|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-223 |
7.19e-121 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 342.41 E-value: 7.19e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIVG 223
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-221 |
3.74e-106 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 304.80 E-value: 3.74e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQF----FMnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:cd03255 81 RRHIGFVFQSFnllpDL----TALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-222 |
2.35e-93 |
|
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: 273.16 E-value: 2.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKkmALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARAR--ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-222 |
4.16e-85 |
|
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: 251.50 E-value: 4.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-226 |
3.58e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 229.17 E-value: 3.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQF-FMNAKdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:COG2884 78 R-RRIGVVFQDFrLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLAARCD-RQVHVRDGLIVGGDE 226
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPkRVLELEDGRLVRDEA 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-222 |
2.02e-75 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 228.02 E-value: 2.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:COG3638 1 PMLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEeFGFVFQQFFMNAKDTVLNNVLLPLkIGGISGSKR---------KKMALDALKAVGLEDKVQNKANNLSGGQKQRV 152
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVLAGR-LGRTSTWRSllglfppedRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-222 |
1.67e-72 |
|
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: 220.15 E-value: 1.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-212 |
1.02e-70 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 219.18 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQF-FMNAKdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:COG1135 82 -RKIGMIFQHFnLLSSR-TVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDR 212
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDR 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
2.20e-70 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 215.72 E-value: 2.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVln 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 ktrneefGFVFQQF----FMnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIAR 156
Cdd:COG1116 83 -------GVVFQEPallpWL----TVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDR 212
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADR 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-219 |
9.51e-70 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 213.10 E-value: 9.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-222 |
1.67e-68 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 221.52 E-value: 1.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-222 |
5.98e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 208.69 E-value: 5.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsIRKKVLNKT 82
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQF--FMNAkdTVLNNVLL-PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:COG1126 76 R-RKVGMVFQQFnlFPHL--TVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-221 |
6.05e-68 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 208.52 E-value: 6.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 8 NIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEF 87
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 88 GFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFA 167
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286249 168 DEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-222 |
2.20e-66 |
|
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: 204.49 E-value: 2.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTS-----IRKKV 78
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKknlreLRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktrneefGFVFQ----QFFMnakDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:COG1122 78 ---------GLVFQnpddQLFA---PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAElADRVIVLDDGRIV 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
3.17e-65 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 209.76 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYG-KNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRnEEFGFVFQ----QFfmNAKDTVLNNVLLPLKI-GGISGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQKQRVCIA 155
Cdd:COG1123 340 LR-RRVQMVFQdpysSL--NPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRqVHV-RDGLIV 222
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADR-VAVmYDGRIV 484
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-212 |
1.73e-64 |
|
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: 198.61 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 7 KNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEE 86
Cdd:TIGR03608 2 KNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 87 FGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIF 166
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286249 167 ADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLAARCDR 212
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADR 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-222 |
1.85e-64 |
|
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: 200.03 E-value: 1.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVFQQFF--MNAKDTVLNNVLLPLKIGGISGSKRKkmALDALKAVGLEDKVQNK-ANNLSGGQKQRVCIARALVN 160
Cdd:COG1124 81 ---VQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 161 NPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-222 |
1.86e-64 |
|
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: 199.72 E-value: 1.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMNAKDTVLNNVLLPL-----KIGGISG--SKR-KKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIA 155
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVLSGRlgrrsTWRSLFGlfPKEeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
2.14e-64 |
|
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: 198.85 E-value: 2.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVlnktr 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neefGFVFQQF----FMnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:cd03293 76 ----GYVFQQDallpWL----TVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDR 212
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADR 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-219 |
3.23e-64 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 198.12 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIkkSYGKNETKFdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI-----RKKV 78
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppewRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktrneefGFVFQQFFMNAkDTVLNNVLLPLKIGGISGSKRKkmALDALKAVGLEDKVQNK-ANNLSGGQKQRVCIARA 157
Cdd:COG4619 77 ---------AYVPQEPALWG-GTVRDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKpVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-222 |
