DTATGRQIADLLfaKQRENGLTMVLVTHDPSLAAR 213
Cdd:PRK14243 183 DPISTLRIEELM--HELKEQYTIIIVTHNMQQAAR 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-226 |
3.47e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.35 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHltlgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:PRK15439 10 PLLCARSIS----KQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FrgaNIGIVFQSFHLIPNMTALENVAvpLELAGRRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:PRK15439 86 L---GIYLVPQEPLLFPNLSVKENIL--FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 168 ILIADEPTGNLDTATGRQiadlLFAKQRE---NGLTMVLVTHD-PSLAARCDREIPVRSGRIA 226
Cdd:PRK15439 161 ILILDEPTASLTPAETER----LFSRIREllaQGVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-207 |
4.00e-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: 88.66 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKiagetisqmsedqaaafR 89
Cdd:cd03221 1 IELENLSKTYG----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-----------------W 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GANIGIVfqsfhlipnmtalenvavplelagrrdafdvaerelravglgerlthYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:cd03221 60 GSTVKIG-----------------------------------------------YFEQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*...
gi 489055174 170 IADEPTGNLDTATGRQIADLLfakQRENGlTMVLVTHD 207
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEAL---KEYPG-TVILVSHD 126
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-182 |
6.11e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.91 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHltlgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGetisqmsedQAAA 87
Cdd:PRK10762 3 ALLQLKGID----KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---------KEVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRG------ANIGIVFQSFHLIPNMTALENVAVPLELAGR------RDAFDVAERELRAVGLGERLTHYPSELSGGEQQR 155
Cdd:PRK10762 70 FNGpkssqeAGIGIIHQELNLIPQLTIAENIFLGREFVNRfgridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQM 149
|
170 180
....*....|....*....|....*...
gi 489055174 156 VAIARALAPSPKILIADEPTGNL-DTAT 182
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALtDTET 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
27-210 |
1.28e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 89.25 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGlehvdngivkiagetisQMSEDQAAAFrganigIVFQSFHLIPNM 106
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-----------------ALKGTPVAGC------VDVPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENVavplelaGRRDAFDVAERELRAVGLGERLTHY--PSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:COG2401 101 SLIDAI-------GRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|....*.
gi 489055174 185 QIADLLFAKQRENGLTMVLVTHDPSL 210
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHYDV 199
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-225 |
1.66e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.15 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKST-------LLMVLAGLEHVDN----------GIVKIAGeTISQMSEDQAAAfrg 90
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTiakhmnaLLIPSEGKVYVDGldtsdeenlwDIRNKAG-MVFQNPDNQIVA--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 aniGIVFQSFHLIPnmtalENVAV-PLELAGRRDafdvaeRELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:PRK13633 101 ---TIVEEDVAFGP-----ENLGIpPEEIRERVD------ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 170 IADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-207 |
1.69e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.82 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:PRK11831 7 LVDMRGVSFTRGNRC----IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPNMTALENVAVPLelagrRDAFDVAERELR--------AVGLGERLTHYPSELSGGEQQRVAIAR 160
Cdd:PRK11831 83 R-KRMSMLFQSGALFTDMNVFDNVAYPL-----REHTQLPAPLLHstvmmkleAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 161 ALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
9-206 |
2.53e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLG-HAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAA 87
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRGANIGIVFQ-SFHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERL-THYPSELSGGEQQRVAIARALA 163
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGipKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489055174 164 PSPKILIADEPTGNLDTATGRQIADlLFAKQRENGLTMVLVTH 206
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTH 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
26-205 |
2.82e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.46 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqaAAFRGANIGIVFQ--SFHLI 103
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD----YSYRSQRIRMIFQdpSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNMTALENVAVPLELagrRDAFDVAERE------LRAVGL-GERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTG 176
Cdd:PRK15112 102 PRQRISQILDFPLRL---NTDLEPEQREkqiietLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180
....*....|....*....|....*....
gi 489055174 177 NLDTATGRQIADLLFAKQRENGLTMVLVT 205
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-226 |
4.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.34 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmseDQAAAFRG--ANIGIVFQ-SFHLIPN 105
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKLSDirKKVGLVFQyPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVPLELAGRRDAfDVAERELRA---VGLG--ERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDT 180
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEE-EIENRVKRAmniVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 181 ATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRIA 226
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
14-206 |
4.91e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.93 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 14 DVHLTLGHaassvHVLKgVSLHIaPGQSV-GIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGAN 92
Cdd:PRK11144 5 NFKQQLGD-----LCLT-VNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 93 IGIVFQSFHLIPNMTALENVAVPLElAGRRDAFDvaeRELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIAD 172
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYGMA-KSMVAQFD---KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190
....*....|....*....|....*....|....
gi 489055174 173 EPTGNLDTATGRQIADLLFAKQRENGLTMVLVTH 206
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINIPILYVSH 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-210 |
5.48e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 31 GVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAafrgaNIGIV--FQSFHLIPNMTA 108
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-----RMGVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 109 LENVAVPLE-------LAG--RRDAFDVAERE--------LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIA 171
Cdd:PRK11300 98 IENLLVAQHqqlktglFSGllKTPAFRRAESEaldraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 172 DEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSL 210
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-227 |
7.81e-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: 86.70 E-value: 7.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDvhLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMsedqaaafr 89
Cdd:cd03369 7 IEVEN--LSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gaNIGIVFQSFHLIPNMTALENVAVPLELagrrDAFD-VAERELRAVglgERLTHYPSELSGGEQQRVAIARALAPSPKI 168
Cdd:cd03369 76 --PLEDLRSSLTIIPQDPTLFSGTIRSNL----DPFDeYSDEEIYGA---LRVSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 169 LIADEPTGNLDTATGRQIADLLfakqRE--NGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTI----REefTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-212 |
1.15e-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: 85.28 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTL--GHAassvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVkiagetisqmsedqaaa 87
Cdd:cd03223 1 IELENLSLATpdGRV-----LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 frganigivfqsfhlipnmtalenvavplELAGRRDAFDVAERELRAVG-LGERLThYP--SELSGGEQQRVAIARALAP 164
Cdd:cd03223 59 -----------------------------GMPEGEDLLFLPQRPYLPLGtLREQLI-YPwdDVLSGGEQQRLAFARLLLH 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLfakqRENGLTMVLVTHDPSLAA 212
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWK 152
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-225 |
1.15e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrgANIGIVFQSFHL-IPNMT 107
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIR---KLVGIVFQNPETqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAV--------PLELAGRRDafdvaeRELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:PRK13644 95 VEEDLAFgpenlclpPIEIRKRVD------RALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489055174 180 TATGRQIADLLfAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:PRK13644 169 PDSGIAVLERI-KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-206 |
1.42e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.04 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLE--HVDNGIVKIAGETISQMSEDQAAAf 88
Cdd:COG0396 2 EIKNLHVSVE----GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 rgANIGIVFQSFHLIPNM-------TALEnvAVPLELAGRRDAFDVAERELRAVGLGERLTHYP--SELSGGEQQRVAIA 159
Cdd:COG0396 77 --AGIFLAFQYPVEIPGVsvsnflrTALN--ARRGEELSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489055174 160 RALAPSPKILIADEPTGNLDTATGRQIADlLFAKQRENGLTMVLVTH 206
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDALRIVAE-GVNKLRSPDRGILIITH 198
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-225 |
2.06e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 16 HLTLGHAASSVhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAafrgANIGI 95
Cdd:PRK11231 7 NLTVGYGTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 96 VFQSfHLIPnmtalENVAV---------P-LELAGR-----RDAFDVAERELRAVGLGERLThypSELSGGEQQRVAIAR 160
Cdd:PRK11231 81 LPQH-HLTP-----EGITVrelvaygrsPwLSLWGRlsaedNARVNQAMEQTRINHLADRRL---TDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 161 ALAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHV 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-209 |
3.89e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVD---NGIVKIAGETI--SQMSedQAAAFrganigiVFQSFH 101
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIdaKEMR--AISAY-------VQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 102 LIPNMTALENVAVPLELAGRRDAFDVAERE-----LRAVGLG---ERLTHYPSE---LSGGEQQRVAIARALAPSPKILI 170
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRRVTKKEKRErvdevLQALGLRkcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 171 ADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPS 209
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVL-KGLAQKGKTIICTIHQPS 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-216 |
5.30e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 5 LVGPIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQ 84
Cdd:PRK09700 1 MATPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 85 AAAFrgaNIGIVFQSFHLIPNMTALENVAV---PLELAGRRDAFDVAERELRA------VGLGERLTHYPSELSGGEQQR 155
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLENLYIgrhLTKKVCGVNIIDWREMRVRAammllrVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 156 VAIARALAPSPKILIADEPTGNLdtaTGRQIaDLLFA---KQRENGLTMVLVTHD-PSLAARCDR 216
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSL---TNKEV-DYLFLimnQLRKEGTAIVYISHKlAEIRRICDR 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-208 |
5.67e-20 |
|
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: 84.33 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaafRGANIGIVFQSFHLIPNMT 107
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAG--RRDAFDVaereLRAVGLGErLTHYP-SELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:TIGR01189 90 ALENLHFWAAIHGgaQRTIEDA----LAAVGLTG-FEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....
