|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-221 |
1.19e-82 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 245.34 E-value: 1.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPL 70
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGK-----------StllnilggldrPTSGEVLIDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 71 FD-KQHRPSDLRLEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQR 149
Cdd:COG1136 73 SSlSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 150 VAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-219 |
9.33e-78 |
|
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: 232.77 E-value: 9.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFD-KQHRPSDLR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 LEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-221 |
3.07e-57 |
|
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: 181.09 E-value: 3.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllSQ-----------TSGTVLYNDAPL 70
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGK-----------STllgllagldrpTSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 71 F--DKQHRpSDLRLEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMtkQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQ 148
Cdd:COG4181 77 FalDEDAR-ARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 149 RVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
12-219 |
1.08e-56 |
|
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: 179.06 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 12 FGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFD-KQHRPSDLRlEDIGFIFQ 90
Cdd:TIGR02982 11 YGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGaSKKQLVQLR-RRIGYIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 91 SSHLVPYLKVIE--QLTLVGQeAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEP 168
Cdd:TIGR02982 90 AHNLLGFLTARQnvQMALELQ-PNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447152655 169 TASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:TIGR02982 169 TAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-221 |
4.60e-56 |
|
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: 177.54 E-value: 4.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 6 EDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFD-KQHRPSDLRLED 84
Cdd:TIGR02211 5 ENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlSSNERAKLRNKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 165 ADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-221 |
7.23e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 174.47 E-value: 7.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 6 EDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllSQ-----------TSGTVLYNDAPLfdKQ 74
Cdd:COG2884 5 ENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGK-----------STllkllygeerpTSGQVLVNGQDL--SR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 75 HRPSD---LRLeDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVA 151
Cdd:COG2884 69 LKRREipyLRR-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 152 IMRAFMNNPKIILADEPTASLDADRATKVVEMIrQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKITD 221
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELL-EEINRRGTTVLIATHDLELVDrMPKRVLELEDGRLVR 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-219 |
4.53e-52 |
|
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: 167.68 E-value: 4.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRL 82
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSH--LVPYLKVIEQL--TLVGQEAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFM 157
Cdd:cd03257 82 KEIQMVFQDPMssLNPRMTIGEQIaePLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 158 NNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEY-ADRVIELEDGKI 219
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
6.09e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 168.34 E-value: 6.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAP 69
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGK-----------StllrliaglekPTSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 70 LfdkqHRPSDlrleDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQR 149
Cdd:COG1116 75 V----TGPGP----DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 150 VAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDrrLFE--Y-ADRVI 212
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD--VDEavFlADRVV 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-219 |
1.23e-51 |
|
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: 166.17 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRlED 84
Cdd:cd03262 3 IKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELR-QK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQSSHLVPYLKVIEQLTLVGQEA-GMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKII 163
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 164 LADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRRlF--EYADRVIELEDGKI 219
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMK-DLAEEGMTMVVVTHEMG-FarEVADRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-219 |
8.41e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 164.78 E-value: 8.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllSQ-----------TSGTVLYNDAPLF 71
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGK-----------STllrcinlleepDSGTITVDGEDLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 72 DKQHRPSDLRlEDIGFIFQSSHLVPYLKVIEQLTLvGQE--AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQR 149
Cdd:COG1126 67 DSKKDINKLR-RKVGMVFQQFNLFPHLTVLENVTL-APIkvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 150 VAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRRlF--EYADRVIELEDGKI 219
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMR-DLAKEGMTMVVVTHEMG-FarEVADRVVFMDGGRI 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-212 |
1.28e-50 |
|
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: 163.80 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqHRPSDlrl 82
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 eDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03293 74 -DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDrrLFE---YADRVI 212
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD--IDEavfLADRVV 203
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
1.41e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 156.76 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAP 69
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGK-----------StllrclnglvePTSGEILVDGQD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 70 LFdkQHRPSDLRL--EDIGFIFQSSHLVPYLKVIEQLtLVGQEAGMTKQQSST---------RAIQLLKNIGLEDRLNVY 138
Cdd:COG3638 67 VT--ALRGRALRRlrRRIGMIFQQFNLVPRLSVLTNV-LAGRLGRTSTWRSLLglfppedreRALEALERVGLADKAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 139 PHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD----RRlfeYADRVIEL 214
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQvdlaRR---YADRIIGL 220
|
....*
gi 447152655 215 EDGKI 219
Cdd:COG3638 221 RDGRV 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-219 |
2.95e-47 |
|
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: 154.87 E-value: 2.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRL 82
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIrQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-220 |
4.77e-47 |
|
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: 155.35 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPsdlR 81
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 LEDIGFIFQ----SSHlvPYLKVIEQLTLVGQEAGMTKQQSstRAIQLLKNIGLEDR-LNVYPHQLSGGEKQRVAIMRAF 156
Cdd:COG1124 78 RRRVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 157 MNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEY-ADRVIELEDGKIT 220
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
8.12e-47 |
|
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: 161.22 E-value: 8.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEGlsETKVLKGINFEVEQGEFVILNGASGSGK---TTLLTILGGLLSQTSGTVLYNDAPLFDkqhRPS 78
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKstlALALMGLLPHGGRISGEVLLDGRDLLE---LSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 79 DLRLEDIGFIFQS--SHLVPyLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAF 156
Cdd:COG1123 79 ALRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 157 MNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLF-EYADRVIELEDGKI 219
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDGRI 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-219 |
5.74e-46 |
|
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: 152.34 E-value: 5.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL-FDKQHRPSDLR 81
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 lEDIGFIFQSSHLVPYLKVIEQLtLVGQEAGMTKQQS---------STRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAI 152
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENV-LSGRLGRRSTWRSlfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLF-EYADRVIELEDGKI 219
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-219 |
5.54e-45 |
|
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: 148.82 E-value: 5.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFdkqHRPSDLRl 82
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 eDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03259 73 -NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRR-LFEYADRVIELEDGKI 219
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-219 |
1.22e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFI 88
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL--SAMPPPEWR-RQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 FQSSHLVPYlKVIEQLTLVGQEAGmtKQQSSTRAIQLLKNIGLEDRLNVYP-HQLSGGEKQRVAIMRAFMNNPKIILADE 167
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 168 PTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-221 |
1.62e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 148.43 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRP-SDLR 81
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 LEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-219 |
1.60e-43 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 154.50 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGT---------VLYNDAPlfdk 73
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvaTLDADAL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 74 qhrpSDLRLEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIM 153
Cdd:PRK10535 81 ----AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 154 RAFMNNPKIILADEPTASLDADRATKVVEmIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-214 |
3.24e-43 |
|
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: 144.30 E-value: 3.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYND---APLFDKQhrPSDLR 81
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetPPLNSKK--ASKFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 LEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFEYADRVIEL 214
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEGKTI-IIVTHDPEVAKQADRVIEL 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-219 |
4.48e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 144.54 E-value: 4.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL--FDKQHRpSDL 80
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEAR-AKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 RLEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNP 160
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 161 KIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-212 |
2.27e-42 |
|
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: 145.20 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS--------------QTSGTVLYNDA 68
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGK-----------StlarailgllpppgITSGEILFDGE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 69 PLFD-KQHRPSDLRLEDIGFIFQS--SHLVPYLKVIEQLTlvgqEA-----GMTKQQSSTRAIQLLKNIGL---EDRLNV 137
Cdd:COG0444 71 DLLKlSEKELRKIRGREIQMIFQDpmTSLNPVMTVGDQIA----EPlrihgGLSKAEARERAIELLERVGLpdpERRLDR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 138 YPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD----RRLfeyADRVI 212
Cdd:COG0444 147 YPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlgvvAEI---ADRVA 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-219 |
2.27e-42 |
|
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: 143.11 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKqhRPSDLRLE- 83
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL--SGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 -DIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03258 82 rRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD----RRLfeyADRVIELEDGKI 219
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmevvKRI---CDRVAVMEKGEV 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-219 |
5.47e-42 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 142.44 E-value: 5.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRL 82
Cdd:TIGR02315 2 LEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI--TKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 --EDIGFIFQSSHLVPYLKVIEQLtLVGQEA---------GMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVA 151
Cdd:TIGR02315 77 lrRRIGMIFQHYNLIERLTVLENV-LHGRLGykptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 152 IMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGKI 219
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLaKKYADRIVGLKAGEI 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-219 |
1.08e-41 |
|
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: 140.93 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPLFDKQhrPSDLRlEDIG 86
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGK-----------StllrllngllkPTSGEVLVDGKDITKKN--LRELR-RKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQSSHlvpylkviEQL--TLVGQE-------AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFM 157
Cdd:COG1122 79 LVFQNPD--------DQLfaPTVEEDvafgpenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 158 NNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLF-EYADRVIELEDGKI 219
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTV-IIVTHDLDLVaELADRVIVLDDGRI 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
22-218 |
1.26e-41 |
|
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: 140.46 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLEDIGFIFQSSHLVPYLKVI 101
Cdd:TIGR02673 18 LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRIGVVFQDFRLLPDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 EQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVV 181
Cdd:TIGR02673 98 ENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERIL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 447152655 182 EMIrQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGK 218
Cdd:TIGR02673 178 DLL-KRLNKRGTTVIVATHDLSLVDrVAHRVIILDDGR 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-219 |
3.34e-41 |
|
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: 146.20 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGE-GLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPL 70
Cdd:COG1123 261 LEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGK-----------StlarlllgllrPTSGSILFDGKDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 71 FDKQHRPSDLRLEDIGFIFQ--SSHLVPYLKVIEQLTLVGQEAG-MTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGE 146
Cdd:COG1123 330 TKLSRRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 147 KQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIG-IMITHDRRL-FEYADRVIELEDGKI 219
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR-DLQRELGLTyLFISHDLAVvRYIADRVAVMYDGRI 483
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
5.54e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 5.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPlFDKQHRPSD- 79
Cdd:COG4161 1 MSIQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ-FDFSQKPSEk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 ----LRlEDIGFIFQSSHLVPYLKVIEQLTlvgqEA-----GMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRV 150
Cdd:COG4161 76 airlLR-QKVGMVFQQYNLWPHLTVMENLI----EApckvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 151 AIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHD----RRLfeyADRVIELEDGKI 219
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIR-ELSQTGITQVIVTHEvefaRKV---ASQVVYMEKGRI 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-218 |
5.77e-41 |
|
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: 138.75 E-value: 5.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPsdlRLEDIGFIFQ--SSHL 94
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKVGLVFQnpDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VpYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDA 174
Cdd:cd03225 89 F-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447152655 175 DRATKVVEMIRqQIKEQQMIGIMITHD-RRLFEYADRVIELEDGK 218
Cdd:cd03225 168 AGRRELLELLK-KLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-219 |
1.88e-39 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 141.75 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllSQT---------------SGTVLYND 67
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGK-----------SVTalsilrllpdpaahpSGSILFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 68 APLF---DKQHRpsDLRLEDIGFIFQ---SShLVPYLKVIEQLTlvgqEA-----GMTKQQSSTRAIQLLKNIGL---ED 133
Cdd:COG4172 76 QDLLglsERELR--RIRGNRIAMIFQepmTS-LNPLHTIGKQIA----EVlrlhrGLSGAAARARALELLERVGIpdpER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 134 RLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD----RRlfeYAD 209
Cdd:COG4172 149 RLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRR---FAD 225
|
250
....*....|
gi 447152655 210 RVIELEDGKI 219
Cdd:COG4172 226 RVAVMRQGEI 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
1.92e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.53 E-value: 1.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTV-LYNDAplFDKQHRPSD 79
Cdd:PRK11124 1 MSIQLNGINCFYGA----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGNH--FDFSKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 -----LRlEDIGFIFQSSHLVPYLKVIEQLTlvgqEA-----GMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQR 149
Cdd:PRK11124 75 kaireLR-RNVGMVFQQYNLWPHLTVQQNLI----EApcrvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 150 VAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqqikEQQMIGI---MITHD----RRLfeyADRVIELEDGKI 219
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIR----ELAETGItqvIVTHEvevaRKT---ASRVVYMENGHI 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-219 |
2.36e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.19 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDaplF 71
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGK-----------TttirmllgllrPTSGEVRVLG---E 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 72 DKQHRPSDLRlEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVA 151
Cdd:COG1131 63 DVARDPAEVR-RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 152 IMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDrrLFE---YADRVIELEDGKI 219
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTHY--LEEaerLCDRVAIIDKGRI 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-219 |
1.52e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.98 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGLSETKVLKGINFEVEQGE-F-VIlnGASGSGKttlltilggllSQ-----------TSGTVLYNDAPLf 71
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEiFgII--GYSGAGK-----------STlircinllerpTSGSVLVDGVDL- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 72 dKQHRPSDLRLE--DIGFIFQSSHL---------VPY-LKVieqltlvgqeAGMTKQQSSTRAIQLLKNIGLEDRLNVYP 139
Cdd:COG1135 70 -TALSERELRAArrKIGMIFQHFNLlssrtvaenVALpLEI----------AGVPKAEIRKRVAELLELVGLSDKADAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 140 HQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGI-MITHD----RRLfeyADRVIEL 214
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLK-DINRELGLTIvLITHEmdvvRRI---CDRVAVL 214
|
....*
gi 447152655 215 EDGKI 219
Cdd:COG1135 215 ENGRI 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-219 |
1.95e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.00 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPL 70
Cdd:COG3842 5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGK-----------TtllrmiagfetPDSGRILLDGRDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 71 FdkqHRPSDLRleDIGFIFQSSHLVPYLKVIEQltlVG---QEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEK 147
Cdd:COG3842 70 T---GLPPEKR--NVGMVFQDYALFPHLTVAEN---VAfglRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 148 QRVAIMRAFMNNPKIILADEPTASLDAdratKVVEMIRQQIKE-QQMIGI---MITHDRR-LFEYADRVIELEDGKI 219
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDA----KLREEMREELRRlQRELGItfiYVTHDQEeALALADRIAVMNDGRI 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-219 |
3.30e-38 |
|
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: 132.41 E-value: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEglseTKVLKGINFEVEQGE-FVILnGASGSGKttlltilggllS-----------QTSGTVLYNDAP 69
Cdd:COG1127 5 MIEVRNLTKSFGD----RVVLDGVSLDVPRGEiLAII-GGSGSGK-----------SvllkliigllrPDSGEILVDGQD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 70 LFD-KQHRPSDLRLEdIGFIFQSSHLVPYLKVIE--QLTLVgQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGE 146
Cdd:COG1127 69 ITGlSEKELYELRRR-IGMLFQGGALFDSLTVFEnvAFPLR-EHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 147 KQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-219 |
4.35e-38 |
|
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: 132.04 E-value: 4.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRl 82
Cdd:cd03295 1 IEFENVTKRYGGG---KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI--REQDPVELR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDR--LNVYPHQLSGGEKQRVAIMRAFMNNP 160
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 161 KIILADEPTASLDA-DRATKVVEMIRQQIKEQQMIgIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:cd03295 155 PLLLMDEPFGALDPiTRDQLQEEFKRLQQELGKTI-VFVTHDiDEAFRLADRIAIMKNGEI 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-219 |
4.58e-38 |
|
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: 131.86 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFD---KQHRPSDLR 81
Cdd:cd03261 3 LRGLTKSFGG----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 ledIGFIFQSSHLVPYLKVIEQLTL-VGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNP 160
Cdd:cd03261 79 ---MGMLFQSGALFDSLTVFENVAFpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 161 KIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-217 |
1.23e-37 |
|
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: 130.63 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNF---GEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllSQ-----------TSGTVLYNDa 68
Cdd:COG4778 5 LEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGK-----------STllkciygnylpDSGSILVRH- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 69 plfdkQHRPSD-----------LRLEDIGFIFQsshlvpYLKVIEQ---LTLVGQ---EAGMTKQQSSTRAIQLLKNIGL 131
Cdd:COG4778 73 -----DGGWVDlaqaspreilaLRRRTIGYVSQ------FLRVIPRvsaLDVVAEpllERGVDREEARARARELLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 132 EDRL-NVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQ--QMIGimITHDRRLFE-Y 207
Cdd:COG4778 142 PERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIE-EAKARgtAIIG--IFHDEEVREaV 218
|
250
....*....|
gi 447152655 208 ADRVIELEDG 217
Cdd:COG4778 219 ADRVVDVTPF 228
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-219 |
1.29e-37 |
|
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: 134.01 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRl 82
Cdd:TIGR03265 5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR---DITRLPPQKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 eDIGFIFQSSHLVPYLKVIEQLT--LVGQeaGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNP 160
Cdd:TIGR03265 77 -DYGIVFQSYALFPNLTVADNIAygLKNR--GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 161 KIILADEPTASLDAdratKVVEMIRQQIKE-QQMIG---IMITHDR-RLFEYADRVIELEDGKI 219
Cdd:TIGR03265 154 GLLLLDEPLSALDA----RVREHLRTEIRQlQRRLGvttIMVTHDQeEALSMADRIVVMNHGVI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-220 |
1.75e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 130.60 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 7 DIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLEdIG 86
Cdd:PRK09493 6 NVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQE-AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQSSHLVPYLKVIEQLTLvG--QEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMF-GplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 165 ADEPTASLDADRATKVVEMIrQQIKEQQMIGIMITHD----RRLfeyADRVIELEDGKIT 220
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVM-QDLAEEGMTMVIVTHEigfaEKV---ASRLIFIDKGRIA 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-218 |
6.33e-37 |
|
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: 127.30 E-value: 6.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRl 82
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVgqeagmtkqqsstraiqllknigledrlnvyphqLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGK 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-219 |
9.44e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 9.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAP 69
Cdd:COG1118 1 MSIEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGK-----------TtllriiagletPDSGRIVLNGRD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 70 LFDKQHrPSDLRledIGFIFQSSHLVPYLKVIEQLtlvgqEAGMTKQQSSTRAI-----QLLKNIGLEDRLNVYPHQLSG 144
Cdd:COG1118 66 LFTNLP-PRERR---VGFVFQHYALFPHMTVAENI-----AFGLRVRPPSKAEIrarveELLELVQLEGLADRYPSQLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 145 GEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGKI 219
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEaLELADRVVVMNQGRI 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-218 |
1.29e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 127.21 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllsqTS-------------GTVLYND 67
Cdd:COG4133 1 MMLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGK-------------TTllrilagllppsaGEVLWNG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 68 APLfdkqHRPSDLRLEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMtkQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEK 147
Cdd:COG4133 64 EPI----RDAREDYRRRLAYLGHADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 148 QRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFEyADRVIELEDGK 218
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQPLELA-AARVLDLGDFK 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-219 |
1.03e-35 |
|
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: 126.13 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaplFDKQHRPSDLRl 82
Cdd:COG4555 2 IEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG---EDVRKEPREAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTV-LFSSHIMQEVEaLCDRVVILHKGKV 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-216 |
1.07e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.90 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 8 IVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLS---QTSGTVLYNDAPLfdkQHRPSDLRleD 84
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRL---TALPAEQR--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQSSHLVPYLKVIEQLtLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENL-AFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447152655 165 ADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELED 216
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-219 |
1.48e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 125.95 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrpsdlrl 82
Cdd:PRK11247 13 LLLNAVSKRYGE----RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLvgqeaGMtKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:PRK11247 81 EDTRLMFQDARLLPWKKVIDNVGL-----GL-KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-219 |
3.05e-35 |
|
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: 124.66 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLsetkVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDLRl 82
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 eDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03300 73 -PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 163 ILADEPTASLDAdratKVVEMIRQQIKE-QQMIGI---MITHDRrlfEYA----DRVIELEDGKI 219
Cdd:cd03300 152 LLLDEPLGALDL----KLRKDMQLELKRlQKELGItfvFVTHDQ---EEAltmsDRIAVMNKGKI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
1.32e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 120.45 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRledIGFIFQSSHLVPYLKVI 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE---IGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 102 EQLTLVGQEAGMTKQQSSTRAIQLLKNIGLED----RLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTA 170
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-221 |
2.34e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFgeglSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYND------APLFDKQH 75
Cdd:PRK11264 3 AIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtaRSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 76 RPSDLRlEDIGFIFQSSHLVPYLKVIEQL----TLVGQEAgmtKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVA 151
Cdd:PRK11264 79 LIRQLR-QHVGFVFQNFNLFPHRTVLENIiegpVIVKGEP---KEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 152 IMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLF-EYADRVIELEDGKITD 221
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTM-VIVTHEMSFArDVADRAIFMDQGRIVE 224
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-219 |
4.40e-34 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 121.83 E-value: 4.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYN--DAPLFDKQHRpsdl 80
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNgqDATRVHARDR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 rleDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNP 160
Cdd:TIGR00968 73 ---KIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 161 KIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDR-RLFEYADRVIELEDGKI 219
Cdd:TIGR00968 150 QVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQeEAMEVADRIVVMSNGKI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
5.84e-33 |
|
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: 124.49 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVknFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPL 70
Cdd:COG4987 333 SLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGK-----------StllalllrfldPQSGSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 71 fdKQHRPSDLRlEDIGFIFQSSHLVpYLKVIEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLEDRLNVYPH---------- 140
Cdd:COG4987 400 --RDLDEDDLR-RRIAVVPQRPHLF-DTTLRENLRLARPDA------TDEELWAALERVGLGDWLAALPDgldtwlgegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 141 -QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:COG4987 470 rRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERMDRILVLEDGRI 547
|
.