9.80e-64 |
|
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: 197.73 E-value: 9.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEeFGFVFQQFF--MNAKDTVLNNVLLPLKIGGISGSK--RKKMALDALKAVGLEDKVQNK-ANNLSGGQKQRVCIARA 157
Cdd:cd03257 81 RKE-IQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRqVHV-RDGLIV 222
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADR-VAVmYAGKIV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-219 |
1.05e-63 |
|
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: 196.92 E-value: 1.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 5 EAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtrn 84
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 85 eEFGFVFQ----QFFMnakDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:cd03225 76 -KVGLVFQnpddQFFG---PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 161 NPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-222 |
1.22e-63 |
|
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: 197.89 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:COG1127 4 PMIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRnEEFGFVFQQ---F-FMnakdTVLNNVLLPLKI-GGISGSKRKKMALDALKAVGLEDkVQNKA-NNLSGGQKQRVCIA 155
Cdd:COG1127 80 LR-RRIGMLFQGgalFdSL----TVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPG-AADKMpSELSGGMRKRVALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-222 |
1.20e-62 |
|
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: 195.21 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQFFMNAKDTVLNNVLLPL-----KIGGISG---SKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRlgykpTWRSLLGrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
1.61e-62 |
|
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: 194.32 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALL-----DQPTSGDIYLNGKNVTSIRKKV 78
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 LNKTRneEFGFVFQQFFMNAKdTVLNNVLLPLKIGGISGSK-RKKMALDALKAVGLEDKVQNKAN--NLSGGQKQRVCIA 155
Cdd:cd03260 77 LELRR--RVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEeLDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAARC-DRQVHVRDGLIV 222
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-221 |
2.55e-62 |
|
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: 193.51 E-value: 2.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsIRKKVLNKTR 83
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMNAKDTVLNNVLL-PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLA-ARCDRQVHVRDGLI 221
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-222 |
2.27e-61 |
|
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: 191.19 E-value: 2.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNetkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvlnKTR 83
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------PPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-219 |
2.53e-61 |
|
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: 189.71 E-value: 2.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNetkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeeFGFVFQQFFMNAKDTVLNNVLLPLkiggisgskrkkmaldalkavgledkvqnkannlSGGQKQRVCIARALVNNPQ 163
Cdd:cd03229 77 R--IGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-205 |
5.24e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 191.85 E-value: 5.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI--RKkv 78
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppEK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktRNeeFGFVFQQF----FMnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:COG3842 77 ----RN--VGMVFQDYalfpHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPD 205
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE 197
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-219 |
1.83e-59 |
|
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: 186.30 E-value: 1.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAARCD-RQVHVRDG 219
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAhRVIILDDG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-222 |
1.20e-58 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 188.09 E-value: 1.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:PRK11153 81 R-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-223 |
4.21e-58 |
|
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: 183.47 E-value: 4.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEeFGFVFQQ--FF--MnakdTVLNNVLLPLKI-GGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:cd03261 77 RR-MGMLFQSgaLFdsL----TVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD-PDLAARCDRQVHVRDGLIVG 223
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVA 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-222 |
6.84e-58 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 186.43 E-value: 6.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIR-KKvl 79
Cdd:COG3839 1 MASLELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPpKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 nktRNeeFGFVFQQF----FMnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIA 155
Cdd:COG3839 75 ---RN--IAMVFQSYalypHM----TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPD----LAarcDRQVHVRDGLIV 222
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeamtLA---DRIAVMNDGRIQ 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-212 |
5.41e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.64 E-value: 5.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLnktr 83
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDR 212
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERlCDR 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-221 |
1.04e-56 |
|
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: 179.14 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:cd03292 1 IEFINVTKTYPNGTA---ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAARCDRQV-HVRDGLI 221
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRViALERGKL 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
1.59e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 179.90 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLdQPTSGDIYLNGKNVTSIRKKVl 79
Cdd:COG1121 4 MPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPPRRARRRI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 nktrneefGFVFQQ------FFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVC 153
Cdd:COG1121 78 --------GYVPQRaevdwdFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 154 IARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDRQVHVRDGLIVGGD 225
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGP 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-212 |
3.72e-56 |
|
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: 181.02 E-value: 3.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLDQP--TSGDIYLNGKNVTSIRKKVL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 NKTRNEEFGFVFQqffmnakD--TVLNNVL-------LPLKI-GGISGSKRKKMALDALKAVGLEDKVQnKANN----LS 145
Cdd:COG0444 81 RKIRGREIQMIFQ-------DpmTSLNPVMtvgdqiaEPLRIhGGLSKAEARERAIELLERVGLPDPER-RLDRypheLS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 146 GGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDR 212
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADR 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-222 |