gi 489055174 185 QIADLLFAKQRENGLTmVLVTHDP 208
Cdd:TIGR01189 165 LLAGLLRAHLARGGIV-LLTTHQD 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-224 |
8.51e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 8.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 24 SSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL-EHVD-NGIVKIAGETIsqmsedQAAAFR---GANIGIVFQ 98
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEEL------QASNIRdteRAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 99 SFHLIPNMTALENVAVPLEL--AGRRDaFDV----AERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIAD 172
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEItpGGIMD-YDAmylrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489055174 173 EPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGR 224
Cdd:PRK13549 169 EPTASLTESETAVLLDII-RDLKAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-207 |
1.59e-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: 86.91 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGivkiagetisqmsedQAAAFRGANIGIVFQSFHLIPNM 106
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG---------------EARPQPGIKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENV---------------AVPLELAGRRDAFDVA-------ERELRAVGLGE------------RLthyP------S 146
Cdd:TIGR03719 84 TVRENVeegvaeikdaldrfnEISAKYAEPDADFDKLaaeqaelQEIIDAADAWDldsqleiamdalRC---PpwdadvT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 147 ELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATgrqIADLLFAKQRENGlTMVLVTHD 207
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPG-TVVAVTHD 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-207 |
3.19e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 85.94 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGivkiagetisqmsedQAAAFRGANIGIVFQSFHLIPNM 106
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG---------------EARPAPGIKVGYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENV---------------AVPLELAGRRDAFD-VAER------ELRAVGLGE------------RLthyP------S 146
Cdd:PRK11819 86 TVRENVeegvaevkaaldrfnEIYAAYAEPDADFDaLAAEqgelqeIIDAADAWDldsqleiamdalRC---PpwdakvT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 147 ELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATgrqIADLlfakqrENGL-----TMVLVTHD 207
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWL------EQFLhdypgTVVAVTHD 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-224 |
3.23e-19 |
|
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: 86.03 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 25 SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL-EHVDngivkIAGETISQMSEDQAAAFR---GANIGIVFQSF 100
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyPHGT-----WDGEIYWSGSPLKASNIRdteRAGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 101 HLIPNMTALENVAVPLELAGRRDAFDVAERELRAVGLGERL-------THYPSELSGGEQQRVAIARALAPSPKILIADE 173
Cdd:TIGR02633 88 TLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELqldadnvTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489055174 174 PTGNLDTATGRQIADLLFAKQReNGLTMVLVTHD-PSLAARCDREIPVRSGR 224
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKA-HGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-225 |
8.05e-19 |
|
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: 81.75 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 24 SSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaaFRGANIGIVFQSFHLI 103
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK----YLHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNmTALENVAVPL---------ELAGRRDAFD-VAERELR-AVGLGERlthyPSELSGGEQQRVAIARALAPSPKILIAD 172
Cdd:cd03248 101 AR-SLQDNIAYGLqscsfecvkEAAQKAHAHSfISELASGyDTEVGEK----GSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489055174 173 EPTGNLDTATGRQIADLLFAKQRENglTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-227 |
8.16e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVhlTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmsEDQAAAFR 89
Cdd:PRK11176 342 IEFRNV--TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIpNMTALENVAVPLELAGRRDAFDVAERELRAVGLGERLTH--------YPSELSGGEQQRVAIARA 161
Cdd:PRK11176 417 -NQVALVSQNVHLF-NDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNgldtvigeNGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENglTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-225 |
1.13e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFrGANIGIVFQSFHLIPNMT 107
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS---SKAF-ARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAV---PLELA-GRrdaFDVAERE-----LRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNL 178
Cdd:PRK10575 102 VRELVAIgryPWHGAlGR---FGAADREkveeaISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 179 DTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-231 |
2.09e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.74 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKG-VSLHIAPGQSVGIVGPSGSGKSTLLMVLAG-LEHvdNGIVKIAGETISQMSEDQaaaFRgANIGIVFQSFHLiP 104
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPY--QGSLKINGIELRELDPES---WR-KHLSWVGQNPQL-P 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 NMTALENVavpleLAGRRDAFDVA-ERELRAVGLGERLTHYP-----------SELSGGEQQRVAIARALAPSPKILIAD 172
Cdd:PRK11174 436 HGTLRDNV-----LLGNPDASDEQlQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 173 EPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAEpvQG 231
Cdd:PRK11174 511 EPTASLDAHSEQLVMQAL--NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ--QG 565
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-225 |
2.41e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 19 LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdQAAAFRGanIGIVFQ 98
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL-HARARRG--IGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 99 SFHLIPNMTALENVAVPLELagrRDAFDVAERELRAVGLGER--LTHYPSE----LSGGEQQRVAIARALAPSPKILIAD 172
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQI---RDDLSAEQREDRANELMEEfhIEHLRDSmgqsLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489055174 173 EPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:PRK10895 163 EPFAGVDPISVIDIKRII-EHLRDSGLGVLITDHNvRETLAVCERAYIVSQGHL 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-206 |
3.17e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETisQMSEDQAAAFrGANIGIVFQSFHLIPN 105
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTAAL-AAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENV---AVP--LELAGRRDAFDVAERELRavGLGERLThyPS----ELSGGEQQRVAIARALAPSPKILIADEPTG 176
Cdd:PRK11288 94 MTVAENLylgQLPhkGGIVNRRLLNYEAREQLE--HLGVDID--PDtplkYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|..
gi 489055174 177 NLdtaTGRQIADL--LFAKQRENGLTMVLVTH 206
Cdd:PRK11288 170 SL---SAREIEQLfrVIRELRAEGRVILYVSH 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-207 |
5.31e-18 |
|
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: 82.29 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 3 EKLVGPIIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIaGETIsqmse 82
Cdd:TIGR03719 316 PRLGDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 83 dqaaafrgaNIGIVFQSF-HLIPNMTALEnvavplELAGRRDAFDVAEREL--RA-VGL----GERLTHYPSELSGGEQQ 154
Cdd:TIGR03719 386 ---------KLAYVDQSRdALDPNKTVWE------EISGGLDIIKLGKREIpsRAyVGRfnfkGSDQQKKVGQLSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLDTATGRQIADLL--FAkqrenGLTMVlVTHD 207
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALlnFA-----GCAVV-ISHD 499
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-206 |
8.60e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGAN------------I 93
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfkelrrrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 94 GIVFQ--SFHLIPNMTALENVAVPLELA-GRRDAFDVAERELRAVGLGER-LTHYPSELSGGEQQRVAIARALAPSPKIL 169
Cdd:PRK13631 119 SMVFQfpEYQLFKDTIEKDIMFGPVALGvKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 489055174 170 IADEPTGNLDTATGRQIADLLF-AKQreNGLTMVLVTH 206
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILdAKA--NNKTVFVITH 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-207 |
1.52e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKiagetisqmsedQAAA 87
Cdd:PRK09544 3 SLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 88 FRganIGIVFQSFHLIPNMTALENVAVPLELAGRRDAFDVAereLRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPK 167
Cdd:PRK09544 67 LR---IGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-207 |
1.13e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.54 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHvDNgiVKIAGETIS-------QM 80
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DN--WRVTADRMRfddidllRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 81 SEDQAAAFRGANIGIVFQSFH--LIPNmtalENVAVPLELA-------GR---------RDAFDVAERelraVGLGER-- 140
Cdd:PRK15093 79 SPRERRKLVGHNVSMIFQEPQscLDPS----ERVGRQLMQNipgwtykGRwwqrfgwrkRRAIELLHR----VGIKDHkd 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 141 -LTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:PRK15093 151 aMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-208 |
1.64e-16 |
|
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: 75.22 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQM--SEDQAAAFRGANIGIVfqsfhliPN 105
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrdSIARGLLYLGHAPGIK-------TT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVPLELAGRRDAFD-VAERELRavGLGERLTHYpseLSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:cd03231 88 LSVLENLRFWHADHSDEQVEEaLARVGLN--GFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|....
gi 489055174 185 QIADlLFAKQRENGLTMVLVTHDP 208
Cdd:cd03231 163 RFAE-AMAGHCARGGMVVLTTHQD 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-209 |
1.74e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDN--GIVKIAGETISQMSEDQaaafrganIGIVFQSFHLIPN 105
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKR--------TGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVA------VPLELAgRRDAFDVAERELRAVGLGERL-----THYPSELSGGEQQRVAIARALAPSPKILIADEP 174
Cdd:PLN03211 155 LTVRETLVfcsllrLPKSLT-KQEKILVAESVISELGLTKCEntiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|....*.
gi 489055174 175 TGNLD-TATGRQIADLLFAKQRenGLTMVLVTHDPS 209
Cdd:PLN03211 234 TSGLDaTAAYRLVLTLGSLAQK--GKTIVTSMHQPS 267
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-207 |
2.43e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEhVDNGIVKIAGETISQMSEDQAAAFRG--------ANIGIVFQ--SFH 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAylsqqqtpPFAMPVFQylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 102 LiPNMTALENVAVPLElagrrdafDVAERelraVGLGERLTHYPSELSGGEQQRVAIA-------RALAPSPKILIADEP 174
Cdd:PRK03695 94 Q-PDKTRTEAVASALN--------EVAEA----LGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|....