gi 447152655 220 T 220
Cdd:COG4987 548 V 548
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-219 |
6.72e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 116.73 E-value: 6.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDkqhRPSDLRl 82
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK---EPEEVK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLtlvgqeagmtkqqsstraiqllknigledrlnvyphQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLR-ELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-201 |
9.57e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 118.81 E-value: 9.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqHRPSDL 80
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 RlediGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNP 160
Cdd:COG4525 78 R----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447152655 161 KIILADEPTASLDAdratkvveMIRQQIKE---------QQMIgIMITHD 201
Cdd:COG4525 154 RFLLMDEPFGALDA--------LTREQMQEllldvwqrtGKGV-FLITHS 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-218 |
1.47e-32 |
|
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: 115.56 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIvkNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRl 82
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVpylkvieqltlvgqeagmtkqqSSTraiqLLKNIgledrlnvyphqLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03228 76 KNIAYVPQDPFLF----------------------SGT----IRENI------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGK 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-219 |
1.71e-32 |
|
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: 117.44 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRl 82
Cdd:cd03299 1 LKVENLSKDWKE-----FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK---DITNLPPEKR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 eDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03299 72 -DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDrrlFE----YADRVIELEDGKI 219
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD---FEeawaLADKVAIMLNGKL 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-219 |
5.13e-32 |
|
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: 115.81 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrPSDlrl 82
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP--PKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 163 ILADEPTASLDAdratKVVEMIRQQIKE-QQMIG---IMITHDR-RLFEYADRVIELEDGKI 219
Cdd:cd03301 152 FLMDEPLSNLDA----KLRVQMRAELKRlQQRLGtttIYVTHDQvEAMTMADRIAVMNDGQI 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-218 |
5.82e-32 |
|
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: 113.88 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGlsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKqhrPSDLRLED 84
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL---PLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQsshlvpylkvieqltlvgqeagmtkqqsstraiqllknigledrlnvyphqLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:cd00267 75 IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 165 ADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFE-YADRVIELEDGK 218
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTV-IIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-219 |
5.93e-32 |
|
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: 115.74 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGlsetKVLKGINFEVEQGEFVILNGASGSGK-----TTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSD 79
Cdd:cd03260 3 LRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKstllrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 LRLEdIGFIFQSSHLVPyLKVIEQLTLVGQEAGM-TKQQSSTRAIQLLKNIGL----EDRLNvyPHQLSGGEKQRVAIMR 154
Cdd:cd03260 79 LRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 155 AFMNNPKIILADEPTASLDAdRATKVVEMIRQQIKEQQMIgIMITHD----RRLfeyADRVIELEDGKI 219
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDP-ISTAKIEELIAELKKEYTI-VIVTHNmqqaARV---ADRTAFLLNGRL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-219 |
6.93e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.64 E-value: 6.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MA-LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDA 68
Cdd:COG3839 1 MAsLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGK-----------StllrmiagledPTSGEILIGGR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 69 PLFDKqhRPSDlRleDIGFIFQSSHLVPYLKVIEQ----LTLvgqeAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSG 144
Cdd:COG3839 66 DVTDL--PPKD-R--NIAMVFQSYALYPHMTVYENiafpLKL----RKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 145 GEKQRVAIMRAFMNNPKIILADEPTASLDAD-RatkvVEMiRQQIKE-QQMIGI-MI--THDR----RLfeyADRVIELE 215
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKlR----VEM-RAEIKRlHRRLGTtTIyvTHDQveamTL---ADRIAVMN 208
|
....
gi 447152655 216 DGKI 219
Cdd:COG3839 209 DGRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-219 |
1.14e-31 |
|
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: 116.20 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAP---LFDKQHRpsDLRLEDIGFIFQSSHLVPYLKVI 101
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaaMSRKELR--ELRRKKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 EQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDA-DRATKV 180
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlIRREMQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447152655 181 VEMIRQQIKEQQMIgIMITHDR----RLfeyADRVIELEDGKI 219
Cdd:cd03294 201 DELLRLQAELQKTI-VFITHDLdealRL---GDRIAIMKDGRL 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-219 |
1.24e-31 |
|
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: 114.99 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQSSHLVp 96
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI--RQLDPADLR-RNIGYVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKVIEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLEDRLNVYPH-----------QLSGGEKQRVAIMRAFMNNPKIILA 165
Cdd:cd03245 91 YGTLRDNITLGAPLA------DDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447152655 166 DEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-219 |
1.50e-31 |
|
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: 121.09 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIvkNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPL 70
Cdd:COG2274 473 DIELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGK-----------StllklllglyePTSGRILIDGIDL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 71 fdKQHRPSDLRlEDIGFIFQSSHLvpyLK--VIEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLEDRLNVYPH-------- 140
Cdd:COG2274 540 --RQIDPASLR-RQIGVVLQDVFL---FSgtIRENITLGDPDA------TDEEIIEAARLAGLHDFIEALPMgydtvvge 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 141 ---QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDG 217
Cdd:COG2274 608 ggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIRLADRIIVLDKG 685
|
..
gi 447152655 218 KI 219
Cdd:COG2274 686 RI 687
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-219 |
1.92e-31 |
|
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: 114.74 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPsdL 80
Cdd:cd03296 1 MSIEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDVP--V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 RLEDIGFIFQSSHLVPYLKVIEQ----LTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAF 156
Cdd:cd03296 72 QERNVGFVFQHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 157 MNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDR-RLFEYADRVIELEDGKI 219
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQeEALEVADRVVVMNKGRI 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-219 |
1.23e-30 |
|
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: 113.21 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPLfdKQHRP 77
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGK-----------StllralagllkPSSGEVLLDGRDL--ASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 SDL-RLedIGFIFQSSHLVPYLKVIEqltLV--------GQEAGMTKQ--QSSTRAIQLLkniGLEDRLNVYPHQLSGGE 146
Cdd:COG1120 71 RELaRR--IAYVPQEPPAPFGLTVRE---LValgryphlGLFGRPSAEdrEAVEEALERT---GLEHLADRPVDELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 147 KQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGKI 219
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDGRI 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-221 |
1.95e-30 |
|
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: 117.55 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQSSHLvPY 97
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL--SDLDPASWR-RQIAWVPQNPYL-FA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLEDRLNVYPH-----------QLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:COG4988 425 GTIRENLRLGRPDA------SDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 167 EPTASLDADRATKVVEMIRqQIKEQQMIgIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:COG4988 499 EPTAHLDAETEAEILQALR-RLAKGRTV-ILITHRLALLAQADRILVLDDGRIVE 551
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-213 |
2.14e-30 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 114.44 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllSQT--------------SGTVLYNDA 68
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGK-----------SQTafalmgllaangriGGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 69 PLFD-KQHRPSDLRLEDIGFIFQS--SHLVPYLKVIEQLTLVGQ-EAGMTKQQSSTRAIQLLKNIGLED---RLNVYPHQ 141
Cdd:PRK09473 82 EILNlPEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMlHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD---------RRLFEYADRVI 212
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlgvvagicdKVLVMYAGRTM 241
|
.
gi 447152655 213 E 213
Cdd:PRK09473 242 E 242
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-220 |
2.91e-30 |
|
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: 110.22 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDLRLEDIGFi 88
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL---ASLSPKELARKIAY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 fqsshlVPylkvieqltlvgqeagmtkqqsstraiQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEP 168
Cdd:cd03214 78 ------VP---------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 169 TASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGKIT 220
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLaARYADRVILLKDGRIV 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-219 |
4.31e-30 |
|
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: 110.85 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEqGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFD---KQHRPSDLRleDIGFIFQSSHLVPYLKVI 101
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkKINLPPQQR--KIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 EQLTLvgqeaGMTKQQSSTRAI---QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRAT 178
Cdd:cd03297 94 ENLAF-----GLKRKRNREDRIsvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447152655 179 KVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRL 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-219 |
6.46e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 113.64 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqhrpSDL 80
Cdd:PRK10851 1 MSIEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-------SRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 RLED--IGFIFQSSHLVPYLKVIEQLTLvgqeaGMT----KQQSSTRAI-----QLLKNIGLEDRLNVYPHQLSGGEKQR 149
Cdd:PRK10851 70 HARDrkVGFVFQHYALFRHMTVFDNIAF-----GLTvlprRERPNAAAIkakvtQLLEMVQLAHLADRYPAQLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 150 VAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRR-LFEYADRVIELEDGKI 219
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEeAMEVADRVVVMSQGNI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-220 |
2.61e-29 |
|
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: 108.50 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrpsdlRLED 84
Cdd:cd03226 2 IENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE------RRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQSSHLVPYLK-VIEQLTLVGQEAGMTKQQSStraiQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKII 163
Cdd:cd03226 73 IGYVMQDVDYQLFTDsVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 164 LADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRR-LFEYADRVIELEDGKIT 220
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-219 |
3.46e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.43 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 6 EDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRLE-- 83
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL--TALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 DIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKII 163
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 164 LADEPTASLDADRATKVVEMIRqQIKEQQMIGI-MITHD----RRLfeyADRVIELEDGKI 219
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLK-DINRELGLTIvLITHEmdvvKRI---CDRVAVIDAGRL 219
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
21-219 |
3.39e-28 |
|
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: 108.93 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILG--GLLSQTSGTVLYNDAplfDKQHRPSDLRleDIGFIFQSSHLVPYL 98
Cdd:TIGR03258 20 VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAgfVKAAGLTGRIAIADR---DLTHAPPHKR--GLALLFQNYALFPHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 99 KVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAD-RA 177
Cdd:TIGR03258 95 KVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANiRA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447152655 178 TKVVEMIRQQIKEQQMIGIMITHDR-RLFEYADRVIELEDGKI 219
Cdd:TIGR03258 175 NMREEIAALHEELPELTILCVTHDQdDALTLADKAGIMKDGRL 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-219 |
3.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.44 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEGLS-ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSD 79
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 LRlEDIGFIFQSSHLVPYLKVIEQLTLVG-QEAGMTKQQSSTRAIQLLKNIGL--EDRLNVYPHQLSGGEKQRVAIMRAF 156
Cdd:PRK13637 81 IR-KKVGLVFQYPEYQLFEETIEKDIAFGpINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 157 MNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRR-LFEYADRVIELEDGKI 219
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKC 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-219 |
5.67e-28 |
|
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: 105.60 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGeGLsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRL 82
Cdd:cd03219 1 LEVRGLTKRFG-GL---VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI--TGLPPHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQ--------EAGMTKQQSSTR--AIQLLKNIGLEDRLNVYPHQLSGGEKQRVAI 152
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAAQartgsgllLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIR-ELRERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
1.73e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 106.36 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALV-VEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQ----TSGTVLYNDAPLF---D 72
Cdd:PRK11022 1 MALLnVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrvMAEKLEFNGQDLQrisE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 73 KQHRpsDLRLEDIGFIFQS-------SHLVPYlKVIEQLTlVGQeaGMTKQQSSTRAIQLLKNIGLED---RLNVYPHQL 142
Cdd:PRK11022 81 KERR--NLVGAEVAMIFQDpmtslnpCYTVGF-QIMEAIK-VHQ--GGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 143 SGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLF-EYADRVIELEDGKITD 221
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVE 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-214 |
2.15e-27 |
|
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: 108.53 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDLRLEDIGFIFQSSHLVPY 97
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL---ADADADSWRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 lKVIEQLTLVGQEAGMTK-QQSSTRA--IQLLKNI--GLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:TIGR02857 411 -TIAENIRLARPDASDAEiREALERAglDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447152655 173 DADRATKVVEMIRQQIKEQqmIGIMITHDRRLFEYADRVIEL 214
Cdd:TIGR02857 490 DAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-220 |
2.31e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.78 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIvkNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrpsDLRL 82
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE----KALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVpylkvieqltlvgqeagmtkqqsstrAIQLLKNIGLedrlnvyphQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03247 75 SLISVLNQRPYLF--------------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKIT 220
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHMDKILFLENGKII 175
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-217 |
3.00e-27 |
|
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: 103.70 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqHRPSDLRLedigFIFQSSHLVPYLKVI 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRM----VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 EQLTLVGQEAGMTKQQSSTRAI--QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATK 179
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447152655 180 VVEMIRQQIKEQQMIGIMITH--DRRLFeYADRVIELEDG 217
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHdvDEALL-LSDRVVMLTNG 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-219 |
7.17e-27 |
|
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: 102.62 E-value: 7.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRL 82
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ---DITKLPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 ED-IGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:cd03218 74 RLgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 162 IILADEPTASLDAdratKVVEMIRQQIKE--QQMIGIMIT-HD-RRLFEYADRVIELEDGKI 219
Cdd:cd03218 154 FLLLDEPFAGVDP----IAVQDIQKIIKIlkDRGIGVLITdHNvRETLSITDRAYIIYEGKV 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-220 |
8.19e-27 |
|
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: 105.18 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEQGEFVILNGASGSGKttlltilggllsqTS-------------GTVLYNDAPLFD---KQHRPSDLRleDIGFI 88
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGK-------------TTllraiaglerpdsGRIRLGGEVLQDsarGIFLPPHRR--RIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 FQSSHLVPYLKVIEQLtlvgqEAGM--TKQQSST----RAIQLLkniGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:COG4148 83 FQEARLFPHLSVRGNL-----LYGRkrAPRAERRisfdEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD----RRLfeyADRVIELEDGKIT 220
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSldevARL---ADHVVLLEQGRVV 213
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-219 |
9.43e-27 |
|
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: 102.45 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 24 GINFEVEQGEFVILNGASGSGKTTLLTILG----GLLSQTSGTVLYNDAPLfdkqhRPSDLRLEDIGFIFQS--SHLVPY 97
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILgllpPGLTQTSGEILLDGRPL-----LPLSIRGRHIATIMQNprTAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDR---LNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDA 174
Cdd:TIGR02770 79 FTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447152655 175 DRATKVVEMIRQQIKEQQMIGIMITHDRRLFEY-ADRVIELEDGKI 219
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFGTGILLITHDLGVVARiADEVAVMDDGRI 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-219 |
1.13e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 102.89 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPsDLRlEDIGFIFQS--SHL 94
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLW-EIR-KKVGMVFQNpdNQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VPylkvieqlTLV------GQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADE 167
Cdd:TIGR04520 91 VG--------ATVeddvafGLEnLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447152655 168 PTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:TIGR04520 163 ATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-219 |
1.47e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.86 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGL-SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLR 81
Cdd:COG1101 2 LELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 LEDIGFIFQ--SSHLVPYLKVIEQLTLV---GQEAGMTKQQSSTRA---IQLLK--NIGLEDRLNVYPHQLSGGEKQRVA 151
Cdd:COG1101 79 AKYIGRVFQdpMMGTAPSMTIEENLALAyrrGKRRGLRRGLTKKRRelfRELLAtlGLGLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 152 IMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNmEQALDYGNRLIMMHEGRI 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-220 |
1.47e-26 |
|
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: 104.42 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHR---PSDLRleDIGFIFQSSHLVPYLKVI 101
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflPPEKR--RIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 EQLtlvgqEAGMTKQQSSTRAI---QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRAT 178