gi 489055174 175 TGNLDTAtgRQIA-DLLFAKQRENGLTMVLVTHD 207
Cdd:PRK03695 161 MNSLDVA--QQAAlDRLLSELCQQGIAVVMSSHD 192
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-210 |
6.20e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqMSEDQAAAFRgANIGIVFQS------FH 101
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALR-QQVATVFQDpeqqifYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 102 LIPNMTA--LENVAVPLELAGRR--DAFDVAErelravglGERLTHYPSE-LSGGEQQRVAIARALAPSPKILIADEPTG 176
Cdd:PRK13638 94 DIDSDIAfsLRNLGVPEAEITRRvdEALTLVD--------AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190
....*....|....*....|....*....|....
gi 489055174 177 NLDTAtGRQIADLLFAKQRENGLTMVLVTHDPSL 210
Cdd:PRK13638 166 GLDPA-GRTQMIAIIRRIVAQGNHVIISSHDIDL 198
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-227 |
1.23e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.39 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASSVhvlKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsqmSEDQAAAFR 89
Cdd:PRK10522 323 LELRNVTFAYQDNGFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNMTALENVAVPLELagrrdafdvAERELRAVGLGERLTHYPSE-----LSGGEQQRVAIARALAP 164
Cdd:PRK10522 397 -KLFSAVFTDFHLFDQLLGPEGKPANPAL---------VEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 165 SPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-182 |
1.55e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.37 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 34 LHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGE-TISQMSEDQAAAFRG----------ANIGIVFQSFHL 102
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQQDPPRNVEGtvydfvaegiEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 IPNMTALENVAVPL-ELAGRRDAFDVA---ERELRAVGLGERLTHYP----SELSGGEQQRVAIARALAPSPKILIADEP 174
Cdd:PRK11147 104 ISHLVETDPSEKNLnELAKLQEQLDHHnlwQLENRINEVLAQLGLDPdaalSSLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
....*...
gi 489055174 175 TGNLDTAT 182
Cdd:PRK11147 184 TNHLDIET 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-206 |
2.01e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGlehvdngiVKIAGETISQMS-EDQAAAFRGAN------IGIVFQ 98
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG--------VYPHGSYEGEILfDGEVCRFKDIRdsealgIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 99 SFHLIPNMTALENVAVPLELAGR-----RDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADE 173
Cdd:NF040905 86 ELALIPYLSIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190
....*....|....*....|....*....|...
gi 489055174 174 PTGNLDTATGRQIADLLFaKQRENGLTMVLVTH 206
Cdd:NF040905 166 PTAALNEEDSAALLDLLL-ELKAQGITSIIISH 197
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-202 |
2.37e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.19 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 19 LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGivfq 98
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 99 sfhLIPNMTALENVAVPLELAGRRdAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARA-LAPSPKILIaDEPTGN 177
Cdd:PRK13543 93 ---LKADLSTLENLHFLCGLHGRR-AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYAN 167
|
170 180
....*....|....*....|....*
gi 489055174 178 LDTATGRQIADLLFAKQRENGLTMV 202
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGGAALV 192
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-210 |
2.99e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 1 MTEKLvgPIIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGleH----VDNGIVKIAGET 76
Cdd:CHL00131 1 MNKNK--PILEIKNLHASVN----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HpaykILEGDILFKGES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 77 ISQMSEDQAaafrgANIGIvFQSFHL---IP---NMTALE------------NVAVPLELagrrdaFDVAERELRAVGLG 138
Cdd:CHL00131 73 ILDLEPEER-----AHLGI-FLAFQYpieIPgvsNADFLRlaynskrkfqglPELDPLEF------LEIINEKLKLVGMD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 139 ER-LTHYPSE-LSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL--FAKQrENGltMVLVTHDPSL 210
Cdd:CHL00131 141 PSfLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGInkLMTS-ENS--IILITHYQRL 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-227 |
3.18e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 30 KGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrgANIGIVFQSFH---LIPNM 106
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVK---KGMAYITESRRdngFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENVAVP--LELAGRRDAFDV-----------AERELRAV---GLGERLThypsELSGGEQQRVAIARALAPSPKILI 170
Cdd:PRK09700 357 SIAQNMAISrsLKDGGYKGAMGLfhevdeqrtaeNQRELLALkchSVNQNIT----ELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 171 ADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRIAE 227
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVM-RQLADDGKVILMVSSElPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-227 |
4.37e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLGHAASsvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqaAAFR 89
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 gANIGIVFQSFHLIPNmTALENVAVplelaGRRDAFDVAERELRAVGLGE-----------RLTHYPSELSGGEQQRVAI 158
Cdd:PRK10790 415 -QGVAMVQQDPVVLAD-TFLANVTL-----GRDISEEQVWQALETVQLAElarslpdglytPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 159 ARALAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENgLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREH-TTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-220 |
5.47e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLehvdngIVKIAGETI-------SQMSEDQAAAFRGANIGIVFQ--S 99
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTIvgdyaipANLKKIKEVKRLRKEIGLVFQfpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 FHLIPNMTALENVAVPLEL-AGRRDAFDVAERELRAVGLGER-LTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGN 177
Cdd:PRK13645 101 YQLFQETIEKDIAFGPVNLgENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489055174 178 LDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPV 220
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-206 |
6.16e-15 |
|
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: 73.89 E-value: 6.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 40 QSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsqmsEDQAAAFRgANIGIVFQSFHLIPNMTALENVAVPLELA 119
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 120 GRrdAFDVAERELRAV----GLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFakQR 195
Cdd:TIGR01257 1032 GR--SWEEAQLEMEAMledtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL--KY 1107
|
170
....*....|.
gi 489055174 196 ENGLTMVLVTH 206
Cdd:TIGR01257 1108 RSGRTIIMSTH 1118
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-207 |
1.00e-14 |
|
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: 71.29 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 36 IAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIS----QMSEDQAAAFRGANIGIVfQSFHLIPNMTAleN 111
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRDLLSSIT-KDFYTHPYFKT--E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 112 VAVPLELAgrrdafDVAERELRavglgerlthypsELSGGEQQRVAIARALAPSPKILIADEPTGNLD-------TATGR 184
Cdd:cd03237 99 IAKPLQIE------QILDREVP-------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSKVIR 159
|
170 180
....*....|....*....|...
gi 489055174 185 QIADllfakqrENGLTMVLVTHD 207
Cdd:cd03237 160 RFAE-------NNEKTAFVVEHD 175
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-225 |
1.01e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQaaafrGANIGIVFQSFH-----LI 103
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-----GLANGIVYISEDrkrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 PNMTALENVAVPL-----ELAGRRDAfdvaERELRAVGLGERL--THYPS------ELSGGEQQRVAIARALAPSPKILI 170
Cdd:PRK10762 343 LGMSVKENMSLTAlryfsRAGGSLKH----ADEQQAVSDFIRLfnIKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 171 ADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-227 |
1.35e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.44 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 23 ASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDqaaAFRGaNIGIVFQSFHL 102
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD---SWRS-RLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 IPNMTAlENVAVplelaGRRDAF-DVAERELRAVGLGE---RLTH-YPSE-------LSGGEQQRVAIARALAPSPKILI 170
Cdd:PRK10789 401 FSDTVA-NNIAL-----GRPDATqQEIEHVARLASVHDdilRLPQgYDTEvgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 171 ADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-227 |
2.33e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.12 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmsedqAAAFRGANigivfQSFHLIP--- 104
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG------AYGLRELR-----RQFSMIPqdp 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 ---NMTALENV-----AVP------LELAGRRDAFdVAERElravGLGERLTHYPSELSGGEQQRVAIARALAP--SPKI 168
Cdd:PTZ00243 1394 vlfDGTVRQNVdpfleASSaevwaaLELVGLRERV-ASESE----GIDSRVLEGGSNYSVGQRQLMCMARALLKkgSGFI 1468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 169 LIaDEPTGNLDTATGRQI-ADLLFAKqreNGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PTZ00243 1469 LM-DEATANIDPALDRQIqATVMSAF---SAYTVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-209 |
2.69e-14 |
|
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: 69.21 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 14 DVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVD---NGIVKIAGETIsqmseDQAAAFRG 90
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-----KEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 ANIGIVFQSFHLIPNMTALENVAVPLELAGrrDAFdvaereLRAVglgerlthypselSGGEQQRVAIARALAPSPKILI 170
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFALRCKG--NEF------VRGI-------------SGGERKRVSIAEALVSRASVLC 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 171 ADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPS 209
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAS 180
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-207 |
6.02e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 6 VGP-----IIELEDVHLTLGHaassvHVL-KGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIaGETISQ 79
Cdd:PRK11819 316 PGPrlgdkVIEAENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 80 MSEDQaaaFRGAnigivfqsfhLIPNMTALEnvavplELAGRRDAFDVAEREL--RA---------------VGlgerlt 142
Cdd:PRK11819 390 AYVDQ---SRDA----------LDPNKTVWE------EISGGLDIIKVGNREIpsRAyvgrfnfkggdqqkkVG------ 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055174 143 hypsELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLL--FAkqrenGLTMVlVTHD 207
Cdd:PRK11819 445 ----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALleFP-----GCAVV-ISHD 501
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-227 |
8.92e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAG-LEHVDNGIVKIAGET--ISQMSEDQAAAFRgANI--GIVFQS--FH 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVayVPQVSWIFNATVR-ENIlfGSDFESerYW 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 102 LIPNMTALENvavPLELAGRRDAFDVAERELravglgerlthypsELSGGEQQRVAIARALAPSPKILIADEPTGNLDTA 181
Cdd:PLN03232 712 RAIDVTALQH---DLDLLPGRDLTEIGERGV--------------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489055174 182 TGRQIADLLFaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PLN03232 775 VAHQVFDSCM-KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-194 |
9.96e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrganIGIVF-----QSFHLI--- 103
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA-----RGLVYlpedrQSSGLYlda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 P---NMTALENVAVPLELAGRRDAfDVAERELRAVGLgeRLTHYPSE---LSGGEQQRVAIARALAPSPKILIADEPTGN 177
Cdd:PRK15439 357 PlawNVCALTHNRRGFWIKPAREN-AVLERYRRALNI--KFNHAEQAartLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170
....*....|....*....
gi 489055174 178 LDTATGRQIADLL--FAKQ 194
Cdd:PRK15439 434 VDVSARNDIYQLIrsIAAQ 452
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-227 |
1.32e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVHLTlgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAA 86
Cdd:PLN03232 1232 RGSIKFEDVHLR--YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 AFRGAnIGIVFQS---------FHLIPnmTALENVAVPLELAGRRDAFDVAERElrAVGLGERLTHYPSELSGGEQQRVA 157
Cdd:PLN03232 1307 DLRRV-LSIIPQSpvlfsgtvrFNIDP--FSEHNDADLWEALERAHIKDVIDRN--PFGLDAEVSEGGENFSVGQRQLLS 1381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 158 IARALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDVRTDSLIQRTI--REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-225 |
1.82e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAG---LEHVDNGI-----VKIAGETISQMSEDQAAAFRGANIGIVFQS 99
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltGGGAPRGArvtgdVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 FHLIPNMTALENVAVPLELAG---RRDAfDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALA---------PSPK 167
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGaltHRDG-EIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 168 ILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAAR-CDREIPVRSGRI 225
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAI 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-227 |
2.05e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFRgANIGIVFQS-------- 99
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQApvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 -FHLIPnmTALENVAVPLELAGRRDAFDVAERElrAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNL 178
Cdd:PLN03130 1330 rFNLDP--FNEHNDADLWESLERAHLKDVIRRN--SLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489055174 179 DTATgrqiaDLLFAKQ-RE--NGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PLN03130 1406 DVRT-----DALIQKTiREefKSCTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-206 |
2.07e-13 |
|
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: 69.17 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 17 LTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDnGIVKIAGETISQMSEDQaaaFRGAnIGIV 96
Cdd:TIGR01271 1223 LTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQT---WRKA-FGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 97 FQSFhLIPNMTALENVAvPLELAGRRDAFDVAERelraVGLGERLTHYPSE-----------LSGGEQQRVAIARALAPS 165
Cdd:TIGR01271 1298 PQKV-FIFSGTFRKNLD-PYEQWSDEEIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSK 1371
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTH 206
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTL--KQSFSNCTVILSEH 1410
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-207 |
2.61e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQS-----VGIVGPSGSGKSTLLMVLAGLEHVDNG----IVKIA----------GETISQMSEDQAAAFR 89
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpELKISykpqyikpdyDGTVEDLLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 90 GanigivfqSFHLipnmtalENVAVPLELAgrrdafDVAERELRavglgerlthypsELSGGEQQRVAIARALAPSPKIL 169
Cdd:PRK13409 430 S--------SYYK-------SEIIKPLQLE------RLLDKNVK-------------DLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489055174 170 IADEPTGNLD----TATGRQIADLLfakqRENGLTMVLVTHD 207
Cdd:PRK13409 476 LLDEPSAHLDveqrLAVAKAIRRIA----EEREATALVVDHD 513
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-225 |
2.63e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGhaasSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAF 88
Cdd:NF033858 1 VARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 R--------GANigivfqsfhLIPNMTALENvavpLELAGRRDAFDVAERE------LRAVGLGERLTHYPSELSGGEQQ 154
Cdd:NF033858 77 RiaympqglGKN---------LYPTLSVFEN----LDFFGRLFGQDAAERRrridelLRATGLAPFADRPAGKLSGGMKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLDTATGRQ----IADLlfaKQRENGLTmVLV-THDPSLAARCDREIPVRSGRI 225
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQfwelIDRI---RAERPGMS-VLVaTAYMEEAERFDWLVAMDAGRV 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-225 |
3.22e-13 |
|
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: 67.19 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 11 ELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDnGIVKIAGETISQMSEDQaaaFRG 90
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQK---WRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 91 AnIGIVFQSFhLIPNMTALENVAvPLELAGRRDAFDVAERelraVGLGERLTHYPSE-----------LSGGEQQRVAIA 159
Cdd:cd03289 78 A-FGVIPQKV-FIFSGTFRKNLD-PYGKWSDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 160 RALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRI 225
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-227 |
3.95e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLL-MVLAGLEHVDNGIVKIAGET--ISQMSEDQAAAFRGaNI--GIVFQS-- 99
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRGTVayVPQVSWIFNATVRD-NIlfGSPFDPer 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 FHLIPNMTALENvavPLELAGRRDAFDVAERELravglgerlthypsELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:PLN03130 710 YERAIDVTALQH---DLDLLPGGDLTEIGERGV--------------NISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 180 TATGRQIADLLFaKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:PLN03130 773 AHVGRQVFDKCI-KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
8-226 |
1.08e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 8 PIIELEDVHLTL--GHAAssvhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQmsedqa 85
Cdd:PRK15056 5 AGIVVNDVTVTWrnGHTA-----LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 aAFRGANIGIVFQSFHLIPNMTAL-ENVAVP--------LELAGRRDAfDVAERELRAVGLGERLTHYPSELSGGEQQRV 156
Cdd:PRK15056 74 -ALQKNLVAYVPQSEEVDWSFPVLvEDVVMMgryghmgwLRRAKKRDR-QIVTAALARVDMVEFRHRQIGELSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 157 AIARALAPSPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGRIA 226
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLL-RELRDEGKTMLVSTHNlGSVTEFCDYTVMVKGTVLA 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-236 |
1.32e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLTLgHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKST---LLMVLAGLEHvDNGIV-------KIAGETISQ 79
Cdd:PTZ00265 1166 IEIMDVNFRY-ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTvmsLLMRFYDLKN-DHHIVfknehtnDMTNEQDYQ 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 80 MSEDQAAAFRGAN-----------------------------------------IGIVFQSFHLIpNMTALENVAVPLEL 118
Cdd:PTZ00265 1244 GDEEQNVGMKNVNefsltkeggsgedstvfknsgkilldgvdicdynlkdlrnlFSIVSQEPMLF-NMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 119 AGRRDAfdvaERELRAVGLGERLTHYPSE-----------LSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIA 187
Cdd:PTZ00265 1323 ATREDV----KRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489055174 188 DLLFAKQRENGLTMVLVTHDPSLAARCDREI----PVRSGRIaepVQGAGIPE 236
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITIAHRIASIKRSDKIVvfnnPDRTGSF---VQAHGTHE 1448
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-207 |
1.41e-12 |
|
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: 66.35 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQ-----SVGIVGPSGSGKSTLLMVLAGLEHVDNGIV----KIA--GETISQMSEDQAAAF-RGANIGIV 96
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlKISykPQYISPDYDGTVEEFlRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 97 FQSFHLipnmtalENVAVPLELAgrrdafDVAERELravglgerlthypSELSGGEQQRVAIARALAPSPKILIADEPTG 176
Cdd:COG1245 431 GSSYYK-------TEIIKPLGLE------KLLDKNV-------------KDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190
....*....|....*....|....*....|....*
gi 489055174 177 NLD----TATGRQIADLLfakqRENGLTMVLVTHD 207
Cdd:COG1245 485 HLDveqrLAVAKAIRRFA----ENRGKTAMVVDHD 515
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-209 |
3.15e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.42 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVdnGIVKiaGE-TISQMSEDQA 85
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTA--GVIT--GEiLINGRPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 86 AAFRganIGIVFQSFHLIPNMTalenVAVPLELAGRrdafdvaereLRAVGLGERlthypselsggeqQRVAIARALAPS 165
Cdd:cd03232 77 FQRS---TGYVEQQDVHSPNLT----VREALRFSAL----------LRGLSVEQR-------------KRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489055174 166 PKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPS 209
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFL-KKLADSGQAILCTIHQPS 169
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-207 |
4.77e-12 |
|
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: 63.92 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 37 APGQSVGIVGPSGSGKSTLLMVLAGlEHVDNgivkiAGETISQMSEDQA-AAFRGANIGIVF--------------QSFH 101
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAG-KLKPN-----LGKFDDPPDWDEIlDEFRGSELQNYFtkllegdvkvivkpQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 102 LIPNmTALENVAVPLELAGRRDAFD--VAERELRAVglgerLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD 179
Cdd:cd03236 98 LIPK-AVKGKVGELLKKKDERGKLDelVDQLELRHV-----LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|....*...