Cdd:TIGR02142 94 GNL-----RYGMKRARPSERRIsfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447152655 179 KVVEMIRQQIKEQQMIGIMITHD----RRLfeyADRVIELEDGKIT 220
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSlqevLRL---ADRVVVLEDGRVA 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-219 |
1.68e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.76 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDLRLedIGFIFQSSHLVPYLKVIEQL 104
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPPAERP--VSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 105 TLvGQEAGM--TKQQSStRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLD-ADRAtkvv 181
Cdd:COG3840 93 GL-GLRPGLklTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpALRQ---- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447152655 182 EM---IRQQIKEQQMIGIMITHD----RRLfeyADRVIELEDGKI 219
Cdd:COG3840 167 EMldlVDELCRERGLTVLMVTHDpedaARI---ADRVLLVADGRI 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-219 |
1.69e-26 |
|
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: 106.31 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 12 FGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS----------QTSGTVLYNDAPLFD---KQHRPs 78
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGK-----------StlglallrliPSEGEIRFDGQDLDGlsrRALRP- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 79 dLRlEDIGFIFQ---SShLVPYLKVIEQLT--LVGQEAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAI 152
Cdd:COG4172 360 -LR-RRMQVVFQdpfGS-LSPRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAI 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEY-ADRVIELEDGKI 219
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKV 504
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.87e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.24 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEGLS-ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTV--LYNDA--------- 68
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 69 -----------PLFDKQHRPSDLRlEDIGFIFQSSHLVPYLKVIEQLTLVGQEA-GMTKQQSSTRAIQLLKNIGL-EDRL 135
Cdd:PRK13651 81 ekvleklviqkTRFKKIKKIKEIR-RRVGVVFQFAEYQLFEQTIEKDIIFGPVSmGVSKEEAKKRAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 136 NVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHD-RRLFEYADRVIEL 214
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTI-ILVTHDlDNVLEWTKRTIFF 238
|
....*
gi 447152655 215 EDGKI 219
Cdd:PRK13651 239 KDGKI 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-219 |
2.05e-26 |
|
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: 99.98 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRl 82
Cdd:cd03246 1 LEVENVSFRYPGA--EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI--SQWDPNELG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSshlvpylkvieqltlvgqeagmtkqqsstraIQLLK-----NIgledrlnvyphqLSGGEKQRVAIMRAFM 157
Cdd:cd03246 76 DHVGYLPQD-------------------------------DELFSgsiaeNI------------LSGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 158 NNPKIILADEPTASLDADRATKVVEMIrQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
2.58e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL-FDKQhrpSDLR 81
Cdd:PRK13639 2 LETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkYDKK---SLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 L-EDIGFIFQSSHLVPYLKVIEQLTLVGQ-EAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNN 159
Cdd:PRK13639 76 VrKTVGIVFQNPDDQLFAPTVEEDVAFGPlNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 160 PKIILADEPTASLDADRATKVVEMIrQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLL-YDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-214 |
2.78e-26 |
|
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: 100.69 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRpsdlrledIGFI 88
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR--------IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 FQSSHLVPYLKV-IEQLTLVG--QEAGMTKQQSST---RAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03235 74 PQRRSIDRDFPIsVRDVVLMGlyGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRR-LFEYADRVIEL 214
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTHDLGlVLEYFDRVLLL 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-219 |
4.31e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 7 DIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRleDIG 86
Cdd:PRK09452 19 GISKSFDG----KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ---DITHVPAENR--HVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 167 EPTASLDAdratKVVEMIRQQIKE-QQMIGI---MITHDR-RLFEYADRVIELEDGKI 219
Cdd:PRK09452 170 ESLSALDY----KLRKQMQNELKAlQRKLGItfvFVTHDQeEALTMSDRIVVMRDGRI 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
5.88e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 100.55 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAP 69
Cdd:COG1121 5 PAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGK-----------StllkailgllpPTSGTVRLFGKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 70 LFDKQHRpsdlrledIGFIFQSSHL---VPyLKVIE--QLTLVGQeAGMTKQQSST---RAIQLLKNIGLEDRLNVYPHQ 141
Cdd:COG1121 70 PRRARRR--------IGYVPQRAEVdwdFP-ITVRDvvLMGRYGR-RGLFRRPSRAdreAVDEALERVGLEDLADRPIGE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREGKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-219 |
7.04e-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: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL-FDKQHRpsdlr 81
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdIAARNR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 ledIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:cd03269 72 ---IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 162 IILADEPTASLDADRatkvVEMIRQQIKEQQMIG---IMITHDRRLFE-YADRVIELEDGKI 219
Cdd:cd03269 149 LLILDEPFSGLDPVN----VELLKDVIRELARAGktvILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-219 |
7.66e-26 |
|
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: 100.04 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKT---TLLTILGGLLSQTSGTVLYNDAPlfdkqhRPSDLRLEDIGFIFQSSHLVP 96
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTtllDAISGRVEGGGTTSGQILFNGQP------RKPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKVIEQLTLVGQEAGMTKQQSSTR----AIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447152655 173 DADRATKVVEMIRQQIKEQQMIgIMITHDRR--LFEYADRVIELEDGKI 219
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIV-ILTIHQPRsdLFRLFDRILLLSSGEI 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-219 |
7.95e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.94 E-value: 7.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGeGlseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAP 69
Cdd:COG1129 3 PLLEMRGISKSFG-G---VKALDGVSLELRPGEVHALLGENGAGK-----------StlmkilsgvyqPDSGEILLDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 70 LfdKQHRPSDLRLEDIGFIFQSSHLVPYLKVIEQLTLvGQE---------AGMTKqqsstRAIQLLKNIGLEDRLNVYPH 140
Cdd:COG1129 68 V--RFRSPRDAQAAGIAIIHQELNLVPNLSVAENIFL-GREprrgglidwRAMRR-----RARELLARLGLDIDPDTPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 141 QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHdrRL---FEYADRVIELEDG 217
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIR-RLKAQGVAIIYISH--RLdevFEIADRVTVLRDG 216
|
..
gi 447152655 218 KI 219
Cdd:COG1129 217 RL 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-219 |
1.28e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.11 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRl 82
Cdd:PRK11432 7 VVLKNITKRFGS----NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQQR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 eDIGFIFQSSHLVPYLKVIEQ----LTLVGQEAGMTKQQSStRAIQLLKNIGLEDRlnvYPHQLSGGEKQRVAIMRAFMN 158
Cdd:PRK11432 79 -DICMVFQSYALFPHMSLGENvgygLKMLGVPKEERKQRVK-EALELVDLAGFEDR---YVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 159 NPKIILADEPTASLDAD--RAtkvvemIRQQIKE-QQMIGIM---ITHDR-RLFEYADRVIELEDGKI 219
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANlrRS------MREKIRElQQQFNITslyVTHDQsEAFAVSDTVIVMNKGKI 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-220 |
2.46e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 96.73 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRL 82
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV--SFASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIfqsshlvpylkvieqltlvgqeagmtkqqsstraiqllknigledrlnvypHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03216 75 AGIAMV---------------------------------------------------YQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 163 ILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHdrRL---FEYADRVIELEDGKIT 220
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIR-RLRAQGVAVIFISH--RLdevFEIADRVTVLRDGRVV 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-220 |
4.29e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.02 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLEDIGFIFQSSHLVPYLK 99
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 100 VIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAdratK 179
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD----A 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447152655 180 VVEMIRQQIKEQQMIGI---MITHDRRLFEYAD-RVIELEDGKIT 220
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVtvlMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-219 |
7.01e-25 |
|
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: 101.42 E-value: 7.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLS--QTSGTVLYN----------DAPLFD 72
Cdd:TIGR03269 3 VKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyvERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 73 KQHRP---SDLRLEDIGFIFQSSHLVPYLK------------------VIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGL 131
Cdd:TIGR03269 79 GEPCPvcgGTLEPEEVDFWNLSDKLRRRIRkriaimlqrtfalygddtVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 132 EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFE-YADR 210
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDK 238
|
....*....
gi 447152655 211 VIELEDGKI 219
Cdd:TIGR03269 239 AIWLENGEI 247
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-219 |
2.43e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.56 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALV-VEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrPSD 79
Cdd:PRK11000 1 MASVtLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP--PAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 lrlEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNN 159
Cdd:PRK11000 75 ---RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 160 PKIILADEPTASLDAdrATKvVEMiRQQI-KEQQMIG---IMITHDR-RLFEYADRVIELEDGKI 219
Cdd:PRK11000 152 PSVFLLDEPLSNLDA--ALR-VQM-RIEIsRLHKRLGrtmIYVTHDQvEAMTLADKIVVLDAGRV 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-220 |
2.58e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 100.24 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllSQ-----------TSGTVLYNDAPLfdKQHRPSDLRlEDIG 86
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGK-----------STlvnlllrfydpTSGRILIDGVDI--RDLTLESLR-RQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQSSHLVpYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNI-GLEDRLN--VYP--HQLSGGEKQRVAIMRAFMNNPK 161
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIeALPDGYDtvVGErgVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 162 IILADEPTASLDAdratkVVE-MIRQQIKE--QQMIGIMITHdrRL--FEYADRVIELEDGKIT 220
Cdd:COG1132 497 ILILDEATSALDT-----ETEaLIQEALERlmKGRTTIVIAH--RLstIRNADRILVLDDGRIV 553
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-212 |
2.61e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.88 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNF--GEGL--SETKVLK---GINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKqh 75
Cdd:COG4608 8 LEVRDLKKHFpvRGGLfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 76 RPSDLRL--EDIGFIFQ---SShLVPYLKVIEQLTLVGQEAGM-TKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQ 148
Cdd:COG4608 86 SGRELRPlrRRMQMVFQdpyAS-LNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 149 RVAIMRAFMNNPKIILADEPTASLDADratkvvemIRQQI----KE-QQMIG---IMITHDRRLFEY-ADRVI 212
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVS--------IQAQVlnllEDlQDELGltyLFISHDLSVVRHiSDRVA 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-219 |
2.97e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 96.44 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNF--GEGL---SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLF--DKQH 75
Cdd:COG4167 5 LEVRNLSKTFkyRTGLfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 76 RPSDLRLedigfIFQ--SSHLVPYLKVIEQLtlvgqEA------GMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGE 146
Cdd:COG4167 85 RCKHIRM-----IFQdpNTSLNPRLNIGQIL-----EEplrlntDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 147 KQRVAIMRAFMNNPKIILADEPTASLDADratkvvemIRQQI-----KEQQMIG---IMITHDRRLFEY-ADRVIELEDG 217
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMS--------VRSQIinlmlELQEKLGisyIYVSQHLGIVKHiSDKVLVMHQG 226
|
..
gi 447152655 218 KI 219
Cdd:COG4167 227 EV 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-221 |
3.64e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.19 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRL 82
Cdd:PRK10619 6 LNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 ED----------IGFIFQSSHLVPYLKVIEQLTLVG-QEAGMTKQQSSTRAIQLLKNIGLEDRLNV-YPHQLSGGEKQRV 150
Cdd:PRK10619 82 ADknqlrllrtrLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 151 AIMRAFMNNPKIILADEPTASLDADRATKVVEmIRQQIKEQQMIGIMITHDRRLFEY-ADRVIELEDGKITD 221
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-219 |
6.63e-24 |
|
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: 96.79 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 37 LNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRleDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQ 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE---DVTNVPPHLR--HINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 117 QSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDadraTKVVEMIRQQIKEQQ---- 192
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD----KKLRDQMQLELKTIQeqlg 151
|
170 180
....*....|....*....|....*...
gi 447152655 193 MIGIMITHDRR-LFEYADRVIELEDGKI 219
Cdd:TIGR01187 152 ITFVFVTHDQEeAMTMSDRIAIMRKGKI 179
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-219 |
7.05e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 94.49 E-value: 7.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaplFDKQHRPSDLRl 82
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEY-ADRVIELEDGKI 219
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-201 |
7.66e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDkqhrPSDLRlediGFIFQSSHLVPYLKV 100
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG----PGAER----GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 101 IEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKV 180
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|.
gi 447152655 181 VEMIRQQIKEQQMIGIMITHD 201
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHD 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-214 |
1.54e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.01 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 10 KNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIF 89
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI--STLKPEIYR-QQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 90 QSSHL---VPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIgLEDRLNvyphQLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:PRK10247 88 QTPTLfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTI-LTKNIA----ELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447152655 167 EPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIEL 214
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-221 |
1.65e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.08 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEglSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrPSDLRlED 84
Cdd:PRK13635 8 VEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET--VWDVR-RQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQS--SHLVPylKVIEQLTLVGQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK13635 83 VGMVFQNpdNQFVG--ATVQDDVAFGLEnIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 162 IILADEPTASLDADRATKVVEMIRqQIKEQQMIG-IMITHDRRLFEYADRVIELEDGKITD 221
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVR-QLKEQKGITvLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-219 |
2.88e-23 |
|
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: 92.88 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDLRL 82
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 ED-IGFIFQSSHLVPYLKVIEQLTLvgqeAGMTKQQSSTRAI-----QLLKNigLEDRLNVYPHQLSGGEKQRVAIMRAF 156
Cdd:cd03224 74 RAgIGYVPEGRRIFPELTVEENLLL----GAYARRRAKRKARlervyELFPR--LKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 157 MNNPKIILADEPTASLdadrATKVVEMIR---QQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:cd03224 148 MSRPKLLLLDEPSEGL----APKIVEEIFeaiRELRDEGVTILLVEQNaRFALEIADRAYVLERGRV 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-220 |
4.52e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 96.36 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVknFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPLF 71
Cdd:COG4618 331 LSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGK-----------StlarllvgvwpPTAGSVRLDGADLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 72 dkQHRPSDLRlEDIGFIFQSSHLVP--------------YLKVIEQLTLVGQEAgmtkqqsstrAIQLLKNiGLEDRLNV 137
Cdd:COG4618 398 --QWDREELG-RHIGYLPQDVELFDgtiaeniarfgdadPEKVVAAAKLAGVHE----------MILRLPD-GYDTRIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 138 YPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRRLFEYADRVIELEDG 217
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIR-ALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
...
gi 447152655 218 KIT 220
Cdd:COG4618 543 RVQ 545
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-218 |
6.16e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGL-----LSQTSGTVLYNDAPLFDKQHRP 77
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 -SDLRLEDIGFIFQS--SHLVPYLKVIEQLTLV-GQEAGMTKQQSSTRAIQLLKNIGLED---RLNVYPHQLSGGEKQRV 150
Cdd:PRK15134 86 lRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVlSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 151 AIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD----RRLfeyADRVIELEDGK 218
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlsivRKL---ADRVAVMQNGR 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-219 |
1.20e-22 |
|
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: 91.02 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 29 VEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYN--DAPLFDKQHRPsdlrledIGFIFQSSHLVPYLKViEQLTL 106
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvDVTAAPPADRP-------VSMLFQENNLFAHLTV-EQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 107 VGQEAGMTKQQSSTRAIQ-LLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIR 185
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 447152655 186 QQIKEQQMIGIMITHD----RRLFeyaDRVIELEDGKI 219
Cdd:cd03298 173 DLHAETKMTVLMVTHQpedaKRLA---QRVVFLDNGRI 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-219 |
1.41e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.33 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGE-----------GLSETKVL---------KGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTS 60
Cdd:PRK10070 3 IKLEIKNLYKIFGEhpqrafkyieqGLSKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 61 GTVLYND---APLFDKQHRpsDLRLEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNV 137
Cdd:PRK10070 83 GQVLIDGvdiAKISDAELR--EVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 138 YPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVV-EMIRQQIKEQQMIgIMITHD-RRLFEYADRVIELE 215
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTI-VFISHDlDEAMRIGDRIAIMQ 239
|
....
gi 447152655 216 DGKI 219
Cdd:PRK10070 240 NGEV 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-219 |
1.66e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.46 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHrpsdlrLEDI----GFIFQSSH 93
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN------LWDIrnkaGMVFQNPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 94 LVPYLKVIEQLTLVGQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:PRK13633 96 NQIVATIVEEDVAFGPEnLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447152655 173 DADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-220 |
2.19e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.02 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 39 GASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHR---PSDLRleDIGFIFQSSHLVPYLKVIEQLTLvgqeaGMTK 115
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclPPEKR--RIGYVFQDARLFPHYKVRGNLRY-----GMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 116 QQSS--TRAIQLLkniGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVV---EMIRQQIKe 190
Cdd:PRK11144 104 SMVAqfDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLpylERLAREIN- 179
|
170 180 190
....*....|....*....|....*....|..