gi 489055174 180 TATgRQIADLLFAKQRENGLTMVLVTHD 207
Cdd:cd03236 172 IKQ-RLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-214 |
5.06e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGlEH---VDNGIV-----KIAGETISQMSEdqaaafrgaNIGIVFQS 99
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHpqgYSNDLTlfgrrRGSGETIWDIKK---------HIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 FHLIPNM-TALENVAvpleLAGRRDAFDV-----------AERELRAVGLGERLTHYP-SELSGGEQQRVAIARALAPSP 166
Cdd:PRK10938 345 LHLDYRVsTSVRNVI----LSGFFDSIGIyqavsdrqqklAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489055174 167 KILIADEPTGNLDTaTGRQIA----DLLFAkqreNGLTMVL-VTHDPSLAARC 214
Cdd:PRK10938 421 TLLILDEPLQGLDP-LNRQLVrrfvDVLIS----EGETQLLfVSHHAEDAPAC 468
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-207 |
7.82e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 38 PGQSVGIVGPSGSGKSTLLMVLAGlEHVDNgivkiAGETISQMSEDQA-AAFRGANIGIVF--------------QSFHL 102
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSG-ELIPN-----LGDYEEEPSWDEVlKRFRGTELQNYFkklyngeikvvhkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 IPNmtALE-NVAVPLELAGRRDAFD-VAERelraVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDT 180
Cdd:PRK13409 172 IPK--VFKgKVRELLKKVDERGKLDeVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190
....*....|....*....|....*....|..
gi 489055174 181 atgRQ---IADLLfakqRE--NGLTMVLVTHD 207
Cdd:PRK13409 246 ---RQrlnVARLI----RElaEGKYVLVVEHD 270
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-216 |
1.64e-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: 63.88 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 17 LTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmsedqaaafrgANIGIV 96
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------------TNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 97 FQSFHLIPNMTALENVavpleLAGRRDAF--------------DVAERELRAVGLGERLTHYPSELSGGEQQRVAIARAL 162
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDL-----LTGREHLYlyarlrgvpaeeieKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 163 APSPKILIADEPTGNLDTATGRQIADLLFAKQREnGLTMVLVTHD-PSLAARCDR 216
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSmEECEALCTR 2139
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-227 |
2.82e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLL-MVLAGLEHVDnGIVKIAGetisqmsedqaaafrgaNIGIVFQSfHLIPNMT 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLsALLAEMDKVE-GHVHMKG-----------------SVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAGRRdafdvAERELRAVGLGERLTHYPS-----------ELSGGEQQRVAIARALAPSPKILIADEPTG 176
Cdd:TIGR00957 715 LRENILFGKALNEKY-----YQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489055174 177 NLDTATGRQIAD-LLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIAE 227
Cdd:TIGR00957 790 AVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-216 |
4.14e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISqmSEDQAAAFRganIGIVFQSFHLIPNMTALEN 111
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--AGDIATRRR---VGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 112 vavpLELAGRrdAFDVAERELRA--------VGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATG 183
Cdd:NF033858 360 ----LELHAR--LFHLPAAEIAArvaemlerFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
170 180 190
....*....|....*....|....*....|...
gi 489055174 184 RQIADLLFAKQRENGLTMVLVTHDPSLAARCDR 216
Cdd:NF033858 434 DMFWRLLIELSREDGVTIFISTHFMNEAERCDR 466
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-206 |
7.17e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLE--HVDNGIVKIAGETISQMSEDQAAafrGANIGIVFQSFHLIPN 105
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 M-------TALENV-----AVPLElagRRDAFDVAERELRAVGLGERLTHYPSEL--SGGEQQRVAIARALAPSPKILIA 171
Cdd:PRK09580 93 VsnqfflqTALNAVrsyrgQEPLD---RFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 489055174 172 DEPTGNLDTATGRQIADLLFAkQRENGLTMVLVTH 206
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNS-LRDGKRSFIIVTH 203
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-233 |
8.27e-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: 61.35 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 10 IELEDVHLT-LGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsqmSEDQAAAF 88
Cdd:COG4615 328 LELRGVTYRyPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgANIGIVFQSFHLIPnmtalenvavplELAGRRDAFDV--AERELRAVGLGERLTHY-----PSELSGGEQQRVAIARA 161
Cdd:COG4615 405 R-QLFSAVFSDFHLFD------------RLLGLDGEADParARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVA 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 162 LAPSPKILIADE------PtgnldtaTGRQIadllFAKQ-----RENGLTMVLVTHDPSLAARCDREIPVRSGRIAEPVQ 230
Cdd:COG4615 472 LLEDRPILVFDEwaadqdP-------EFRRV----FYTEllpelKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTG 540
|
...
gi 489055174 231 GAG 233
Cdd:COG4615 541 PAA 543
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-205 |
9.38e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGEtISQMSEdqaaafrganigivfqsFHLIPNMT 107
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQ-----------------FSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVavplelagrrdAFDVAERELR------AVGLGERLTHYPSE-----------LSGGEQQRVAIARALAPSPKILI 170
Cdd:cd03291 114 IKENI-----------IFGVSYDEYRyksvvkACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYL 182
|
170 180 190
....*....|....*....|....*....|....*
gi 489055174 171 ADEPTGNLDTATGRQIADLLFAKQRENGlTMVLVT 205
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMANK-TRILVT 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-207 |
9.66e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAG-LEHVDNGIVKIAGETISQMSEDQAAafrganigivFQSFHLI------- 103
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPSAGNVSLDPNERLGKLRQDQFA----------FEEFTVLdtvimgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 ----------------PNMTALENVAVPlELAGRRDAFDVAERELRA------VGLGERLtHYP--SELSGGEQQRVAIA 159
Cdd:PRK15064 90 telwevkqerdriyalPEMSEEDGMKVA-DLEVKFAEMDGYTAEARAgelllgVGIPEEQ-HYGlmSEVAPGWKLRVLLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 160 RALAPSPKILIADEPTGNLDTATGRQIADLLfaKQRENglTMVLVTHD 207
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINTIRWLEDVL--NERNS--TMIIISHD 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-207 |
1.31e-10 |
|
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: 60.57 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 38 PGQSVGIVGPSGSGKSTLLMVLAGLehvdngIVKIAGETISQMSEDQA-AAFRGANIGIVF--------------QSFHL 102
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGE------LKPNLGDYDEEPSWDEVlKRFRGTELQDYFkklangeikvahkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 IPNMTALeNVAVPLELAGRRDAFD-VAERelraVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLD-- 179
Cdd:COG1245 172 IPKVFKG-TVRELLEKVDERGKLDeLAEK----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiy 246
|
170 180 190
....*....|....*....|....*....|
gi 489055174 180 --TATGRQIADLLfakqrENGLTMVLVTHD 207
Cdd:COG1245 247 qrLNVARLIRELA-----EEGKYVLVVEHD 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-190 |
3.20e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 25 SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAG-LEHVDNGIV-KIAGETISQmsEDQAAAFRGANIGIVFQSFHL 102
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIGVEgVITYDGITP--EEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 iPNMTalenVAVPLELAGR------------RDAFDVAERELRAVGLGerLTH---------YPSELSGGEQQRVAIARA 161
Cdd:TIGR00956 151 -PHLT----VGETLDFAARcktpqnrpdgvsREEYAKHIADVYMATYG--LSHtrntkvgndFVRGVSGGERKRVSIAEA 223
|
170 180
....*....|....*....|....*....