gi 447152655 191 qqmIGIM-ITHD-RRLFEYADRVIELEDGKIT 220
Cdd:PRK11144 180 ---IPILyVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-219 |
2.21e-22 |
|
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: 90.51 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaplFDKQHRPSDLRl 82
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPREVR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEqLCDRVAIIDHGRI 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-220 |
2.22e-22 |
|
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: 90.33 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsetKVLKGINFEVEQGEFVILnGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRl 82
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQqmIGIMITHDRRLFEY-ADRVIELEDGKIT 220
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESlCNQVAVLNKGKLV 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-219 |
3.19e-22 |
|
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: 90.12 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaplFDKQHRPSDLRL 82
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EdIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03266 79 R-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCI-LFSTHIMQEVErLCDRVVVLHRGRV 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-219 |
3.76e-22 |
|
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: 90.29 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQSSHLVpY 97
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLR-SQIGLVSQEPVLF-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNI-GLEDRLN--VYPH--QLSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDtlVGERgsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447152655 173 DADratkvVEMIRQQIKEQQMIG---IMITHdrRL--FEYADRVIELEDGKI 219
Cdd:cd03249 171 DAE-----SEKLVQEALDRAMKGrttIVIAH--RLstIRNADLIAVLQNGQV 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-221 |
1.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.22 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLF----DKQHRPSDLRledIGFIFQSSH 93
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRKR---IGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 94 LVPYLKVIEQLTLVG-QEAGMTKQQSSTRAIQLLKNIGLE-DRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTAS 171
Cdd:PRK13646 96 SQLFEDTVEREIIFGpKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447152655 172 LDADRATKVVEMIRQ-QIKEQQMIgIMITHD-RRLFEYADRVIELEDGKITD 221
Cdd:PRK13646 176 LDPQSKRQVMRLLKSlQTDENKTI-ILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-219 |
1.28e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqhRPSDLR 81
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 leDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:COG4152 72 --RIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTV-IFSSHQMELVEeLCDRIVIINKGRK 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-219 |
1.47e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFgeglSETKVLKGINFEVEQGEFVILNGASGSGKTTLLtilggllSQTSGTVLYNDAP------LFDKQHRPS 78
Cdd:PRK09984 7 VEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKSAgshielLGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 79 DLRlEDI-------GFIFQSSHLVPYLKVIEQLtLVGQeAGMT----------KQQSSTRAIQLLKNIGLEDrlnvYPHQ 141
Cdd:PRK09984 76 RLA-RDIrksrantGYIFQQFNLVNRLSVLENV-LIGA-LGSTpfwrtcfswfTREQKQRALQALTRVGMVH----FAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 ----LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDR--RLFEYADRVIELE 215
Cdd:PRK09984 149 rvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLR-DINQNDGITVVVTLHQvdYALRYCERIVALR 227
|
....
gi 447152655 216 DGKI 219
Cdd:PRK09984 228 QGHV 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-212 |
1.77e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.41 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLEDIGFIFQSSH--LVPY 97
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYgsLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTlvgqE-----AGMTKQQSSTRAIQLLKNIGLE----DRlnvYPHQLSGGEKQRVAIMRAFMNNPKIILADEP 168
Cdd:PRK11308 109 KKVGQILE----EpllinTSLSAAERREKALAMMAKVGLRpehyDR---YPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 169 TASLDADratkvvemIRQQIKE-----QQMIG---IMITHDRRLFEY-ADRVI 212
Cdd:PRK11308 182 VSALDVS--------VQAQVLNlmmdlQQELGlsyVFISHDLSVVEHiADEVM 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-219 |
4.26e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.21 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL--FDKQHRPSDLRleDIGFIFQSS--HLVP 96
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakLNRAQRKAFRR--DIQMVFQDSisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKV-------IEQLTlvgqeaGMTKQQSSTRAIQLLKNIGLE----DRLnvyPHQLSGGEKQRVAIMRAFMNNPKIILA 165
Cdd:PRK10419 105 RKTVreiirepLRHLL------SLDKAERLARASEMLRAVDLDdsvlDKR---PPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 166 DEPTASLDADRATkvvEMIRQQIKEQQMIGI---MITHDRRLFEY-ADRVIELEDGKI 219
Cdd:PRK10419 176 DEAVSNLDLVLQA---GVIRLLKKLQQQFGTaclFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
4.66e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIvkNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLR 81
Cdd:PRK11160 338 SLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI--ADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 lEDIGFIFQSSHLVP-YLKviEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLE------DRLNVY----PHQLSGGEKQRV 150
Cdd:PRK11160 414 -QAISVVSQRVHLFSaTLR--DNLLLAAPNA------SDEALIEVLQQVGLEklleddKGLNAWlgegGRQLSGGEQRRL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 151 AIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLTGLEQFDRICVMDNGQI 551
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-219 |
6.14e-21 |
|
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: 87.45 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYndapLFDKQHR---PSDLRlE 83
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGK-----------StllslitgdlpPTYGNDVR----LFGERRGgedVWELR-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 DIGFIfqSSHLVPYLKV---IEQLTLVG--------QEAgmTKQQSsTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAI 152
Cdd:COG1119 79 RIGLV--SPALQLRFPRdetVLDVVLSGffdsiglyREP--TDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITH---DrrLFEYADRVIELEDGKI 219
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveE--IPPGITHVLLLKDGRV 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-219 |
8.32e-21 |
|
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: 85.68 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 15 GLSETKVLKGINFEVEQGEFVILNGASGSGKT--TLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSdlrledIGFIFQSS 92
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKStlLNALAGRRTGLGVSGEVLINGRPLDKRSFRKI------IGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 93 HLVPYLKVIEQLTLVGQeagmtkqqsstraiqlLKNIgledrlnvyphqlSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:cd03213 92 ILHPTLTVRETLMFAAK----------------LRGL-------------SGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447152655 173 DADRATKVVEMIRqQIKEQQMIGIMITHDRR--LFEYADRVIELEDGKI 219
Cdd:cd03213 143 DSSSALQVMSLLR-RLADTGRTIICSIHQPSseIFELFDKLLLLSQGRV 190
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-212 |
1.19e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 88.22 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLEDIGFIFQS--SHLVPY 97
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLT--LVGQEAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDA 174
Cdd:PRK15079 115 MTIGEIIAepLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 447152655 175 DRATKVVEMIRQQIKEQQMIGIMITHDRRLFEY-ADRVI 212
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVL 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-219 |
1.53e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.73 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQS---------- 91
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--TDDNFEKLR-KHIGIVFQNpdnqfvgsiv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 ---------SHLVPYLKVIEQLTlvgqeagmtkqqsstraiQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:PRK13648 102 kydvafgleNHAVPYDEMHRRVS------------------EALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-221 |
1.84e-20 |
|
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: 89.09 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGT--VLYNDApLFDKQHRPSDLR---LEDIGFIFQSSHL 94
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDE-WVDMTKPGPDGRgraKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VPYLKVIEQLT-LVGQEagMTKQQSSTRAIQLLKNIGLEDR-----LNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEP 168
Cdd:TIGR03269 377 YPHRTVLDNLTeAIGLE--LPDELARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447152655 169 TASLDADRATKVVEMIRQQIKEQQMIGIMITHDRR-LFEYADRVIELEDGKITD 221
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKIVK 508
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-219 |
2.03e-20 |
|
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: 85.79 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaplFDKQHRPSDLRL 82
Cdd:TIGR04406 2 LVAENLIKSYKK----RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDG---QDITHLPMHERA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 E-DIGFIFQSSHLVPYLKVIEQLTLVGQEAG-MTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNP 160
Cdd:TIGR04406 75 RlGIGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 161 KIILADEPTASLDAdratKVVEMIRQQIK--EQQMIGIMIT-HD-RRLFEYADRVIELEDGKI 219
Cdd:TIGR04406 155 KFILLDEPFAGVDP----IAVGDIKKIIKhlKERGIGVLITdHNvRETLDICDRAYIISDGKV 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
2.42e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRl 82
Cdd:PRK13636 6 LKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQS-SHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK13636 82 ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKI 219
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-221 |
3.56e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTIlggllsqTSGTVLYNDAP--------LFDKQHRPSDLRlEDIGFI 88
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKL-------INGLLLPDDNPnskitvdgITLTAKTVWDIR-EKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 FQSSHLVPYLKVIEQLTLVGQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADE 167
Cdd:PRK13640 90 FQNPDNQFVGATVGDDVAFGLEnRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447152655 168 PTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-219 |
4.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPS--DLRlEDIGFIFQSSHLV 95
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkKLR-KKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 96 PYLK-VIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLD 173
Cdd:PRK13641 98 LFENtVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447152655 174 AdRATKvvEMIrQQIKEQQMIG---IMITHDR-RLFEYADRVIELEDGKI 219
Cdd:PRK13641 178 P-EGRK--EMM-QLFKDYQKAGhtvILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-218 |
6.65e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 6.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVlYNDAPLFDKQHRP----- 77
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV-QCDKMLLRRRSRQviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 -------SDLRLEDIGFIFQS--SHLVPYLKVIEQLT-LVGQEAGMTKQQSSTRAIQLLKNIGLEDR---LNVYPHQLSG 144
Cdd:PRK10261 92 eqsaaqmRHVRGADMAMIFQEpmTSLNPVFTVGEQIAeSIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 145 GEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLF-EYADRVIELEDGK 218
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGE 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-219 |
9.61e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 83.67 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRpsdlrledigfifqsshlvp 96
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK-------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKviEQLTLVGQEA-------------GMTkQQSSTRAIQLLKNIGLEDRLNVYPH-----------QLSGGEKQRVAI 152
Cdd:cd03248 85 YLH--SKVSLVGQEPvlfarslqdniayGLQ-SCSFECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTV--LVIAHRLSTVERADQILVLDGGRI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-219 |
1.03e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.37 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 23 KGINFEVEQGEFVILNGASGSGKTTLLTILGGL----LSQTSGTVLYNDAPLfdkqhRPSDLRLEDIGFIFQS--SHLVP 96
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPV-----APCALRGRKIATIMQNprSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLK----VIEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLEDR---LNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPT 169
Cdd:PRK10418 95 LHTmhthARETCLALGKPA------DDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 170 ASLDADRATKVVEMIrQQIKEQQMIGIMI-THD----RRLfeyADRVIELEDGKI 219
Cdd:PRK10418 169 TDLDVVAQARILDLL-ESIVQKRALGMLLvTHDmgvvARL---ADDVAVMSHGRI 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
1.13e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.67 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MA-LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrPSD 79
Cdd:PRK11650 1 MAgLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE--PAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 lrlEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNN 159
Cdd:PRK11650 76 ---RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 160 PKIILADEPTASLDAdratKV-VEMiRQQIKE-QQMIG---IMITHDRrlFE---YADRVIELEDGKI 219
Cdd:PRK11650 153 PAVFLFDEPLSNLDA----KLrVQM-RLEIQRlHRRLKttsLYVTHDQ--VEamtLADRVVVMNGGVA 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-217 |
1.26e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTtlltilggllsqT------------SGTVlyndaplfdkqHRPSDlrlEDIGFI 88
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKS------------TllraiaglwpygSGRI-----------ARPAG---ARVLFL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 FQSshlvPYLKV---IEQLTLVGQEAGMTKQQsstrAIQLLKNIGLE---DRLNV---YPHQLSGGEKQRVAIMRAFMNN 159
Cdd:COG4178 432 PQR----PYLPLgtlREALLYPATAEAFSDAE----LREALEAVGLGhlaERLDEeadWDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 160 PKIILADEPTASLDADRATKVVEMIRQQIKEqqMIGIMITHDRRLFEYADRVIELEDG 217
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREELPG--TTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-219 |
2.90e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDL 80
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL--ADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 --RLediGFIFQSSHLV-PYL--KVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLnvYPhQLSGGEKQRVAIMRA 155
Cdd:PRK13548 75 arRR---AVLPQHSSLSfPFTveEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRD--YP-QLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 156 FM------NNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGKI 219
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLaARYADRIVLLHQGRL 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-219 |
3.65e-19 |
|
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: 82.27 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQSSHLVPYlKV 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRKSLR-SMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 101 IEQLTLVGQEAGMTKQQSSTRAIQLLKNI-----GLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDad 175
Cdd:cd03254 94 MENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447152655 176 raTKVVEMIRQQIKE--QQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03254 172 --TETEKLIQEALEKlmKGRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-219 |
3.74e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.75 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYND--------------APLFDKQHRPSDLRlE 83
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitNPYSKKIKNFKELR-R 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 DIGFIFQSSHLVPYLKVIEQLTLVGQEA-GMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK13631 117 RVSMVFQFPEYQLFKDTIEKDIMFGPVAlGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTV-FVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-219 |
6.05e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.73 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 12 FGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQS 91
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI--SKENLKEIR-KKIGIIFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 shlvPYLKVI----EQLTLVGQEAGMTKQQSSTRAI-QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:PRK13632 92 ----PDNQFIgatvEDDIAFGLENKKVPPKKMKDIIdDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 167 EPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-220 |
6.49e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.54 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRpsDLRlEDIGFIFQSSHLVP 96
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR--EVR-KFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKVIEQLTLVGQ-EAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAD 175
Cdd:PRK13652 92 FSPTVEQDIAFGPiNLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447152655 176 RATKVVEMIRQQIKEQQMIGIMITHDRRLF-EYADRVIELEDGKIT 220
Cdd:PRK13652 172 GVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIV 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-219 |
1.19e-18 |
|
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: 81.12 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 12 FGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHrpSDLRlEDIGFIFQS 91
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTL--ASLR-RQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 SHLVpYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNI-----GLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:cd03251 85 VFLF-NDTVAENIAYGRPGATREEVEEAARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 167 EPTASLDAdratkVVEMIRQQIKEQQMIG---IMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03251 164 EATSALDT-----ESERLVQAALERLMKNrttFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-219 |
1.28e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.84 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllsqT-------------SGTVLYND 67
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGK-------------TttfymivglvkpdSGRIFLDG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 68 AplfDKQHRPSDLR-LEDIGF------IFQsshlvpYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPH 140
Cdd:COG1137 65 E---DITHLPMHKRaRLGIGYlpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 141 QLSGGEKQRVAIMRAFMNNPKIILADEPTASLD--AdratkvVEMIRQQIKE--QQMIGIMIT-HD-RRLFEYADRVIEL 214
Cdd:COG1137 136 SLSGGERRRVEIARALATNPKFILLDEPFAGVDpiA------VADIQKIIRHlkERGIGVLITdHNvRETLGICDRAYII 209
|
....*
gi 447152655 215 EDGKI 219
Cdd:COG1137 210 SEGKV 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-219 |
1.34e-18 |
|
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: 80.34 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaPLFDKQHRPsdlrL 82
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEA----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQqsstRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 163 ILADEPTASLDADRATKVVEMIRQqiKEQQMIGIMI-THD-RRLFEYADRVIELEDGKI 219
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILS--LRDQGITVLIsSHLlSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-219 |
1.83e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.32 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL-----FDKQHRpsdlrledIGFIFQS 91
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvWDIRHK--------IGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 SHLVPYLKVIEQLTLVGQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTA 170
Cdd:PRK13650 90 PDNQFVGATVEDDVAFGLEnKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447152655 171 SLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-201 |
2.03e-18 |
|
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: 83.18 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHrpSDLRlEDIGFIFQSSHLVPyLKV 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ--DEVR-RRVSVCAQDAHLFD-TTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 101 IEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLEDRLNVYPH-----------QLSGGEKQRVAIMRAFMNNPKIILADEPT 169
Cdd:TIGR02868 426 RENLRLARPDA------TDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|..