gi 489055174 162 LAPSPKILIADEPTGNLDTATGRQIADLL 190
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRAL 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-213 |
3.80e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 1 MTEKLVGPIIELEDvhltLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIA-GETISQ 79
Cdd:PRK15064 311 QDKKLHRNALEVEN----LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSeNANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 80 MSEDQAAAFRGanigivfqsfhlipNMTALENVAvplelAGRRDAFDvaERELRAVgLGERL------THYPSELSGGEQ 153
Cdd:PRK15064 387 YAQDHAYDFEN--------------DLTLFDWMS-----QWRQEGDD--EQAVRGT-LGRLLfsqddiKKSVKVLSGGEK 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055174 154 QRVAIARALAPSPKILIADEPTGNLDTATgrqIADLLFAKQRENGlTMVLVTHD----PSLAAR 213
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKYEG-TLIFVSHDrefvSSLATR 504
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-223 |
6.38e-10 |
|
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: 57.34 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 24 SSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHLI 103
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 104 pNMTALENVAVPLELAGRR-----DAFDVA-ERELRAVG----LGERLTHypseLSGGEQQRVAIARALAPSPKILIADE 173
Cdd:cd03290 92 -NATVEENITFGSPFNKQRykavtDACSLQpDIDLLPFGdqteIGERGIN----LSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489055174 174 PTGNLDTatgrQIADLLFAKQ-----RENGLTMVLVTHDPSLAARCDREIPVRSG 223
Cdd:cd03290 167 PFSALDI----HLSDHLMQEGilkflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-205 |
6.41e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGEtisqmsedqaaafrganIGIVFQSFHLIPNmT 107
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVavplelagrrdAFDVAERELR------AVGLGERLTHYPSE-----------LSGGEQQRVAIARALAPSPKILI 170
Cdd:TIGR01271 503 IKDNI-----------IFGLSYDEYRytsvikACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYL 571
|
170 180 190
....*....|....*....|....*....|....*
gi 489055174 171 ADEPTGNLDTATGRQIADLLFAKQRENGlTMVLVT 205
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFESCLCKLMSNK-TRILVT 605
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-224 |
6.87e-10 |
|
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: 55.84 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 38 PGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVK-IAGETIsqmsedqaaafrganigivfqsfhlipnmtalenvavpl 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 117 elagrrdafdvaERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQI-----ADLLF 191
Cdd:smart00382 42 ------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 192 AKQRENGLTMVLVTHDPS------LAARCDREIPVRSGR 224
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-182 |
7.35e-10 |
|
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: 58.80 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETIsqmsedqaaafrgANIGIVFQSFHL--IPN 105
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-------------AKIGLHDLRFKItiIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTAL-----------------ENVAVPLELAGRRDAFDvaerelravGLGERLTHYPSE----LSGGEQQRVAIARALAP 164
Cdd:TIGR00957 1368 DPVLfsgslrmnldpfsqysdEEVWWALELAHLKTFVS---------ALPDKLDHECAEggenLSVGQRQLVCLARALLR 1438
|
170
....*....|....*...
gi 489055174 165 SPKILIADEPTGNLDTAT 182
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLET 1456
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-182 |
1.29e-09 |
|
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: 56.84 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSedqAAAFRgANIGIVFQS-------- 99
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLR-SRLSIILQDpilfsgsi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 -FHLIPNMTALEN-VAVPLELAGRRDAFDVAERELRAVglgerLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGN 177
Cdd:cd03288 112 rFNLDPECKCTDDrLWEALEIAQLKNMVKSLPGGLDAV-----VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
....*
gi 489055174 178 LDTAT 182
Cdd:cd03288 187 IDMAT 191
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-217 |
1.30e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQ--MSEDQAAAFRGANIGIVfqsfhliPN 105
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlCTYQKQLCFVGHRSGIN-------PY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVPLELAGRRDAFDvaerELRAVGLGERLTHYPSE-LSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGR 184
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVGIT----ELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180 190
....*....|....*....|....*....|...
gi 489055174 185 QIADLLFAkQRENGLTMVLVTHDPSLAARCDRE 217
Cdd:PRK13540 165 TIITKIQE-HRAKGGAVLLTSHQDLPLNKADYE 196
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-218 |
1.65e-09 |
|
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: 55.41 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 25 SVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLlmVLAGLEhvdngivkiagETISQMSEDQAAAFrGANIGIVFQSFhlip 104
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY-----------ASGKARLISFLPKF-SRNKLIFIDQL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 105 nmtalenvavplelagrrdafdvaeRELRAVGLGE-RLTHYPSELSGGEQQRVAIARALA--PSPKILIADEPTGNLDTA 181
Cdd:cd03238 69 -------------------------QFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|....*..
gi 489055174 182 TGRQIADLLfAKQRENGLTMVLVTHDPSLAARCDREI 218
Cdd:cd03238 124 DINQLLEVI-KGLIDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-215 |
2.26e-09 |
|
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: 56.08 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLM----------------------VLAGLEHVDNgIVKIAGETISQMSED 83
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrlhlkkeqpgnhdRIEGLEHIDK-VIVIDQSPIGRTPRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 84 QAAAFRGA--NIGIVF--------------------QSFHLIPNMTALENV----AVPlelagrrdafdVAERELRA--- 134
Cdd:cd03271 87 NPATYTGVfdEIRELFcevckgkrynretlevrykgKSIADVLDMTVEEALeffeNIP-----------KIARKLQTlcd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 135 VGLGE-RLTHYPSELSGGEQQRVAIARAL---APSPKILIADEPTGNLDTAtgrQIADLLFAKQR--ENGLTMVLVTHDP 208
Cdd:cd03271 156 VGLGYiKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFH---DVKKLLEVLQRlvDKGNTVVVIEHNL 232
|
....*..
gi 489055174 209 SLAARCD 215
Cdd:cd03271 233 DVIKCAD 239
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
33-210 |
2.62e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.07 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 33 SLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGEtisqmsedqaaafrgANIGIVFQSfhliPNM---TAL 109
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK---------------GKLFYVPQR----PYMtlgTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 110 ENVAVP--LELAGRRDAFD-VAERELRAVGLGERLTH---------YPSELSGGEQQRVAIARALAPSPKILIADEPTgn 177
Cdd:TIGR00954 533 DQIIYPdsSEDMKRRGLSDkDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECT-- 610
|
170 180 190
....*....|....*....|....*....|...
gi 489055174 178 ldTATGRQIADLLFAKQRENGLTMVLVTHDPSL 210
Cdd:TIGR00954 611 --SAVSVDVEGYMYRLCREFGITLFSVSHRKSL 641
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-226 |
4.53e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 18 TLGHAASSVHVLKG------VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdqAAAFRGa 91
Cdd:PRK11288 252 PLGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP--RDAIRA- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 92 niGIVF-----QSFHLIPNMTALENVAVP---------LELAGRRDAfDVAERELRAVGLGERLTHYP-SELSGGEQQRV 156
Cdd:PRK11288 329 --GIMLcpedrKAEGIIPVHSVADNINISarrhhlragCLINNRWEA-ENADRFIRSLNIKTPSREQLiMNLSGGNQQKA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 157 AIARALAPSPKILIADEPTGNLDTATGRQIADLLF--AKQrenGLTMVLVTHD-PSLAARCDREIPVRSGRIA 226
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYelAAQ---GVAVLFVSSDlPEVLGVADRIVVMREGRIA 475
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-210 |
5.81e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 3 EKLVGPIIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGlehvdngivkiageTISQMSE 82
Cdd:PRK10636 306 ESLPNPLLKMEKVSAGYGDRI----ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--------------ELAPVSG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 83 DQAAAfRGANIGIVFQsfHLIPNMTALENvavPLE-LAgrRDAFDVAERELR----AVGL-GERLTHYPSELSGGEQQRV 156
Cdd:PRK10636 368 EIGLA-KGIKLGYFAQ--HQLEFLRADES---PLQhLA--RLAPQELEQKLRdylgGFGFqGDKVTEETRRFSGGEKARL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489055174 157 AIARALAPSPKILIADEPTGNLDTATGRQIADLLFakQRENGLtmVLVTHDPSL 210
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI--DFEGAL--VVVSHDRHL 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-207 |
6.33e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 4 KLVgpiIELEDVHLTLGHAAssvhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIaGETISQMSED 83
Cdd:PRK11147 317 KIV---FEMENVNYQIDGKQ----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 84 QaaaFRGAnigivfqsfhLIPNMTALENVAvplelAGRRDAfDVAERELRAVG-LGERLTHyPSE-------LSGGEQQR 155
Cdd:PRK11147 389 Q---HRAE----------LDPEKTVMDNLA-----EGKQEV-MVNGRPRHVLGyLQDFLFH-PKRamtpvkaLSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489055174 156 VAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQrenGlTMVLVTHD 207
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ---G-TVLLVSHD 496
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-204 |
1.11e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 33 SLHIAPGQSVGIVGPSGSGKSTLLMVLAGlehvdnGIVKIAGETISQMSEdqaaafrganigIVFQSFHLIPNMTALE-- 110
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG------ELPLLSGERQSQFSH------------ITRLSFEQLQKLVSDEwq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 111 ----NVAVPLELAGRRDAFDVAERELRAVGLGERL------THYPSE----LSGGEQQRVAIARALAPSPKILIADEPTG 176
Cdd:PRK10938 85 rnntDMLSPGEDDTGRTTAEIIQDEVKDPARCEQLaqqfgiTALLDRrfkyLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|....*...
gi 489055174 177 NLDTATGRQIADLLFAKQREnGLTMVLV 204
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-209 |
3.38e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 9 IIELEDVHLTLGHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAglEHVDNGIVKiAGETISQMSEDQAAAF 88
Cdd:TIGR00956 759 IFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 89 RgaNIGIVFQSFHLIPNMT---ALENVAV---PLELAgRRDAFDVAERELRAVGL---GERLTHYPSE-LSGGEQQRVAI 158
Cdd:TIGR00956 836 R--SIGYVQQQDLHLPTSTvreSLRFSAYlrqPKSVS-KSEKMEYVEEVIKLLEMesyADAVVGVPGEgLNVEQRKRLTI 912
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489055174 159 ARALAPSPKILI-ADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPS 209
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLM-RKLADHGQAILCTIHQPS 963
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-226 |
3.45e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVkIAGETISQMSEdQAaafrganigivfqsfhLIPNMT 107
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQ-QA----------------WIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAV--PLELAGRRDAFDVAERELRAVGLGERLTHYPSE----LSGGEQQRVAIARALAPSPKILIADEPTGNLDTA 181
Cdd:PTZ00243 737 VRGNILFfdEEDAARLADAVRVSQLEADLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489055174 182 TGRQIADLLFAKqRENGLTMVLVTHDPSLAARCDREIPVRSGRIA 226
Cdd:PTZ00243 817 VGERVVEECFLG-ALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-179 |
3.72e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 24 SSVHVLKGV-------SLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIV 96
Cdd:PRK10636 5 SSLQIRRGVrvlldnaTATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 97 FQSFHLIPNMTALENVA-------VPLELAGRRDAFDVAERELRAV----GLG---ERLTHYPSELSGGEQQRVAIARAL 162
Cdd:PRK10636 85 IDGDREYRQLEAQLHDAnerndghAIATIHGKLDAIDAWTIRSRAAsllhGLGfsnEQLERPVSDFSGGWRMRLNLAQAL 164
|
170
....*....|....*..
gi 489055174 163 APSPKILIADEPTGNLD 179
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLD 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-210 |
4.27e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 20 GHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLE---HVDnGIVKIAG-----ETISQMS-----EDQAA 86
Cdd:PLN03140 887 GVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtggYIE-GDIRISGfpkkqETFARISgyceqNDIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 AFRGANIGIVFQSFHLIP-------NMTALENVAVPLELAGRRDAFdvaerelraVGLgerlthyP--SELSGGEQQRVA 157
Cdd:PLN03140 966 PQVTVRESLIYSAFLRLPkevskeeKMMFVDEVMELVELDNLKDAI---------VGL-------PgvTGLSTEQRKRLT 1029
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489055174 158 IARALAPSPKILIADEPTGNLDtATGRQIADLLFAKQRENGLTMVLVTHDPSL 210
Cdd:PLN03140 1030 IAVELVANPSIIFMDEPTSGLD-ARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-225 |
5.84e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 32 VSLHIAPGQSVGIVGPSGSGKSTLLMVLAGL-EHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHLIPNMTALE 110
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 111 NVAVP-LELAGRRDAFDvAERELRAVGLG-ERL---THYP----SELSGGEQQRVAIARALAPSPKILIADEPTGNLDTA 181
Cdd:TIGR02633 359 NITLSvLKSFCFKMRID-AAAELQIIGSAiQRLkvkTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489055174 182 TGRQIADLLFAKQREnGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-237 |
7.44e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 12 LEDVHLTLGHAASsvhvLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMS---------- 81
Cdd:PRK10982 251 LEVRNLTSLRQPS----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 82 ---EDQAAAFRGANIGIVFQSfhLIPNMTA-------LENVAVPLELAGRRDAFDVAERELRavglgerlTHYPSeLSGG 151
Cdd:PRK10982 327 lvtEERRSTGIYAYLDIGFNS--LISNIRNyknkvglLDNSRMKSDTQWVIDSMRVKTPGHR--------TQIGS-LSGG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 152 EQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDREIPVRSGRIaepvqg 231
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV------ 469
|
....*.
gi 489055174 232 AGIPET 237
Cdd:PRK10982 470 AGIVDT 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
146-203 |
7.49e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 7.49e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055174 146 SELSGGEQQRVAIARALAPSPKILIADEPTGNLDTAT----GRQIADLlfaKQRENGLTMVL 203
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylvQKTINNL---KGNENRITIII 636
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
44-215 |
8.61e-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: 51.07 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 44 IVGPSGSGKSTLL----MVLAGL--------EHVDngivKIAGETIsqmsedqaaafRGANIGIVFQS-----FHLIPNM 106
Cdd:cd03240 27 IVGQNGAGKTTIIealkYALTGElppnskggAHDP----KLIREGE-----------VRAQVKLAFENangkkYTITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENVA-VPLElagrrDAFDVAERELRAvglgerlthypseLSGGEQQ------RVAIARALAPSPKILIADEPTGNLD 179
Cdd:cd03240 92 AILENVIfCHQG-----ESNWPLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 489055174 180 TATGR-QIADLLFAKQRENGLTMVLVTHDPSLAARCD 215
Cdd:cd03240 154 EENIEeSLAEIIEERKSQKNFQLIVITHDEELVDAAD 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-231 |
1.33e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 7 GPIIELEDVhlTLGHAASSVhVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVkiagetisqmsedqaa 86
Cdd:PLN03073 506 PPIISFSDA--SFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------------- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 aFRGANIGI-VFQSFHLipnmTALENVAVPLeLAGRRDAFDVAERELRA----VGLGERLTHYPS-ELSGGEQQRVAIAR 160
Cdd:PLN03073 567 -FRSAKVRMaVFSQHHV----DGLDLSSNPL-LYMMRCFPGVPEQKLRAhlgsFGVTGNLALQPMyTLSGGQKSRVAFAK 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055174 161 ALAPSPKILIADEPTGNLD-TATGRQIADL-LFakqrENGLTMvlVTHDPSLAARCDREIPVRSGRIAEPVQG 231
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDlDAVEALIQGLvLF----QGGVLM--VSHDEHLISGSVDELWVVSEGKVTPFHG 707
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
148-225 |
2.66e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 2.66e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055174 148 LSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREnGLTMVLVTHD-PSLAARCDREIPVRSGRI 225
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSElPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-231 |
3.86e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEDQAAAfrgANIGIVFQSFHLIPN 105
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVplelaGR--RDAFDVAE----RELRAVGLGERLTHYPSE----LSGGEQQRVAIARALAPSPKILIADEPT 175
Cdd:PRK10982 88 RSVMDNMWL-----GRypTKGMFVDQdkmyRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 176 GNLdtaTGRQIADL--LFAKQRENGLTMVLVTHD-PSLAARCDREIPVRSGR-IA-EPVQG 231
Cdd:PRK10982 163 SSL---TEKEVNHLftIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQwIAtQPLAG 220
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-206 |
4.66e-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: 50.40 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLM-VLA---------------------GLEHVDNgIVKIAGETISQMSED 83
Cdd:TIGR00630 621 ENNLKNITVSIPLGLFTCITGVSGSGKSTLINdTLYpalanrlngaktvpgrytsieGLEHLDK-VIHIDQSPIGRTPRS 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 84 QAAAFRGA--NIGIVFQ---------------SFH--------------LIPNMTALENVAVPLELA-GRR--------- 122
Cdd:TIGR00630 700 NPATYTGVfdEIRELFAetpeakvrgytpgrfSFNvkggrceacqgdgvIKIEMHFLPDVYVPCEVCkGKRynretlevk 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 123 ---------------------DAFDVAERELRA---VGLGE-RLTHYPSELSGGEQQRVAIARAL---APSPKILIADEP 174
Cdd:TIGR00630 780 ykgkniadvldmtveeayeffEAVPSISRKLQTlcdVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEP 859
|
250 260 270
....*....|....*....|....*....|....
gi 489055174 175 TGNLDTAtgrQIADLLFAKQR--ENGLTMVLVTH 206
Cdd:TIGR00630 860 TTGLHFD---DIKKLLEVLQRlvDKGNTVVVIEH 890
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-220 |
6.43e-07 |
|
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: 48.79 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTL---LMVLAGLEHVDNGIVKIAGETISQMSEDQAAAFRGANIGIVFQSFHL 102
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAIAIDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 103 IPN-------MTALENVavpLELAGRRDAFDVAERELRAVGLGE-RLTHYPSELSGGEQQRVAIARALAP--SPKILIAD 172
Cdd:cd03270 88 SRNprstvgtVTEIYDY---LRLLFARVGIRERLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSglTGVLYVLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055174 173 EPTGNLDTATGRQIADLLFaKQRENGLTMVLVTHDPSLAARCDREIPV 220
Cdd:cd03270 165 EPSIGLHPRDNDRLIETLK-RLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
148-218 |
7.37e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 7.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 148 LSGGEQQRVAIARALA-----PSPKILIaDEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAARCDREI 218
Cdd:cd03227 78 LSGGEKELSALALILAlaslkPRPLYIL-DEIDRGLDPRDGQALAEAI-LEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
28-209 |
9.85e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 28 VLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGETISQMSEdQAAAFRGANIGIVFQsfhlipnMT 107
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-PYCTYIGHNLGLKLE-------MT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 108 ALENVAVPLELAGRRDAFDVAERELRavgLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIA 187
Cdd:PRK13541 87 VFENLKFWSEIYNSAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170 180
....*....|....*....|..
gi 489055174 188 DLLFAKQRENGLTMvLVTHDPS 209
Cdd:PRK13541 164 NLIVMKANSGGIVL-LSSHLES 184
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-179 |
6.33e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 33 SLHIAPGQSVGIVGPSGSGKSTLLMVLAglEHVDNGIVK----------IAGETIS-------------QMSEDQA---A 86
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGIPKncqilhveqeVVGDDTTalqcvlntdiertQLLEEEAqlvA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 87 AFRGANIGIVFQSFHlIPNMTALENVAVPLELA---GRRDAFDVAERELRAVGLGERLTHYP-------SELSGGEQQRV 156
Cdd:PLN03073 275 QQRELEFETETGKGK-GANKDGVDKDAVSQRLEeiyKRLELIDAYTAEARAASILAGLSFTPemqvkatKTFSGGWRMRI 353
|
170 180
....*....|....*....|...