gi 447152655 170 ASLDADRATKVVEMIRQQIKEQQMigIMITHD 201
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGRTV--VLITHH 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-220 |
3.29e-18 |
|
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: 80.03 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAP 69
Cdd:COG0410 2 PMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGK-----------TtllkaisgllpPRSGSIRFDGED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 70 LfdkQHRPSDLRLED-IGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSST--RAIQLLKNigLEDRLNVYPHQLSGGE 146
Cdd:COG0410 67 I---TGLPPHRIARLgIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADleRVYELFPR--LKERRRQRAGTLSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 147 KQRVAIMRAFMNNPKIILADEPTASLdadrATKVVEMIRQQIKE--QQMIGIMIT--HDRRLFEYADRVIELEDGKIT 220
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGL----APLIVEEIFEIIRRlnREGVTILLVeqNARFALEIADRAYVLERGRIV 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-219 |
3.30e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 26 NFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRleDIGFIFQSSHLVPYLKVIEQLT 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTPPSRR--PVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 106 LvGQEAGM--TKQQSSTRAiQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEM 183
Cdd:PRK10771 94 L-GLNPGLklNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447152655 184 IRQQIKEQQMIGIMITHD----RRLfeyADRVIELEDGKI 219
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSledaARI---APRSLVVADGRI 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-219 |
3.60e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-------------QTSGTVLYNDAPLFDKqhrPSDLR-LE 83
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGK-----------StlakvlmghpkyeVTSGSILLDGEDILEL---SPDERaRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 DIGFIFQSSHLVPYLKVIEQL-TLVGQEAG--MTKQQSSTRAIQLLKNIGLE----DR-LNVyphQLSGGEKQRVAIMRA 155
Cdd:COG0396 78 GIFLAFQYPVEIPGVSVSNFLrTALNARRGeeLSAREFLKLLKEKMKELGLDedflDRyVNE---GFSGGEKKRNEILQM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 156 FMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRRLFEY--ADRVIELEDGKI 219
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVN-KLRSPDRGILIITHYQRILDYikPDFVHVLVDGRI 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
25-202 |
4.76e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.42 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfDKQHRPSDLRleDIGFIFQSSHLVPYLKVIEQL 104
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV---DLSHVPPYQR--PINMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 105 TLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDA---DRAT-KV 180
Cdd:PRK11607 113 AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrDRMQlEV 192
|
170 180
....*....|....*....|....*
gi 447152655 181 VEMIRQqikeqqmIG---IMITHDR 202
Cdd:PRK11607 193 VDILER-------VGvtcVMVTHDQ 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-213 |
5.48e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.57 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGG-----LLSQTSGTVLYNDAPLFdkQHRP 77
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIF--KMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 SDLRlEDIGFIFQSSHLVPYLKVIEQ--LTLVGQEAGMTKQQSSTRAIQLLKNIGL----EDRLNVYPHQLSGGEKQRVA 151
Cdd:PRK14247 78 IELR-RRVQMVFQIPNPIPNLSIFENvaLGLKLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 152 IMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEqqMIGIMITH---------DRRLFEYADRVIE 213
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHfpqqaarisDYVAFLYKGQIVE 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-214 |
5.61e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.50 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTI-----LGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLEdIGFIFQS 91
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllELNEEARVEGEVRLFGRNIYSPDVDPIEVRRE-VGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 SHLVPYLKVIEQLTLVGQEAGMTKQQSS--TRAIQLLKNIGL----EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILA 165
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 166 DEPTASLDADRATKVVEMIRqQIKEQQMIgIMITH---------DRRLFEYADRVIEL 214
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLF-ELKKEYTI-VLVTHspaqaarvsDYVAFLYLGKLIEV 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-201 |
8.52e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLsQTSGTVLYNDAPLFD---KQHRPSDLRledIGFIFQ--SSHLV 95
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNlnrRQLLPVRHR---IQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 96 PYLKV---IEQLTLVGQEAgMTKQQSSTRAIQLLKNIGLE-DRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTAS 171
Cdd:PRK15134 377 PRLNVlqiIEEGLRVHQPT-LSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190
....*....|....*....|....*....|
gi 447152655 172 LDADRATKVVEMIRQQIKEQQMIGIMITHD 201
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-219 |
9.29e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.95 E-value: 9.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQ--TSGTVLYNDAPLFDKQhrPSDLRLEDIG 86
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLP--PEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQSSHLVPYLKVIEQLTLVgqeagmtkqqsstraiqllkNIGLedrlnvyphqlSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLRYV--------------------NEGF-----------SGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 167 EPTASLDADrATKVVEMIRQQIKEQQMIGIMITHDRRLFEY--ADRVIELEDGKI 219
Cdd:cd03217 130 EPDSGLDID-ALRLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-220 |
1.02e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.53 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRpsdlRLEDIGFIF-QSSHLVP 96
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK----FLRRIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADR 176
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447152655 177 ATKVVEMIRQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKIT 220
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEaLARRVLVIDKGRLL 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
1.15e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDL 80
Cdd:PRK09536 2 PMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 RLED------IGFIFQSSHLV-----PYLkvieqltlvGQEAGMTkqQSSTRAIQLLKNIGLEDRLNVYP-HQLSGGEKQ 148
Cdd:PRK09536 78 RVASvpqdtsLSFEFDVRQVVemgrtPHR---------SRFDTWT--ETDRAAVERAMERTGVAQFADRPvTSLSGGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 149 RVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRL-FEYADRVIELEDGKITD 221
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTA-VAAIHDLDLaARYCDELVLLADGRVRA 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-219 |
2.12e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFgeglSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPlfdkQHRPSDLRL 82
Cdd:PRK15439 12 LCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP----CARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIG--FIFQSSHLVPYLKVIEQLTLvgqeaGMTKQQSSTRAI-QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNN 159
Cdd:PRK15439 84 HQLGiyLVPQEPLLFPNLSVKENILF-----GLPKRQASMQKMkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 160 PKIILADEPTASLdadraTKV-VEMIRQQIKE--QQMIGIM-ITHD-RRLFEYADRVIELEDGKI 219
Cdd:PRK15439 159 SRILILDEPTASL-----TPAeTERLFSRIREllAQGVGIVfISHKlPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-219 |
2.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.52 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYND----APLFDKQHRPsdLRlEDIGFIFQSSH 93
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitAGKKNKKLKP--LR-KKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 94 LVPYLKVIEQLTLVG-QEAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTAS 171
Cdd:PRK13634 96 HQLFEETVEKDICFGpMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447152655 172 LDADRATKVVEMIRQQIKEQQMIGIMITHDRR-LFEYADRVIELEDGKI 219
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKGTV 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-200 |
2.26e-17 |
|
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: 77.01 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqHRPSDLRLEDIGFIFQSSHLVPY 97
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGQEAGmtkqqSSTRAI-QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADR 176
Cdd:TIGR01189 88 LSALENLHFWAAIHG-----GAQRTIeDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....
gi 447152655 177 ATKVVEMIRQQIkEQQMIGIMITH 200
Cdd:TIGR01189 163 VALLAGLLRAHL-ARGGIVLLTTH 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-219 |
2.74e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKT---TLLTILGGLLSQTSGTVLYNDAPL-FDKQHRPSdlrlediGFIFQSSHLVPY 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTtlmNALAFRSPKGVKGSGSVLLNGMPIdAKEMRAIS-------AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTL---VGQEAGMTKQQSSTRAIQLLKN----------IGLEDRLNVyphqLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:TIGR00955 114 LTVREHLMFqahLRMPRRVTKKEKRERVDEVLQAlglrkcantrIGVPGRVKG----LSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 165 ADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHD--RRLFEYADRVIELEDGKI 219
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLK-GLAQKGKTIICTIHQpsSELFELFDKIILMAEGRV 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
3.98e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEglseTKVLKGINFEVEQGEFVIL---NGAsgsGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRP 77
Cdd:COG3845 4 PALELRGITKRFGG----VVANDDVSLTVRPGEIHALlgeNGA---GKSTLMKILYGLYQPDSGEILIDGKPV--RIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 SD-LRLeDIGFIFQSSHLVPYLKVIEQLTLvGQEAGMTKQQSSTRAIQLLKNI----GLEDRLNVYPHQLSGGEKQRVAI 152
Cdd:COG3845 75 RDaIAL-GIGMVHQHFMLVPNLTVAENIVL-GLEPTKGGRLDRKAARARIRELseryGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHdrRL---FEYADRVIELEDGKITD 221
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSI-IFITH--KLrevMAIADRVTVLRRGKVVG 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-221 |
4.84e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.52 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLF--DKQHRPSDLRLedigfIFQ--SSHLV 95
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRM-----IFQdpSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 96 PYLKVIEQLTL-VGQEAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLD 173
Cdd:PRK15112 102 PRQRISQILDFpLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447152655 174 ADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEY-ADRVIELEDGKITD 221
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-218 |
5.46e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEGLsetkVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqhrPSDL 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV------PARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 RL--EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMN 158
Cdd:PRK13536 110 RLarARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 159 NPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHdrrLFEYADRVIE----LEDGK 218
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTI-LLTTH---FMEEAERLCDrlcvLEAGR 249
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-219 |
5.54e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRpsdlrledigfifqsshlvpYLKv 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH--------------------YLH- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 101 iEQLTLVGQE------------------AGMTKQQSSTRAIQLLKNI-GLEDRLN--VYPH--QLSGGEKQRVAIMRAFM 157
Cdd:TIGR00958 555 -RQVALVGQEpvlfsgsvreniaygltdTPDEEIMAAAKAANAHDFImEFPNGYDteVGEKgsQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 158 NNPKIILADEPTASLDADratkvVEMIRQQIKEQQ-MIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:TIGR00958 634 RKPRVLILDEATSALDAE-----CEQLLQESRSRAsRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-211 |
6.17e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEGLsetkVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSdlr 81
Cdd:PRK13537 7 PIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 lEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK13537 80 -QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHdrrLFEYADRV 211
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTI-LLTTH---FMEEAERL 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-219 |
1.47e-16 |
|
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: 75.34 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQSSHL----- 94
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLR-RAIGVVPQDTVLfndti 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 ---VPYLKVieqltlvgqeaGMTKQQsstrAIQLLKNIGLEDRLNVYPHQ-----------LSGGEKQRVAIMRAFMNNP 160
Cdd:cd03253 92 gynIRYGRP-----------DATDEE----VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 161 KIILADEPTASLDADRATKVVEMIRQQIKEQQmiGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRT--TIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-218 |
1.82e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.61 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 14 EGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILG--GLLSQTSGTVLYNDaplfdkqHRPSDLRLEDIGFIFQS 91
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTILANN-------RKPTKQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 SHLVPYLKVIEQL---TLVGQEAGMTKQQSSTRAIQLLKNIGL---EDRL--NVYPHQLSGGEKQRVAIMRAFMNNPKII 163
Cdd:PLN03211 149 DILYPHLTVRETLvfcSLLRLPKSLTKQEKILVAESVISELGLtkcENTIigNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 164 LADEPTASLDADRATKVVEMIRQQI-KEQQMIGIMITHDRRLFEYADRVIELEDGK 218
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
84-201 |
2.03e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.48 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 DIGFIFQ--SSHLVPYLKVIEQLTLV---GQEAGM---TKQQSSTRAIQLLKNIGLEDR---LNVYPHQLSGGEKQRVAI 152
Cdd:COG4170 90 EIAMIFQepSSCLDPSAKIGDQLIEAipsWTFKGKwwqRFKWRKKRAIELLHRVGIKDHkdiMNSYPHELTEGECQKVMI 169
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD 201
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-218 |
3.12e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLS-----QTSGTVLYNDAPLFDKQHRPSDLRLEdIGFIFQSSHL 94
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTVDLRKE-IGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VP---YLKVIEQLTLvgqeAGMTKQQSSTRAIQL-LKNIGL----EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:PRK14239 98 FPmsiYENVVYGLRL----KGIKDKQVLDEAVEKsLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 167 EPTASLDADRATKVVEMIrQQIKEQQMIgIMITH---------DRRLFEYADRVIELEDGK 218
Cdd:PRK14239 174 EPTSALDPISAGKIEETL-LGLKDDYTM-LLVTRsmqqasrisDRTGFFLDGDLIEYNDTK 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-203 |
4.76e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 8 IVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDA-----PLFDKQHRpsdlrl 82
Cdd:PRK10895 5 TAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 eDIGFIFQSSHLVPYLKVIEQLTLVGQ-EAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK10895 79 -GIGYLPQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447152655 162 IILADEPTASLDADRATKVVEMIrQQIKEQQMiGIMIT-HDRR 203
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRII-EHLRDSGL-GVLITdHNVR 198
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-214 |
7.07e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.65 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVlyndaplfdkqHRPSDLRledIGFIFQSSHLVPYLKV 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGAR---VAYVPQRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 101 -IEQLTLVG--QEAGMTKQQS-STRAI--QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDA 174
Cdd:NF040873 73 tVRDLVAMGrwARRGLWRRLTrDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447152655 175 DRATKVVEMIRQQIKEQQMIgIMITHDRRLFEYADRVIEL 214
Cdd:NF040873 153 ESRERIIALLAEEHARGATV-VVVTHDLELVRRADPCVLL 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-218 |
7.25e-16 |
|
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: 72.89 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 14 EGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYND----AP--------------LFDKQH 75
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayVSqepwiqngtireniLFGKPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 76 RPSdlRLEDIgfiFQSSHLVPYLKVIEQ--LTLVGqEAGMTkqqsstraiqllknigledrlnvyphqLSGGEKQRVAIM 153
Cdd:cd03250 93 DEE--RYEKV---IKACALEPDLEILPDgdLTEIG-EKGIN---------------------------LSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 154 RAFMNNPKIILADEPTASLDADRATKVVEM-IRQQIKEQQMIgIMITHDRRLFEYADRVIELEDGK 218
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTR-ILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-219 |
8.10e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.25 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLed 84
Cdd:PRK13644 4 LENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQSSHLVPYLKVIEQLTLVGQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKII 163
Cdd:PRK13644 79 VGIVFQNPETQFVGRTVEEDLAFGPEnLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 164 LADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTI-VYITHNLEELHDADRIIVMDRGKI 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-221 |
1.03e-15 |
|
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: 73.29 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLY--NDAPLFDkqhrPSDLRLEdIGFIFQSSHL---- 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLALAD----PAWLRRQ-VGVVLQENVLfnrs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 -----------VPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGledrlnvyphqLSGGEKQRVAIMRAFMNNPKII 163
Cdd:cd03252 92 irdnialadpgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAG-----------LSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 164 LADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTV--IIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-219 |
1.26e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.23 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDL---R--LEdigfifQSSHLV 95
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL--AAWSPWELarrRavLP------QHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 96 -PYLkvIEQLTLVGQEAGMTKQQSSTRAIQ-------LLkniGLEDRLnvYPhQLSGGEKQRVAIMRAF-------MNNP 160
Cdd:COG4559 88 fPFT--VEEVVALGRAPHGSSAAQDRQIVRealalvgLA---HLAGRS--YQ-TLSGGEQQRVQLARVLaqlwepvDGGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 161 KIILADEPTASLDadratkvvemIRQQI------KE--QQMIG-IMITHDRRL-FEYADRVIELEDGKI 219
Cdd:COG4559 160 RWLFLDEPTSALD----------LAHQHavlrlaRQlaRRGGGvVAVLHDLNLaAQYADRILLLHQGRL 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-219 |
1.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.61 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 19 TKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFD--KQHRPSDLRlEDIGFIFQ--SSHL 94
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVR-KKVGVVFQfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VPYlKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRL-NVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLD 173
Cdd:PRK13643 98 FEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447152655 174 ADRATKVVEMIrQQIKEQQMIGIMITH-DRRLFEYADRVIELEDGKI 219
Cdd:PRK13643 177 PKARIEMMQLF-ESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-219 |
2.21e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKG-INFEVEQGEFVILNGASGSGKttlltilggllsqTS------------GTVLYNDAPLfdkqhrpSDLRLED-- 84
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGK-------------TSllnallgflpyqGSLKINGIEL-------RELDPESwr 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 --IGFIFQSSHLvPYLKVIEQLTLVGQEAgmtkqqSSTRAIQLLKNIGLEDRLNVYPH-----------QLSGGEKQRVA 151
Cdd:PRK11174 423 khLSWVGQNPQL-PHGTLRDNVLLGNPDA------SDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 152 IMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHdrRLFEYA--DRVIELEDGKI 219
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTH--QLEDLAqwDQIWVMQDGQI 561
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-216 |
2.58e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 70.65 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKttlltilggllsqTS-------------GTVlyndaplfdkqHRPSDlrlEDIGF 87
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGK-------------SSlfralaglwpwgsGRI-----------GMPEG---EDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 88 IFQsshlVPYLKvieQLTLvgqeagmtKQQSstraiqllknigledrlnVYP--HQLSGGEKQRVAIMRAFMNNPKIILA 165
Cdd:cd03223 69 LPQ----RPYLP---LGTL--------REQL------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447152655 166 DEPTASLDADRATKvvemIRQQIKEQQMIGIMITHDRRLFEYADRVIELED 216
Cdd:cd03223 116 DEATSALDEESEDR----LYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-218 |
3.01e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.78 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLsetkVLKGINFEVEQGEFVILNGASGSGKttlltilggllsqtsgtvlyndaplfdkqhrpsdlrl 82
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGK------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 edigfifqsSHLvpyLKVIeqltlvgqeAGMTKQQSSTraIQLLKNIGLedrlnVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:cd03221 40 ---------STL---LKLI---------AGELEPDEGI--VTWGSTVKI-----GYFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 163 ILADEPTASLDADratkVVEMIRQQIKEQQMIGIMITHDRRLF-EYADRVIELEDGK 218
Cdd:cd03221 92 LLLDEPTNHLDLE----SIEALEEALKEYPGTVILVSHDRYFLdQVATKIIELEDGK 144
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-221 |
3.41e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL---FDKQHRPSDLRLEdIGFIFQSSHL 94
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanLKKIKEVKRLRKE-IGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VPYLKVIEQLTLVGQ-EAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:PRK13645 102 QLFQETIEKDIAFGPvNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447152655 173 DADRATKVVEMIRQQIKEQQMIGIMITHDR-RLFEYADRVIELEDGKITD 221
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVIS 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-221 |
9.28e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDA---PLFDKQHRPsdLRlEDIGFIFQSSH- 93
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQA--LR-RDIQFIFQDPYa 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 94 -LVPYLKV----IEQLTLVGQEAGmtkQQSSTRAIQLLKNIGLE-DRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADE 167
Cdd:PRK10261 413 sLDPRQTVgdsiMEPLRVHGLLPG---KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 168 PTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKITD 221
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVE 544
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-219 |
1.04e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNF-----GEGLSET------------KVLKGINFEVEQGEFVILNGASGSGKttlltilggllS------- 57
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLKGAlkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGK-----------Sttikmlt 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 58 ----QTSGTVLYNDaplfdkqHRPSDLR---LEDIGFIF-QSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNI 129
Cdd:COG4586 70 gilvPTSGEVRVLG-------YVPFKRRkefARRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 130 GLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD----RRLf 205
Cdd:COG4586 143 DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddiEAL- 221
|
250
....*....|....