gi 489055174 157 AIARALAPSPKILIADEPTGNLD 179
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLD 376
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-227 |
9.18e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGetisqmsedqAAAFRGANIGIVFQsfhlipnM 106
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------SAALIAISSGLNGQ-------L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 107 TALENVavplELAG------RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEptgnldt 180
Cdd:PRK13545 101 TGIENI----ELKGlmmgltKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE------- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 181 atGRQIADLLFAKQ--------RENGLTMVLVTHDPS-LAARCDREIPVRSGRIAE 227
Cdd:PRK13545 170 --ALSVGDQTFTKKcldkmnefKEQGKTIFFISHSLSqVKSFCTKALWLHYGQVKE 223
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
44-207 |
1.11e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 44 IVGPSGSGKSTLLM----VLAG---------LEHVDNG------------------IVKIAGETISQMSEDQAAafRGAN 92
Cdd:COG0419 28 IVGPNGAGKSTILEairyALYGkarsrsklrSDLINVGseeasvelefehggkryrIERRQGEFAEFLEAKPSE--RKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 93 IGIVFQSFHLIPNMTALENVAVPLE--LAGRRDAFDVAERELRavglgeRLTHY--PSELSGGEQQRVAIARALApspki 168
Cdd:COG0419 106 LKRLLGLEIYEELKERLKELEEALEsaLEELAELQKLKQEILA------QLSGLdpIETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 489055174 169 LIADepTGNLDTATGRQIADLLFAkqrengltMVLVTHD 207
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEE--------LAIITHV 203
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
43-224 |
1.18e-05 |
|
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: 44.95 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 43 GIVGPSGSGKSTLL--MVLAglehvdngivkIAGETI-----SQMSEDQAAAFRGANIGIVFQ----------SFHLipN 105
Cdd:cd03279 32 LICGPTGAGKSTILdaITYA-----------LYGKTPrygrqENLRSVFAPGEDTAEVSFTFQlggkkyrverSRGL--D 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 106 MTALENVAVpleLA-GRRDAFdvaerelravglgerLTHYPSELSGGEQQRVAIARALAPSPKI----------LIADEP 174
Cdd:cd03279 99 YDQFTRIVL---LPqGEFDRF---------------LARPVSTLSGGETFLASLSLALALSEVLqnrggarleaLFIDEG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489055174 175 TGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAARCDREIPVRSGR 224
Cdd:cd03279 161 FGTLDPEALEAVATAL-ELIRTENRMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-223 |
2.87e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055174 148 LSGGEQQRVAIARALAP--SPKILIADEPTGNLDTATGRQIADLLfAKQRENGLTMVLVTHDPSLAARCDREIPVRSG 223
Cdd:PRK00635 477 LSGGEQERTALAKHLGAelIGITYILDEPSIGLHPQDTHKLINVI-KKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
121-225 |
4.98e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 121 RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQREnGLT 200
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100
....*....|....*....|....*.
gi 489055174 201 MVLVTHDPSLAARCDREIPV-RSGRI 225
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTViDRGRV 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-175 |
7.48e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 27 HVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDN--GIVKIAGETISQMSEDQAAAfrgANIGIVFQ---SFH 101
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGKEVDVSTVSDAID---AGLAYVTEdrkGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 102 LIPNMTALENVAVP-LELAGRRDAFDvAERELR-AVGLGERL-THYPS------ELSGGEQQRVAIARALAPSPKILIAD 172
Cdd:NF040905 351 LNLIDDIKRNITLAnLGKVSRRGVID-ENEEIKvAEEYRKKMnIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILD 429
|
...
gi 489055174 173 EPT 175
Cdd:NF040905 430 EPT 432
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-207 |
1.08e-04 |
|
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: 41.79 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 36 IAPGQSVGIVGPSGSGKSTLLMVLAGlehvdngivkiagetisqmsedqaaafrganigivfqsfHLIPNmtalenvavp 115
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG---------------------------------------QLIPN---------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 116 lelaGRRDAFDvaerelravglGERLTHYPS--ELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAK 193
Cdd:cd03222 53 ----GDNDEWD-----------GITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....
gi 489055174 194 QRENGLTMVLVTHD 207
Cdd:cd03222 118 SEEGKKTALVVEHD 131
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-206 |
2.79e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 132 LRAVGLGerlthY-----PS-ELSGGEQQRVAIARALA--PSPKIL-IADEPTgnldtaTGRQIAD---LLFAKQR--EN 197
Cdd:COG0178 810 LQDVGLG-----YiklgqPAtTLSGGEAQRVKLASELSkrSTGKTLyILDEPT------TGLHFHDirkLLEVLHRlvDK 878
|
....*....
gi 489055174 198 GLTMVLVTH 206
Cdd:COG0178 879 GNTVVVIEH 887
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-215 |
2.86e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 140 RLTHYP-----SELSGGEQQRVAIA-RALAPSPK--ILIADEPTGNLDTATGRQIADLLFAKQREnGLTMVLVTHDPSLA 211
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAyELLAPSKKptLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV 875
|
....
gi 489055174 212 ARCD 215
Cdd:PRK00635 876 KVAD 879
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-215 |
3.84e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 145 PSELSGGEQQ------RVAIARALA-------PSPKiLIADEPTGNLDTATGRQIADLLFAKQRENGLTMVLVTHDPSLA 211
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdaPLPP-LILDEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELV 857
|
....
gi 489055174 212 ARCD 215
Cdd:PRK02224 858 GAAD 861
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
40-210 |
4.14e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.43 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 40 QSVGIVGPSGSGKSTLLMVLAGLEHVDNGivkiagetisqmsedQAAAFRGANIGIVFQSFhLIPNMTALENVAVPLELA 119
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEG---------------DFIGLRGDALPLGANSF-ILPGLTGEENARMMASLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 120 GrRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGL 199
Cdd:PRK15177 78 G-LDGDEFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQLQQKGL 156
|
170
....*....|.
gi 489055174 200 tmVLVTHDPSL 210
Cdd:PRK15177 157 --IVLTHNPRL 165
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
29-66 |
8.73e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 8.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 29 LKGVSLHIAPGQSVGIVGPSGSGKSTLLM-----VLA-----------------GLEHVD 66
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINetlykALArklngakkvpgkhkeieGLEHLD 684
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
39-96 |
1.09e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 39.60 E-value: 1.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055174 39 GQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGE---TISQMSEDQAAAFRGANIGIV 96
Cdd:PRK06002 165 GQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGErgrEVREFLEDTLADNLKKAVAVV 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-207 |
1.25e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 20 GHAASSVHVLKGVSLHIAPGQSVGIVGPSGSGKSTLLMVLAGLEHVDNGIVKIAGEtisqmsedqaaafrganIGIVFQS 99
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 100 FHLIPNMTALENVAVPLELAG--RRDAFDVAERELRAVGLGERLTHYPSELSGGEQQRVAIARALAPSPKILIADEPTGN 177
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGfkRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190
....*....|....*....|....*....|
gi 489055174 178 LDTATGRQIADLLFaKQRENGLTMVLVTHD 207
Cdd:PRK13546 174 GDQTFAQKCLDKIY-EFKEQNKTIFFVSHN 202
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
155-216 |
1.58e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055174 155 RVAIARALAPSPKILIADEPTGNLD----TATGRQIADLLFAKQRENGLTMVLVTHDPSLAARCDR 216
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDreniESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGR 1278
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
31-56 |
2.23e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 2.23e-03
10 20
....*....|....*....|....*.
gi 489055174 31 GVSLHIAPGQSVGIVGPSGSGKSTLL 56
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
148-224 |
2.51e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 148 LSGGEQQ------RVAIARALAPSPKILIADEPTGNLDTATGRQIADLLFAKQRENGL--TMVLVTHDPSLAARCD--RE 217
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDipQVIMISHHRELLSVADvaYE 881
|
....*..
gi 489055174 218 IPVRSGR 224
Cdd:PRK01156 882 VKKSSGS 888
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
14-61 |
2.52e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 2.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489055174 14 DVHLTLGHAASSVHVLKGVslhIAPGQSVGIVGPSGSGKSTLLMVLAG 61
Cdd:PRK01889 173 PVLAVSALDGEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-55 |
6.25e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.25e-03
10 20 30
....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTL 55
Cdd:TIGR00630 9 EHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
26-55 |
6.25e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 6.25e-03
10 20 30
....*....|....*....|....*....|
gi 489055174 26 VHVLKGVSLHIAPGQSVGIVGPSGSGKSTL 55
Cdd:COG0178 13 EHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
36-89 |
8.02e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 35.94 E-value: 8.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055174 36 IAPGQSVGIVGPSGSGKSTLLMVLA---GLEHV--DNGIVKIAGETISQM-SEDQAAAFR 89
Cdd:PRK00131 1 MLKGPNIVLIGFMGAGKSTIGRLLAkrlGYDFIdtDHLIEARAGKSIPEIfEEEGEAAFR 60
|
|
| |