gi 447152655 206 eyADRVIELEDGKI 219
Cdd:COG4586 222 --CDRVIVIDHGRI 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-221 |
1.66e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.08 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 16 LSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLS------QTSGTVLYNDAPLFdkQHRPSDLRLEdIGFIF 89
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIF--QIDAIKLRKE-VGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 90 QSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQ-LLKNIGL----EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 165 ADEPTASLDAdRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:PRK14246 177 MDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-220 |
2.18e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.16 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDApLFDKQHRPSDLRL--EDIGFIFQ--SSH 93
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDT-LITSTSKNKDIKQirKKVGLVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 94 LVPYlKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:PRK13649 98 LFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447152655 173 DAdRATKVVEMIRQQIKEQQMIGIMITH---DrrLFEYADRVIELEDGKIT 220
Cdd:PRK13649 177 DP-KGRKELMTLFKKLHQSGMTIVLVTHlmdD--VANYADFVYVLEKGKLV 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-219 |
2.28e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrPSDLRLEDIGFIFQSSHLVPY 97
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQ--TAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGQEAGMTK-QQSSTRAIQLLKNigLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADR 176
Cdd:PRK11614 95 MTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447152655 177 ATKVVEMIrQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:PRK11614 173 IQQIFDTI-EQLREQGMTIFLVEQNaNQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-219 |
2.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.12 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFgEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRl 82
Cdd:PRK13642 5 LEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL--TAENVWNLR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK13642 81 RKIGMVFQNPDNQFVGATVEDDVAFGMEnQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-200 |
3.06e-14 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 68.96 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLsetkVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaplfdkqHRPSDLRL 82
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG-------HPWTRKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQqsstRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKI 162
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 447152655 163 ILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITH 200
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIR-SFPEQGITVILSSH 182
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-213 |
3.57e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.30 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS----------------QTSGTVLYNDAPLFDKQHRPSDLR 81
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGK-----------StllrclnrmndlipgaRVEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 LEdIGFIFQSSHLVP---Y------LKVieqltlvgqeAGMT-KQQSSTRAIQLLKNIGL----EDRLNVYPHQLSGGEK 147
Cdd:COG1117 92 RR-VGMVFQKPNPFPksiYdnvaygLRL----------HGIKsKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 148 QRVAIMRAFMNNPKIILADEPTASLDaDRATKVVEMIRQQIKEQQMIgIMITH---------DRRLFEYADRVIE 213
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALD-PISTAKIEELILELKKDYTI-VIVTHnmqqaarvsDYTAFFYLGELVE 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-217 |
3.98e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPlFDKQHrPSDLRLEDIGFI 88
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLD-HKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 FQSSHLVPYLKVIEQLtLVGQEagMTKQ----------QSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMN 158
Cdd:PRK09700 86 YQELSVIDELTVLENL-YIGRH--LTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 159 NPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHD-RRLFEYADRVIELEDG 217
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAI-VYISHKlAEIRRICDRYTVMKDG 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
14-219 |
7.42e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.33 E-value: 7.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 14 EGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQtSGTVLYNDAPLFD-KQHRPSDLRlediGFIFQSS 92
Cdd:COG4138 4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDwSAAELARHR----AYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 93 HLVPYLKVIEQLTLvGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFM-----NNP--KIILA 165
Cdd:COG4138 79 SPPFAMPVFQYLAL-HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 166 DEPTASLDadratkvvemIRQQIK---------EQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:COG4138 158 DEPMNSLD----------VAQQAAldrllrelcQQGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-219 |
8.87e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLY--NDAPLFDKQHRP-SD 79
Cdd:PRK11701 7 LSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmRDGQLRDLYALSeAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 LRL---EDIGFIFQssHLVPYLK--------VIEQLTLVGQEA-GMTKQQsstrAIQLLKNIGLE-DRLNVYPHQLSGGE 146
Cdd:PRK11701 83 RRRllrTEWGFVHQ--HPRDGLRmqvsaggnIGERLMAVGARHyGDIRAT----AGDWLERVEIDaARIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 147 KQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD---RRLFeyADRVIELEDGKI 219
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlavARLL--AHRLLVMKQGRV 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-214 |
9.62e-14 |
|
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: 67.13 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 8 IVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqHRPSDLRLEDIGF 87
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 88 IFQSSHLVPYLKVIEQLTLVgqeagmtKQQSSTRAI-QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:cd03231 78 LGHAPGIKTTLSVLENLRFW-------HADHSDEQVeEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447152655 167 EPTASLDADRATKVVEMIRQQIKEQQMIgIMITH-DRRLFEYADRVIEL 214
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMV-VLTTHqDLGLSEAGARELDL 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
16-218 |
1.24e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 16 LSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQtSGTVLYNDAPLfdkqhrpSDLRLEDI----GFIFQS 91
Cdd:PRK03695 6 VAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPL-------EAWSAAELarhrAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 SHLVPYLKVIEQLTLvGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFM-----NNP--KIIL 164
Cdd:PRK03695 78 QTPPFAMPVFQYLTL-HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 165 ADEPTASLDadratkvvemIRQQ------IKE--QQMIG-IMITHD-RRLFEYADRVIELEDGK 218
Cdd:PRK03695 157 LDEPMNSLD----------VAQQaaldrlLSElcQQGIAvVMSSHDlNHTLRHADRVWLLKQGK 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-220 |
1.30e-13 |
|
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: 66.90 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 7 DIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKT---TLLTILGGLLSQTSGTVLYNDAPL--FDKQHRpsdlr 81
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCStllKALANRTEGNVSVEGDIHYNGIPYkeFAEKYP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 lEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGmtkqqsstraiqllknigledrlNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:cd03233 83 -GEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD--RRLFEYADRVIELEDGKIT 220
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-218 |
1.38e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPlfdkQHRPS--DLRLEDIGFIFQSSHLVPY 97
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE----MRFASttAALAAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLvGQ---EAGMTKQ-QSSTRAIQLLKNIGLEdrlnVYPHQ----LSGGEKQRVAIMRAFMNNPKIILADEPT 169
Cdd:PRK11288 94 MTVAENLYL-GQlphKGGIVNRrLLNYEAREQLEHLGVD----IDPDTplkyLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447152655 170 ASLDADRATKVVEMIRQQIKEQQMIgIMITHdrRL---FEYADRVIELEDGK 218
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVI-LYVSH--RMeeiFALCDAITVFKDGR 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-219 |
1.62e-13 |
|
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: 69.00 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL--FDK-QHRPSD 79
Cdd:TIGR01193 474 IVINDVSYSYGYG---SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkdIDRhTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 LRLEDIGFIFQSShlvpylkVIEQLtLVGQEAGMTKQQ--SSTRAIQLLKNI-----GLEDRLNVYPHQLSGGEKQRVAI 152
Cdd:TIGR01193 551 NYLPQEPYIFSGS-------ILENL-LLGAKENVSQDEiwAACEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 153 MRAFMNNPKIILADEPTASLDADRATKVVEMIrqqIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNL---LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-221 |
1.75e-13 |
|
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: 67.16 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYND---APLFDKQHRPSD 79
Cdd:TIGR02323 4 LQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgAELELYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 80 LRL---EDIGFIFQssHLVPYLK--------VIEQLTLVGQEA-GMTKQQsstrAIQLLKNIGLE-DRLNVYPHQLSGGE 146
Cdd:TIGR02323 80 RRRlmrTEWGFVHQ--NPRDGLRmrvsaganIGERLMAIGARHyGNIRAT----AQDWLEEVEIDpTRIDDLPRAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 147 KQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD---RRLFeyADRVIELEDGKITD 221
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlgvARLL--AQRLLVMQQGRVVE 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-219 |
1.76e-13 |
|
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: 65.92 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 14 EGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRLEDIGFIFQSSH 93
Cdd:cd03215 8 RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV--TRRSPRDAIRAGIAYVPEDRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 94 ---LVPYLKVIEqltlvgqeagmtkqqsstraiqllkNIGLedrlnvyPHQLSGGEKQRVAIMRAFMNNPKIILADEPTA 170
Cdd:cd03215 86 regLVLDLSVAE-------------------------NIAL-------SSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 171 SLDAdrATKvvEMIRQQIKEQQMIG---IMITHD-RRLFEYADRVIELEDGKI 219
Cdd:cd03215 134 GVDV--GAK--AEIYRLIRELADAGkavLLISSElDELLGLCDRILVMYEGRI 182
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-201 |
2.19e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTT-----LLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLE 83
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkclNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 dIGFIFQSSHLVP---YLKVIEQLTLVGQEAGMTKQ---QSSTRAIQLLKNIglEDRLNVYPHQLSGGEKQRVAIMRAFM 157
Cdd:PRK14258 90 -VSMVHPKPNLFPmsvYDNVAYGVKIVGWRPKLEIDdivESALKDADLWDEI--KHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447152655 158 NNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD 201
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
2.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEGlseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVlyndaPLFDKQHRPSDLR 81
Cdd:PRK13647 4 IIEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV-----KVMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 L--EDIGFIFQS-SHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMN 158
Cdd:PRK13647 76 WvrSKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 159 NPKIILADEPTASLDAdRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGKI 219
Cdd:PRK13647 156 DPDVIVLDEPMAYLDP-RGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-220 |
5.40e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVlyndaplfdk 73
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGK-----------StllkilagelePDSGEV---------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 74 qHRPSDLRledIGFIFQSSHLVPYLKVIE--------------QLTLVGQEAGMTKQQSS------------------TR 121
Cdd:COG0488 56 -SIPKGLR---IGYLPQEPPLDDDLTVLDtvldgdaelraleaELEELEAKLAEPDEDLErlaelqeefealggweaeAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 122 AIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAdratkvvEMIR---QQIKEQQMIGIM 197
Cdd:COG0488 132 AEEILSGLGFpEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESIEwleEFLKNYPGTVLV 204
|
250 260
....*....|....*....|....
gi 447152655 198 ITHDRR-LFEYADRVIELEDGKIT 220
Cdd:COG0488 205 VSHDRYfLDRVATRILELDRGKLT 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-218 |
6.02e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.78 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGLSetkvLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDlRL 82
Cdd:PRK11300 6 LSVSGLMMRFGGLLA----VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI---EGLPGH-QI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 EDIGFI--FQSSHLVPYLKVIEQLtLVGQE--------AGMTK--------QQSSTRAIQLLKNIGLEDRLNVYPHQLSG 144
Cdd:PRK11300 78 ARMGVVrtFQHVRLFREMTVIENL-LVAQHqqlktglfSGLLKtpafrraeSEALDRAATWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 145 GEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGK 218
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLvMGISDRIYVVNQGT 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-218 |
6.62e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 8 IVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGL--LSQTSGTVLYNDAPLfdKQHRPSDLRLEDI 85
Cdd:PRK13549 11 ITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEEL--QASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 86 GFIFQSSHLVPYLKVIEQLTLvGQEAG----MTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFL-GNEITpggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 162 IILADEPTASLDAdRATKVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGK 218
Cdd:PRK13549 164 LLILDEPTASLTE-SETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-219 |
6.88e-13 |
|
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: 65.21 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDIGFIFQSSHLV----- 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI--SKIGLHDLR-SRISIIPQDPVLFsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 96 ----PYLKVI-EQLTLVGQEAGMtkqqsstRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTA 170
Cdd:cd03244 96 snldPFGEYSdEELWQALERVGL-------KEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447152655 171 SLDADRATKVVEMIRQQIKEQQMigIMITHdrRL---FEYaDRVIELEDGKI 219
Cdd:cd03244 169 SVDPETDALIQKTIREAFKDCTV--LTIAH--RLdtiIDS-DRILVLDKGRV 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-211 |
9.97e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKTTL-----LTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRlEDIGFIFQSSHLVP 96
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnRLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEVR-RRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 ---YLKVIEQLTLVGQEAGMTKQ-QSSTRAIQLLKNIglEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASL 172
Cdd:PRK14243 105 ksiYDNIAYGARINGYKGDMDELvERSLRQAALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 447152655 173 DADRATKVVEMIrQQIKEQQMIgIMITHDrrlFEYADRV 211
Cdd:PRK14243 183 DPISTLRIEELM-HELKEQYTI-IIVTHN---MQQAARV 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-204 |
1.04e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLyndaplfdkqhRPSDLRled 84
Cdd:PRK09544 7 LENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLR--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQSSHLVPYLKvieqLTlVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:PRK09544 69 IGYVPQKLYLDTTLP----LT-VNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447152655 165 ADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL 204
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-218 |
1.49e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTS--GTVLYNDAPLfdKQHRPSDL 80
Cdd:TIGR02633 2 LEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPL--KASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 RLEDIGFIFQSSHLVPYLKVIE------QLTLVGQEagMTKQQSSTRAIQLLKNIGLEDRLNVYP-HQLSGGEKQRVAIM 153
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAEniflgnEITLPGGR--MAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 154 RAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHdrRLFEYA---DRVIELEDGK 218
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIR-DLKAHGVACVYISH--KLNEVKavcDTICVIRDGQ 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-216 |
3.25e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfdkqHRPSDLRLE----DIGFIFQSSH 93
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS------HNLKDINLKwwrsKIGVVSQDPL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 94 L--------VPY----LKVIEQLTLVGQEAG-----------------------MTKQQSSTRAIQLLKN---------- 128
Cdd:PTZ00265 471 LfsnsiknnIKYslysLKDLEALSNYYNEDGndsqenknkrnscrakcagdlndMSNTTDSNELIEMRKNyqtikdsevv 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 129 -----IGLEDRLNVYP-----------HQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQ 192
Cdd:PTZ00265 551 dvskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
250 260
....*....|....*....|....
gi 447152655 193 MIGIMITHDRRLFEYADRVIELED 216
Cdd:PTZ00265 631 RITIIIAHRLSTIRYANTIFVLSN 654
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
1.12e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEglseTKVLKGINFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVL------- 64
Cdd:COG0488 316 LELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGK-----------StllkllagelePDSGTVKlgetvki 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 65 -YndaplFDkQHRpSDLRLEDigfifqsshlvpylKVIEQLTLVGQEAgmtkqqSSTRAIQLLKNIGL-EDRLNVYPHQL 142
Cdd:COG0488 381 gY-----FD-QHQ-EELDPDK--------------TVLDELRDGAPGG------TEQEVRGYLGRFLFsGDDAFKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 143 SGGEKQRVAIMRAFMNNPKIILADEPTASLDadratkvVEMIrqQIKEQQMIG-----IMITHDRRLFE-YADRVIELED 216
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLD-------IETL--EALEEALDDfpgtvLLVSHDRYFLDrVATRILEFED 504
|
....*
gi 447152655 217 GKITD 221
Cdd:COG0488 505 GGVRE 509
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
121-211 |
1.13e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 121 RAIQLLKNIGLEDRLNV---YPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIM 197
Cdd:PRK15093 135 RAIELLHRVGIKDHKDAmrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILL 214
|
90
....*....|....*
gi 447152655 198 ITHD-RRLFEYADRV 211
Cdd:PRK15093 215 ISHDlQMLSQWADKI 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-221 |
2.18e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 11 NFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDK---QHRPSDLRLEDIGF 87
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRsifNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 88 IFQSSHlvPYLKVIEQLTLVGQEAGMTKQQSSTRAIQL--LKNIGL----EDRLNVYPHQLSGGEKQRVAIMRAFMNNPK 161
Cdd:PRK14271 106 LFQRPN--PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQarLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 162 IILADEPTASLDADRATKVVEMIRQQikEQQMIGIMITHD-RRLFEYADRVIELEDGKITD 221
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNlAQAARISDRAALFFDGRLVE 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-219 |
3.68e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQ--TSGTVLYNDAPLFDKQhrPSDLRLEDIG 86
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYkiLEGDILFKGESILDLE--PEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLE-DRLNVYPHQL--------SGGEKQRVAIMRAFM 157
Cdd:CHL00131 88 LAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKlKLVGMDPSFLsrnvnegfSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 158 NNPKIILADEPTASLDADrATKVVEMIRQQIKEQQMIGIMITHDRRLFEY--ADRVIELEDGKI 219
Cdd:CHL00131 168 LDSELAILDETDSGLDID-ALKIIAEGINKLMTSENSIILITHYQRLLDYikPDYVHVMQNGKI 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-219 |
4.24e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRlEDIGFIFQS-SHLVP 96
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALR-QQVATVFQDpEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEdRLNVYPHQ-LSGGEKQRVAIMRAFMNNPKIILADEPTASLDAD 175
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-HFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447152655 176 RATKVVEMIRQQIKEQQMIgIMITHDRRL-FEYADRVIELEDGKI 219
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHV-IISSHDIDLiYEISDAVYVLRQGQI 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-219 |
6.79e-11 |
|
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: 59.35 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGLSEtkVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDaplfdkqhrpsdlrlED 84
Cdd:cd03369 9 VENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG---------------ID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGfifqsshLVPYLKVIEQLTLVGQEAGMTkqqSSTRAIQLlknigleDRLNVYPHQ--------------LSGGEKQRV 150
Cdd:cd03369 72 IS-------TIPLEDLRSSLTIIPQDPTLF---SGTIRSNL-------DPFDEYSDEeiygalrvsegglnLSQGQRQLL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 151 AIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTI--LTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-200 |
7.07e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.50 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 13 GEGLS----ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRpsdlrlEDIGFI 88
Cdd:PRK13539 5 GEDLAcvrgGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA------EACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 89 FQSSHLVPYLKVIEQLTLVGQEAGmtkqQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEP 168
Cdd:PRK13539 79 GHRNAMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 447152655 169 TASLDADRATKVVEMIRQQIKEQQMIgIMITH 200
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIV-IAATH 185
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
142-219 |
1.07e-10 |
|
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: 60.60 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDadraTKVVEMIRQQIKE--QQMIGIMITHdrRL--FEYADRVIELEDG 217
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD----SRTERAIQAALREvaRGRTTLVIAH--RLstIVDADEILVLEAG 568
|
..
gi 447152655 218 KI 219
Cdd:COG5265 569 RI 570
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-219 |
1.13e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.36 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYnDAPLFDKQHRPSdLRlEDIGFIFQSSHLvpYLKVI 101
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-DGTDIRTVTRAS-LR-RNIAVVFQDAGL--FNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 EQLTLVGQ----EAGMTKQQSSTRAIQLL--KNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAD 175
Cdd:PRK13657 426 EDNIRVGRpdatDEEMRAAAERAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447152655 176 RATKVVEMIrqqikEQQMIG---IMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK13657 506 TEAKVKAAL-----DELMKGrttFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-220 |
1.58e-10 |
|
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: 58.70 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTV--LYNDAPLFdkqhrpsdlrleDIGFIFQsshlvPYL 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvRGRVSSLL------------GLGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 99 KVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRAT 178
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447152655 179 KVVEMIRQQIKeQQMIGIMITHDRRLF-EYADRVIELEDGKIT 220
Cdd:cd03220 180 KCQRRLRELLK-QGKTVILVSHDPSSIkRLCDRALVLEKGKIR 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-218 |
1.60e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 7 DIVKNFGeGLsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTilggllsqtsgtVL--------YNDAPLFDKQHRP- 77
Cdd:NF040905 6 GITKTFP-GV---KALDDVNLSVREGEIHALCGENGAGKSTLMK------------VLsgvyphgsYEGEILFDGEVCRf 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 SDLRL-EDIGF--IFQSSHLVPYLKVIEQLTLvGQEAG----MTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRV 150
Cdd:NF040905 70 KDIRDsEALGIviIHQELALIPYLSIAENIFL-GNERAkrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 151 AIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHdrRLFE---YADRVIELEDGK 218
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLL-ELKAQGITSIIISH--KLNEirrVADSITVLRDGR 216
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-215 |
2.34e-10 |
|
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: 58.00 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 141 QLSGGEKQ------RVAIMRAFMNNPKIILADEPTASLDADR-ATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIE 213
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYR 194
|
..
gi 447152655 214 LE 215
Cdd:cd03240 195 VE 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-214 |
2.79e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLR-LEDIGfifqssHLV- 95
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEYHQdLLYLG------HQPg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 96 --PYLKVIEQLTLVGQEAGMTKQQsstRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLD 173
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447152655 174 ADrATKVVEMIRQQIKEQQMIGIMITHdRRLFEYADRVIEL 214
Cdd:PRK13538 162 KQ-GVARLEALLAQHAEQGGMVILTTH-QDLPVASDKVRKL 200
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-221 |
2.81e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 22 LKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQhrPSDLRlEDIGFIFQSSHLVPYlkvi 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--PEDYR-KLFSAVFTDFHLFDQ---- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 eqltLVGQEagmtKQQSSTRAIQL-LKNIGLEDRLNVYPH-----QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAD 175
Cdd:PRK10522 412 ----LLGPE----GKPANPALVEKwLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447152655 176 RATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-217 |
2.90e-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: 57.73 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 11 NFGEGLSetkVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLE-DIGFIF 89
Cdd:cd03290 9 SWGSGLA---TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 90 QSSHLVPylKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGL-----EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:cd03290 86 QKPWLLN--ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447152655 165 ADEPTASLDADRATKVV-EMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDG 217
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-200 |
3.30e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 5 VEDIVKNFGEGLS--ETKVLKGINFEVEQGEFVILNGASGSGKttlltilggllsqtsgTVLyndaplfdkqhrpsdLRL 82
Cdd:COG2401 27 VAIVLEAFGVELRvvERYVLRDLNLEIEPGEIVLIVGASGSGK----------------STL---------------LRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 83 ---EDIGFIFQSSHLVPYLKVIEQLTLVGQeagMTKQQSSTRAIQLLKNIGLEDrlnVY-----PHQLSGGEKQRVAIMR 154
Cdd:COG2401 76 lagALKGTPVAGCVDVPDNQFGREASLIDA---IGRKGDFKDAVELLNAVGLSD---AVlwlrrFKELSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447152655 155 AFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITH 200
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-220 |
4.88e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.72 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 8 IVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKqhrpSDLRL-EDIG 86
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML----SSRQLaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQsSHLVPY-LKVIE--------QLTLVGQEAGmTKQQSSTRAIQLLKNIGLEDRLnvyPHQLSGGEKQRVAIMRAFM 157
Cdd:PRK11231 80 LLPQ-HHLTPEgITVRElvaygrspWLSLWGRLSA-EDNARVNQAMEQTRINHLADRR---LTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 158 NNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKIT 220
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDlNQASRYCDHLVVLANGHVM 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-219 |
6.90e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDkqHRPSDLRlEDIGFIFQSSHLvpY 97
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD--YTLASLR-NQVALVSQNVHL--F 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGQEAGMTKQQSSTRA--------IQLLKNiGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPT 169
Cdd:PRK11176 430 NDTIANNIAYARTEQYSREQIEEAArmayamdfINKMDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447152655 170 ASLD--ADRAtkvvemIRQQIKEQQ--MIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PRK11176 509 SALDteSERA------IQAALDELQknRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
142-202 |
7.53e-10 |
|
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: 58.02 E-value: 7.53e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRatkvVEMIRQQIKEQQMIGIMITHDR 202
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHDR 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
136-212 |
9.38e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 136 NVYPH--QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADrATKVVEMIRQQIKEQ-QMIGIMITHDRRLFEYADRVI 212
Cdd:PTZ00265 1351 NVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKaDKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-191 |
1.01e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVlyndapLFDKQHRPSDLRLEDIGFIFQSSHLVP 96
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI------QIDGKTATRGDRSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKVIEQLTLVGQEAGMTKQQSSTRAIQLlknIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADR 176
Cdd:PRK13543 96 DLSTLENLHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170
....*....|....*
gi 447152655 177 ATKVVEMIRQQIKEQ 191
Cdd:PRK13543 173 ITLVNRMISAHLRGG 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-205 |
2.50e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqHRPSDLRLEDIGFIFQSSHLVPYLKVIEQL 104
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 105 TLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLD----------- 173
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpysrrsiwdll 1104
|
170 180 190
....*....|....*....|....*....|....*
gi 447152655 174 -ADRATKVVEMIRQQIKEQQMIG--IMITHDRRLF 205
Cdd:TIGR01257 1105 lKYRSGRTIIMSTHHMDEADLLGdrIAIISQGRLY 1139
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
124-215 |
4.69e-09 |
|
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: 54.72 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 124 QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRR 203
Cdd:cd03237 98 EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDII 177
|
90
....*....|...
gi 447152655 204 LFEY-ADRVIELE 215
Cdd:cd03237 178 MIDYlADRLIVFE 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
142-219 |
5.51e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEKQRVAIMRAF---------MNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRV 211
Cdd:PRK13547 146 LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRI 225
|
....*...
gi 447152655 212 IELEDGKI 219
Cdd:PRK13547 226 AMLADGAI 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-219 |
8.99e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 15 GLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDLRLEDIGFIFQSShL 94
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI---QHYASKEVARRIGLLAQNA-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VPYLKVIEQLTLVGQEAGMT-----KQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPT 169
Cdd:PRK10253 92 TPGDITVQELVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447152655 170 ASLDADRATKVVEMIRQQIKEQQMIGIMITHD-RRLFEYADRVIELEDGKI 219
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
123-214 |
1.82e-08 |
|
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: 52.33 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 123 IQLLKNIGLED-RLNVYPHQLSGGEKQRVAIMRAFMNNPK--IILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMIT 199
Cdd:cd03238 68 LQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTV-ILIE 146
|
90
....*....|....*
gi 447152655 200 HDRRLFEYADRVIEL 214
Cdd:cd03238 147 HNLDVLSSADWIIDF 161
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-215 |
2.50e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.80 E-value: 2.50e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEY-ADRVIELE 215
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
117-220 |
3.08e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 117 QSSTRAIQLLKNIGL--EDRLNvyphQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADratkVVEMIRQQIKEQQMI 194
Cdd:PRK11147 134 QLENRINEVLAQLGLdpDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGS 205
|
90 100
....*....|....*....|....*..
gi 447152655 195 GIMITHDRRLFE-YADRVIELEDGKIT 220
Cdd:PRK11147 206 IIFISHDRSFIRnMATRIVDLDRGKLV 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-218 |
4.00e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPL-FDKqhrPSDLRLEDIGFIFQSSHLVPYL 98
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtFNG---PKSSQEAGIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 99 KVIEQLTLvGQE-----AGMTKQQSSTRAIQLLKnigledRLNV--YPHQLSG----GEKQRVAIMRAFMNNPKIILADE 167
Cdd:PRK10762 95 TIAENIFL-GREfvnrfGRIDWKKMYAEADKLLA------RLNLrfSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447152655 168 PTASLdADRATKVVEMIRQQIKEQQmIGIM-ITHD-RRLFEYADRVIELEDGK 218
Cdd:PRK10762 168 PTDAL-TDTETESLFRVIRELKSQG-RGIVyISHRlKEIFEICDDVTVFRDGQ 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
142-202 |
5.80e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 5.80e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRatkvVEMIRQQIKEQQMIGIMITHDR 202
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDYPGTVVAVTHDR 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
124-212 |
7.20e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 124 QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRR 203
Cdd:PRK13409 436 EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIY 515
|
90
....*....|
gi 447152655 204 LFEY-ADRVI 212
Cdd:PRK13409 516 MIDYiSDRLM 525
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
142-215 |
7.78e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEKQ------RVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIG--IMITHDRRLFEYADRVIE 213
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIPqvIMISHHRELLSVADVAYE 881
|
..
gi 447152655 214 LE 215
Cdd:PRK01156 882 VK 883
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-219 |
9.68e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 31 QGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRpsdlrlediGFIFQSSHLVPYLKVIEQLTL---- 106
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---------AFARKVAYLPQQLPAAEGMTVrelv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 107 -VGQ--------EAGMTKQQSSTRAIQLlknIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRA 177
Cdd:PRK10575 107 aIGRypwhgalgRFGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447152655 178 TKVVEMIRQQIKEQQMIGIMITHDRRL-FEYADRVIELEDGKI 219
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEM 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
1.93e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHrpsdlrlediGFIFQSShlvp 96
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQ----------AWIQNDS---- 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 ylkvIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGL---EDRLNVYPH--QLSGGEKQRVAIMRAFMNNPKIILADEPTAS 171
Cdd:TIGR00957 715 ----LRENILFGKALNEKYYQQVLEACALLPDLEIlpsGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447152655 172 LDADRATKVVEMIrqqIKEQQMIG----IMITHDRRLFEYADRVIELEDGKITD 221
Cdd:TIGR00957 791 VDAHVGKHIFEHV---IGPEGVLKnktrILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-219 |
2.52e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 18 ETKVL-KGINFEVEQGEFVILNGASGSGKttlltilggllSQTSGTVLYNdaplFDKQHrpsdlrlediGFIF--QSSHL 94
Cdd:PTZ00243 671 EPKVLlRDVSVSVPRGKLTVVLGATGSGK-----------STLLQSLLSQ----FEISE----------GRVWaeRSIAY 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 95 VPYLKVIEQLTLVGQ-----EAGMTKQQSSTRAIQLLKNI-----GLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIIL 164
Cdd:PTZ00243 726 VPQQAWIMNATVRGNilffdEEDAARLADAVRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 165 ADEPTASLDADRATKVV-EMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVeECFLGALAGKTR--VLATHQVHVVPRADYVVALGDGRV 859
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
125-207 |
3.16e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 125 LLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRL 204
Cdd:cd03236 123 LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAV 201
|
...
gi 447152655 205 FEY 207
Cdd:cd03236 202 LDY 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-221 |
3.19e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.18 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 25 INFEVEQGEFVILNGASGSGKttlltilggllS-----------QTSGTVLYNDAPLfDKQHRPSDLRLedigF--IFQS 91
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGK-----------StlaklltglyrPESGEILLDGQPV-TADNREAYRQL----FsaVFSD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 92 SHLVPYLkvieqltlvgqeAGMTKQQSSTRAIQLLKNIGLEDRLNVYPH-----QLSGGEKQRVAIMRAFMNNPKIILAD 166
Cdd:COG4615 415 FHLFDRL------------LGLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFD 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 167 EPTAslDAD---RA---TKVVEMIRQQikeqqmiG---IMITHDRRLFEYADRVIELEDGKITD 221
Cdd:COG4615 483 EWAA--DQDpefRRvfyTELLPELKAR-------GktvIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-221 |
3.29e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTS-------GTVLYndAP----LFDKQHRPSDLrledI 85
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVAY--VPqvswIFNATVRENIL----F 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 86 GFIFQSSHlvpYLKVIEQLTLvgqeagmtKQQSSTRAIQLLKNIGlEDRLNVyphqlSGGEKQRVAIMRAFMNNPKIILA 165
Cdd:PLN03232 702 GSDFESER---YWRAIDVTAL--------QHDLDLLPGRDLTEIG-ERGVNI-----SGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 166 DEPTASLDADRATKVVE-MIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKITD 221
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDsCMKDELKGKTR--VLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-221 |
5.02e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDI-VKNFGEGLsetkVLKGINFEVEQGEFVILNGASGSGkttlltilggllsQT-------------SGTVLYND 67
Cdd:COG3845 257 VLEVENLsVRDDRGVP----ALKDVSLEVRAGEILGIAGVAGNG-------------QSelaealaglrppaSGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 68 APLFDKqhRPSDLRLEDIGFIFQSSH---LVPYLKVIEQLTLVGQEagmtKQQSSTRAIQLLKNI-----GLEDRLNVYP 139
Cdd:COG3845 320 EDITGL--SPRERRRLGVAYIPEDRLgrgLVPDMSVAENLILGRYR----RPPFSRGGFLDRKAIrafaeELIEEFDVRT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 140 H-------QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAdRATkvvEMIRQQIKEQQMIG---IMITHD-RRLFEYA 208
Cdd:COG3845 394 PgpdtparSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV-GAI---EFIHQRLLELRDAGaavLLISEDlDEILALS 469
|
250
....*....|...
gi 447152655 209 DRVIELEDGKITD 221
Cdd:COG3845 470 DRIAVMYEGRIVG 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
124-212 |
6.37e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.40 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 124 QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRR 203
Cdd:COG1245 438 EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIY 517
|
90
....*....|
gi 447152655 204 LFEY-ADRVI 212
Cdd:COG1245 518 LIDYiSDRLM 527
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
126-220 |
7.29e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 126 LKNIGLEDRLNVYP-HQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADratkVVEMIRQQIKEQQMIGIMITHDRRL 204
Cdd:PLN03073 611 LGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD----AVEALIQGLVLFQGGVLMVSHDEHL 686
|
90
....*....|....*..
gi 447152655 205 FE-YADRVIELEDGKIT 220
Cdd:PLN03073 687 ISgSVDELWVVSEGKVT 703
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
142-220 |
7.39e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIrQQIKEQQMIGIMITHDR-RLFEYADRVIELEDGKIT 220
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRIS 474
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
142-221 |
8.65e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRRLFE-YADRVIELEDGKIT 220
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIR-SIAAQNVAVLFISSDLEEIEqMADRVLVMHQGEIS 482
|
.
gi 447152655 221 D 221
Cdd:PRK15439 483 G 483
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-187 |
1.07e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.56 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHrpSDLRlEDIGFIfQSSHLVPYLKV 100
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH--SVLR-QGVAMV-QQDPVVLADTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 101 IEQLTLvGQEAGMTKQQSSTRAIQLLKNI-----GLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDA- 174
Cdd:PRK10790 432 LANVTL-GRDISEEQVWQALETVQLAELArslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSg 510
|
170
....*....|....*
gi 447152655 175 -DRAT-KVVEMIRQQ 187
Cdd:PRK10790 511 tEQAIqQALAAVREH 525
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-219 |
1.11e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTS-------GTVLYndAP----LFDKQHRPSDLrledI 85
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvirGTVAY--VPqvswIFNATVRDNIL----F 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 86 GFIFQSSHlvpYLKVIEQLTLvgqeagmtkqqssTRAIQLL-----KNIGlEDRLNVyphqlSGGEKQRVAIMRAFMNNP 160
Cdd:PLN03130 702 GSPFDPER---YERAIDVTAL-------------QHDLDLLpggdlTEIG-ERGVNI-----SGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 161 KIILADEPTASLDADRATKVVEM-IRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTR--VLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-219 |
1.16e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 102 EQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVV 181
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110
....*....|....*....|....*....|....*...
gi 447152655 182 EMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:NF000106 185 DEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-221 |
1.17e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 1 MALVVEDIVKNFGEGlsetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfdkqhrpsdl 80
Cdd:PRK15064 318 NALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN------------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 81 rlEDIGFIFQ-SSHLVPylkviEQLTL---VGQEAGMTKQQSSTRAI--QLLKNiglEDRLNVYPHQLSGGEKQRVAIMR 154
Cdd:PRK15064 382 --ANIGYYAQdHAYDFE-----NDLTLfdwMSQWRQEGDDEQAVRGTlgRLLFS---QDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 155 AFMNNPKIILADEPTASLDADRatkvVEMIRQQIKEQQMIGIMITHDRrlfEY----ADRVIELEDGKITD 221
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDR---EFvsslATRIIEITPDGVVD 515
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-204 |
1.65e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVlyndapLFDKQHRPSDLRL--EDIGFIFQSSHLVPYL 98
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI------LFERQSIKKDLCTyqKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 99 KVIEQLTLvgqeaGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDaDRAt 178
Cdd:PRK13540 90 TLRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELS- 162
|
170 180
....*....|....*....|....*...
gi 447152655 179 kvVEMIRQQIKEQQMIG--IMITHDRRL 204
Cdd:PRK13540 163 --LLTIITKIQEHRAKGgaVLLTSHQDL 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-218 |
2.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEkqRVAIMRAFM---------NNPKIILaDEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFEYADRVI 212
Cdd:PRK03918 789 LSGGE--RIALGLAFRlalslylagNIPLLIL-DEPTPFLDEERRRKLVDIMERYLRKIPQV-IIVSHDEELKDAADYVI 864
|
....*...
gi 447152655 213 --ELEDGK 218
Cdd:PRK03918 865 rvSLEGGV 872
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
32-214 |
2.18e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 32 GEFVILNGASGSGKttlltilggllsqtsgtvlyndaplfdkqhrpSDLrLEDIGFIF--QSSHLVPYLKVieqltlvgq 109
Cdd:cd03227 21 GSLTIITGPNGSGK--------------------------------STI-LDAIGLALggAQSATRRRSGV--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 110 EAGMTKQQSSTRAIQLLknigledrlnvypHQLSGGEKQRVAI-----MRAFMNNPKIILaDEPTASLDADRATKVVEMI 184
Cdd:cd03227 59 KAGCIVAAVSAELIFTR-------------LQLSGGEKELSALalilaLASLKPRPLYIL-DEIDRGLDPRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|
gi 447152655 185 RQQIKEQQMiGIMITHDRRLFEYADRVIEL 214
Cdd:cd03227 125 LEHLVKGAQ-VIVITHLPELAELADKLIHI 153
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
140-212 |
3.01e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.30 E-value: 3.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 140 HQLSGGEKQRVA---IMRAFMNNPK-IILADEPTASLDADRATKVVEMIRQQIKEQQMIgiMITHDRRLFEYADRVI 212
Cdd:cd03278 112 SLLSGGEKALTAlalLFAIFRVRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFI--VITHRKGTMEAADRLY 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-201 |
6.05e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.91 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 11 NFGEGlsETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLyndaplFDKQHRP--SDLRL----ED 84
Cdd:PRK11831 14 SFTRG--NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIL------FDGENIPamSRSRLytvrKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 85 IGFIFQSSHLVPYLKVIEQLTLVGQE-AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKII 163
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 447152655 164 LADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD 201
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-217 |
8.14e-06 |
|
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: 44.93 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTT--LLTILGGLLSQTSGTVLYNDAPLfDKQHRPSdlrledIGFIFQSSHLVPY 97
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTllDVLAGRKTAGVITGEILINGRPL-DKNFQRS------TGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGqeagmtkqqsstraiqLLKNIGLEDRlnvyphqlsggekQRVAIMRAFMNNPKIILADEPTASLDADRA 177
Cdd:cd03232 94 LTVREALRFSA----------------LLRGLSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447152655 178 TKVVEMIRQQIKEQQMIGIMItH--DRRLFEYADRVIELEDG 217
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTI-HqpSASIFEKFDRLLLLKRG 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-217 |
8.41e-06 |
|
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: 46.06 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 19 TKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfdkqhrpsdlrledIGFIFQSSHLVPyl 98
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----------------ISFSPQTSWIMP-- 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 99 KVIEQLTLVGQEAGMTKQQSSTRAIQllknigLEDRLNVYPHQ-----------LSGGEKQRVAIMRAFMNNPKIILADE 167
Cdd:TIGR01271 501 GTIKDNIIFGLSYDEYRYTSVIKACQ------LEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447152655 168 PTASLDADRATKVVEMIRQQIKEQQMiGIMITHDRRLFEYADRVIELEDG 217
Cdd:TIGR01271 575 PFTHLDVVTEKEIFESCLCKLMSNKT-RILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-194 |
8.55e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.86 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 17 SETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqhrpSDLRLEDIGFIFQSSHLVP 96
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL-------TKLQLDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YL---KVIEQLTLVGQEAgmTKQQSSTRAiqLLKNIGlEDRLNV---YPHQ-------LSGGEKQRVAIMRAFMNNPKII 163
Cdd:PRK10789 399 FLfsdTVANNIALGRPDA--TQQEIEHVA--RLASVH-DDILRLpqgYDTEvgergvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190
....*....|....*....|....*....|.
gi 447152655 164 LADEPTASLDADRATKVVEMIRQQIKEQQMI 194
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVI 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-212 |
1.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 142 LSGGEKQRVAIMRAF---MNNPKIILA-DEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVI 212
Cdd:TIGR02169 1075 MSGGEKSLTALSFIFaiqRYKPSPFYAfDEVDMFLDGVNVERVAKLIREKAGEAQF--IVVSLRSPMIEYADRAI 1147
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-219 |
1.35e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 9 VKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQ--TSGTVLYNDAPLFDKQhrPSDLRLEDIG 86
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELS--PEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 87 FIFQSSHLVPylKVIEQL---TLVGQEAGMTKQQSSTR---------AIQLLKNIG--LEDRLNVyphQLSGGEKQRVAI 152
Cdd:PRK09580 82 MAFQYPVEIP--GVSNQFflqTALNAVRSYRGQEPLDRfdfqdlmeeKIALLKMPEdlLTRSVNV---GFSGGEKKRNDI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 153 MRAFMNNPKIILADEPTASLDADrATKVVEMIRQQIKEQQMIGIMITHDRRLFEY--ADRVIELEDGKI 219
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDID-ALKIVADGVNSLRDGKRSFIIVTHYQRILDYikPDYVHVLYQGRI 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-217 |
1.84e-05 |
|
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: 44.46 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 19 TKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAplfdkqhrpsdlrledIGFIFQSSHLVPyl 98
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----------------ISFSSQFSWIMP-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 99 KVIEQLTLVGQEAGMTKQQSSTRAIQllknigLEDRLNVYPHQ-----------LSGGEKQRVAIMRAFMNNPKIILADE 167
Cdd:cd03291 112 GTIKENIIFGVSYDEYRYKSVVKACQ------LEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447152655 168 PTASLDADRATKVVEMIRQQIKEQQMiGIMITHDRRLFEYADRVIELEDG 217
Cdd:cd03291 186 PFGYLDVFTEKEIFESCVCKLMANKT-RILVTSKMEHLKKADKILILHEG 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-186 |
2.06e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.10 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 2 ALVVEDIVKNFGEGLSetkVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkqhrPSDLR 81
Cdd:PRK15056 6 GIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT------RQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 82 LEDIGFIFQSSHL---VPYLkvIEQLTLVGQEAGM-----TKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIM 153
Cdd:PRK15056 77 KNLVAYVPQSEEVdwsFPVL--VEDVVMMGRYGHMgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190
....*....|....*....|....*....|...
gi 447152655 154 RAFMNNPKIILADEPTASLDADRATKVVEMIRQ 186
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-219 |
3.82e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.15 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 6 EDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYND--APLFdkqhrpsdlrle 83
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSALL------------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 84 DIGFIFQsshlvPYLKVIEQLTLVGQEAGMTKQQssTRAiqLLKNI----GLEDRLNVYPHQLSGGEKQRV--AIMRAFm 157
Cdd:COG1134 94 ELGAGFH-----PELTGRENIYLNGRLLGLSRKE--IDE--KFDEIvefaELGDFIDQPVKTYSSGMRARLafAVATAV- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447152655 158 nNPKIILADEPTASLDADRATKVVEMIRqQIKEQQMIGIMITHDRRLF-EYADRVIELEDGKI 219
Cdd:COG1134 164 -DPDILLVDEVLAVGDAAFQKKCLARIR-ELRESGRTVIFVSHSMGAVrRLCDRAIWLEKGRL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-220 |
3.96e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.85 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 14 EGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRLEDIGFI---FQ 90
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV--RIRSPRDAIRAGIAYVpedRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 91 SSHLVPYLKVIEQLTLVGQEAGMTK--------QQSSTRAIQLLkNI---GLEDRLNvyphQLSGGEKQRVAIMRAFMNN 159
Cdd:COG1129 338 GEGLVLDLSIRENITLASLDRLSRGglldrrreRALAEEYIKRL-RIktpSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 160 PKIILADEPTASLDAdrATK--VVEMIRQQIKEqqmiG---IMITHD-RRLFEYADRVIELEDGKIT 220
Cdd:COG1129 413 PKVLILDEPTRGIDV--GAKaeIYRLIRELAAE----GkavIVISSElPELLGLSDRILVMREGRIV 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-219 |
6.08e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 6 EDIVKNFGEGLSetKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdKQHRPSDLRlEDI 85
Cdd:PLN03232 1238 EDVHLRYRPGLP--PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--AKFGLTDLR-RVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 86 GFIFQSSHLV---------PYLKvieqltlvGQEAGMTKQQSSTRAIQLLKN--IGLEDRLNVYPHQLSGGEKQRVAIMR 154
Cdd:PLN03232 1313 SIIPQSPVLFsgtvrfnidPFSE--------HNDADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447152655 155 AFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVIELEDGKI 219
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
141-220 |
6.94e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 141 QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDrrLFE---YADRVIELEDG 217
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAI-IVISSE--LPEvlgLSDRVLVMHEG 481
|
...
gi 447152655 218 KIT 220
Cdd:PRK13549 482 KLK 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
98-219 |
7.70e-05 |
|
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: 42.89 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 98 LKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVypHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRA 177
Cdd:TIGR02633 362 LSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI--GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 447152655 178 TKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKI 219
Cdd:TIGR02633 440 YEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-217 |
7.98e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 7.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 142 LSGGEKQRVAIMR---AFMNNPKIILaDEPTASLDADRATKVVEMIrQQIKEQQMIGIMITHDRRLFEYADRVIELEDG 217
Cdd:PRK00635 477 LSGGEQERTALAKhlgAELIGITYIL-DEPSIGLHPQDTHKLINVI-KKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
143-219 |
8.79e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 8.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 143 SGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHD--RRLFEYADRVIELEDGKI 219
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQcsQDAYELFDKVIVLYEGYQ 289
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-173 |
9.08e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.53 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLS-----QTSGtVLYNDAPLfdKQHRP 77
Cdd:cd03289 3 MTVKDLTAKYTEG--GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNtegdiQIDG-VSWNSVPL--QKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 SDLRLEDIGFIFQSS---HLVPYLK-VIEQLTLVGQEAGMtKQQSSTRAIQLlkNIGLEDRLNVyphqLSGGEKQRVAIM 153
Cdd:cd03289 78 AFGVIPQKVFIFSGTfrkNLDPYGKwSDEEIWKVAEEVGL-KSVIEQFPGQL--DFVLVDGGCV----LSHGHKQLMCLA 150
|
170 180
....*....|....*....|
gi 447152655 154 RAFMNNPKIILADEPTASLD 173
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLD 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
124-201 |
1.01e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 1.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 124 QLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHD 201
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYV--LVVEHD 270
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-218 |
1.22e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 20 KVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLfdkQHRPSDLRLED-IGFIFQSSHLVPYL 98
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFKSSKEALENgISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 99 KVIEQLTL-----VGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVypHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLD 173
Cdd:PRK10982 89 SVMDNMWLgryptKGMFVDQDKMYRDTKAIFDELDIDIDPRAKV--ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447152655 174 ADRATKVVEMIRqQIKEQQMIGIMITHD-RRLFEYADRVIELEDGK 218
Cdd:PRK10982 167 EKEVNHLFTIIR-KLKERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
142-218 |
1.29e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.43 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADratkVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELeDGK 218
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYM-DGR 654
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-220 |
1.57e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDR-RLFEYADRVIELEDGKIT 220
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGI-IIISSEMpELLGITDRILVMSNGLVA 470
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-214 |
1.61e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 121 RAIQLLKNIGLED-RLNVYPHQLSGGEKQRVAIMRAFM---NNPKIILADEPTASLDADRATKVVEMIrQQIKEQQMIGI 196
Cdd:TIGR00630 808 RKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVL-QRLVDKGNTVV 886
|
90
....*....|....*...
gi 447152655 197 MITHDRRLFEYADRVIEL 214
Cdd:TIGR00630 887 VIEHNLDVIKTADYIIDL 904
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
141-212 |
3.71e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 3.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447152655 141 QLSGGEKQRVA---IMRAFMNNPK-IILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLFEYADRVI 212
Cdd:pfam02463 1077 LLSGGEKTLVAlalIFAIQKYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQF--IVISLREEMLEKADKLV 1150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
141-201 |
3.83e-04 |
|
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: 40.92 E-value: 3.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 141 QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHD 201
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYV-LVVEHD 271
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-200 |
4.55e-04 |
|
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: 40.77 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 29 VEQGEFVILNGASGSGKTTLLTILGGLLSQTSGtvlynDAPLFDKQhrpsdlRLEDIGFIFQSSHLVPYLKVIEQLtLVG 108
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----DATVAGKS------ILTNISDVHQNMGYCPQFDAIDDL-LTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 109 QE--------AGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKV 180
Cdd:TIGR01257 2030 REhlylyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180
....*....|....*....|
gi 447152655 181 VEMIRQQIKEQQMIgIMITH 200
Cdd:TIGR01257 2110 WNTIVSIIREGRAV-VLTSH 2128
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-221 |
4.86e-04 |
|
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: 40.70 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 21 VLKGINFEVEQGEFVILNGASGSGKTtlltilggllSQTSGTVLYNDAPlfDKQHRPSDLRLEDIGFifqssHLVPYlkv 100
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKS----------SLTLGLFRINESA--EGEIIIDGLNIAKIGL-----HDLRF--- 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 101 ieQLTLVGQEA--------------GMTKQQSSTRAIQL--LKNI--GLEDRLNvypHQ-------LSGGEKQRVAIMRA 155
Cdd:TIGR00957 1361 --KITIIPQDPvlfsgslrmnldpfSQYSDEEVWWALELahLKTFvsALPDKLD---HEcaeggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447152655 156 FMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHdrRLFEYAD--RVIELEDGKITD 221
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTV--LTIAH--RLNTIMDytRVIVLDKGEVAE 1499
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
132-215 |
4.98e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 132 EDRLNVY--------PHQLSGGEKQ------RVAIMR---------AFMnnPKIILaDEPTASLDADRATKVVEMirqqI 188
Cdd:PRK02224 764 EYELTVYqkdgeplePEQLSGGERAlfnlslRCAIYRllaegiegdAPL--PPLIL-DEPTVFLDSGHVSQLVDL----V 836
|
90 100 110
....*....|....*....|....*....|.
gi 447152655 189 KEQQMIG----IMITHDRRLFEYADRVIELE 215
Cdd:PRK02224 837 ESMRRLGveqiVVVSHDDELVGAADDLVRVE 867
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-216 |
4.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 132 EDRLNVYPHQLSGGEK-Q-----RVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMigIMITHDRRLF 205
Cdd:COG4717 549 EDGRTRPVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQV--IYFTCHEELV 626
|
90
....*....|....*
gi 447152655 206 EYAD----RVIELED 216
Cdd:COG4717 627 ELFQeegaHVIELES 641
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-190 |
5.97e-04 |
|
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: 40.66 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 3 LVVEDIVKNFGEGlsETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSqTSGT-----VLYNDAPLfdKQHRP 77
Cdd:TIGR01271 1218 MDVQGLTAKYTEA--GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEiqidgVSWNSVTL--QTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 78 SDLRLEDIGFIFQSS---HLVPYLKVI-EQLTLVGQEAGMtkqQSSTRAIQLLKNIGLEDRLNVyphqLSGGEKQRVAIM 153
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTfrkNLDPYEQWSdEEIWKVAEEVGL---KSVIEQFPDKLDFVLVDGGYV----LSNGHKQLMCLA 1365
|
170 180 190
....*....|....*....|....*....|....*..
gi 447152655 154 RAFMNNPKIILADEPTASLDAdratKVVEMIRQQIKE 190
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDP----VTLQIIRKTLKQ 1398
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
141-220 |
7.21e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 141 QLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKIT 220
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
142-188 |
9.99e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 9.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQI 188
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV 1066
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
97-202 |
1.50e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 97 YLKVIEqltLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYP-HQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAD 175
Cdd:PRK15064 113 GMKVAD---LEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN 189
|
90 100 110
....*....|....*....|....*....|
gi 447152655 176 ratkvveMIR---QQIKEQQMIGIMITHDR 202
Cdd:PRK15064 190 -------TIRwleDVLNERNSTMIIISHDR 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-217 |
2.04e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447152655 142 LSGGEKQRVAIMRAFMNNPK---IILADEPTASLDADRATKVVEMIRQQIKEQQMIgIMITHDRRLFEYADRVIELEDG 217
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSV-IYIDHDPALLKQADYLIEMGPG 1777
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
149-206 |
2.41e-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: 38.49 E-value: 2.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447152655 149 RVAIMRAFMNNPKIILADEPTASLDADR----ATKVVEMIRQQIKEQQMIGIMITHDRRLFE 206
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVE 1274
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-173 |
2.73e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.07 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 16 LSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTvLYNDaplFdkqHRPSDLRLEdigfifQSSHLV 95
Cdd:PRK10938 13 LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQ---F---SHITRLSFE------QLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 96 P---------YLKVIEQLTlvGQEAGMTKQQSS---TRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKII 163
Cdd:PRK10938 80 SdewqrnntdMLSPGEDDT--GRTTAEIIQDEVkdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170
....*....|
gi 447152655 164 LADEPTASLD 173
Cdd:PRK10938 158 ILDEPFDGLD 167
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
116-200 |
3.46e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.07 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 116 QQSSTR----AIQLLKNIGLEDRLNVYP-HQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDAdratkvveMIRQQIKe 190
Cdd:PRK10938 371 QAVSDRqqklAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP--------LNRQLVR- 441
|
90
....*....|
gi 447152655 191 qQMIGIMITH 200
Cdd:PRK10938 442 -RFVDVLISE 450
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
141-209 |
4.68e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 37.17 E-value: 4.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447152655 141 QLSGGEKQRVAI-----MRAFMNNPKIILaDEPTASLDADRATKVVEMIRQQiKEQQMIGIMITHDRRLFEYAD 209
Cdd:cd03275 155 NLSGGEKTMAALallfaIHSYQPAPFFVL-DEVDAALDNTNVGKVASYIREQ-AGPNFQFIVISLKEEFFSKAD 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
120-215 |
5.81e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447152655 120 TRAIQLLKNIGL-EDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADratkVVEMIRQQIKEQQMIGIMI 198
Cdd:PRK10636 127 SRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD----AVIWLEKWLKSYQGTLILI 202
|
90
....*....|....*...
gi 447152655 199 THDRRLFE-YADRVIELE 215
Cdd:PRK10636 203 SHDRDFLDpIVDKIIHIE 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
142-202 |
7.53e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 36.85 E-value: 7.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447152655 142 LSGGEKQRVAIMRAFMNNPKIILADEPTASLDADratkVVEMIRQQIKEQQMIGIMITHDR 202
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE----TLELLEELLDSYQGTVLLVSHDR 497
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
143-213 |
1.00e-02 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 36.64 E-value: 1.00e-02
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447152655 143 SGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGI------MITHDRRLFEYADRVIE 213
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIahrlntIIDCDRILVLDAGRVVE 1452
|
|
| |