1.32e-55 |
|
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: 184.72 E-value: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETkfDALKGVDLKVEKGESVAIIGKSGSGKSTF-MHILALLDQP--TSGDIYLNGKNVTSIRKKV 78
Cdd:COG1123 3 PLLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGgrISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktRNEEFGFVFQQFfMNAKD--TVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIAR 156
Cdd:COG1123 81 ----RGRRIGMVFQDP-MTQLNpvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIV 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-222 |
2.48e-55 |
|
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: 177.45 E-value: 2.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKN-ETKFDALKG-------------------VDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGD 63
Cdd:cd03294 1 IKIKGLYKIFGKNpQKAFKLLAKgkskeeilkktgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 64 IYLNGKNVTSIRKKVLNKTRNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANN 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 144 LSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARC-DRQVHVRDGLIV 222
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLV 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
4.99e-54 |
|
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: 183.88 E-value: 4.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLnktR 83
Cdd:COG2274 474 IELENVSFRYPGDSP--PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---R 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEeFGFVFQQ-FFMNakDTVLNNVLL--PlkigGISgskrKKMALDALKAVGLEDKVQN-----------KANNLSGGQK 149
Cdd:COG2274 549 RQ-IGVVLQDvFLFS--GTIRENITLgdP----DAT----DEEIIEAARLAGLHDFIEAlpmgydtvvgeGGSNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-222 |
9.43e-54 |
|
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: 172.92 E-value: 9.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RneefGFVFQQFFMNAKDTVLNNVLL---P-LKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:COG1120 77 I----AYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 159 VNNPQIIFADEPTGNLDsaTGKKIE--ELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG1120 153 AQEPPLLLLDEPTSHLD--LAHQLEvlELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIV 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-222 |
1.37e-53 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 175.34 E-value: 1.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsIRKKVlnKTR 83
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPP--RER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeeFGFVFQQF----FMnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:COG1118 76 R--VGFVFQHYalfpHM----TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-222 |
1.45e-53 |
|
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: 171.36 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQFFMNAKDTVLNNVLLPLKI-GGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-219 |
1.33e-52 |
|
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: 167.17 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVFQQFFMnAKDTVLNNVLlplkiggisgskrkkmaldalkavgledkvqnkannlSGGQKQRVCIARALVNNPQ 163
Cdd:cd03228 78 ---IAYVPQDPFL-FSGTIRENIL-------------------------------------SGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-212 |
1.54e-52 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 169.83 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTF------MHILalldQP---TSGDIYLNGKN-- 70
Cdd:COG1117 10 PKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDL----IPgarVEGEILLDGEDiy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 71 -----VTSIRKKVlnktrneefGFVFQQ---FFMnakdTVLNNVLLPLKIGGIsgskRKKMALD-----ALKAVGLEDKV 137
Cdd:COG1117 82 dpdvdVVELRRRV---------GMVFQKpnpFPK----SIYDNVAYGLRLHGI----KSKSELDeiveeSLRKAALWDEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 138 QNK----ANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAARC-DR 212
Cdd:COG1117 145 KDRlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVsDY 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
2.26e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 167.63 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNeTKF--DALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDIYLNGKNVTSIRKKVLN 80
Cdd:TIGR04521 1 IKLKNVSYIYQPG-TPFekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIqHLNGLL-KPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRnEEFGFVFQ----QFFmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKAN-NLSGGQKQRVCIA 155
Cdd:TIGR04521 79 DLR-KKVGLVFQfpehQLF---EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPfELSGGQMRRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD-PDLAARCDRQVHVRDGLIV 222
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-222 |
1.53e-50 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 163.95 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKkvlNKtR 83
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP---HK-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeeFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03300 73 P--VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLIV 222
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQ 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
2.19e-50 |
|
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: 164.91 E-value: 2.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDIYLNG------KNVTSIRK 76
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAkLLNGLL-LPTSGKVTVDGldtldeENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVlnktrneefGFVFQ----QFFMNakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRV 152
Cdd:TIGR04520 78 KV---------GMVFQnpdnQFVGA---TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-222 |
4.25e-50 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 163.23 E-value: 4.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLD-----QPTSGDIYLNGKNVTSIRKK 77
Cdd:TIGR00972 1 AIEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlvpgVRIEGKVLFDGQDIYDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VLNKTRNeeFGFVFQQ---FFMnakdTVLNNVLLPLKIGGISGSKR-KKMALDALKAVGLEDKVQNK----ANNLSGGQK 149
Cdd:TIGR00972 77 VVELRRR--VGMVFQKpnpFPM----SIYDNIAYGPRLHGIKDKKElDEIVEESLKKAALWDEVKDRlhdsALGLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAARC-DRQVHVRDGLIV 222
Cdd:TIGR00972 151 QRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK--YTIVIVTHNMQQAARIsDRTAFFYDGELV 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-217 |
1.68e-48 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 159.10 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVlnKT 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE--RL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEEFGFVFQQFFMNAKDTVLNNVLL-PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAarcdRQVHVR 217
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFA----EKVASR 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-219 |
7.01e-48 |
|
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: 154.71 E-value: 7.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 5 EAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirkKVLNKTRN 84
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 85 EEFGFVFQqffmnakdtvlnnvllplkiggisgskrkkmaldalkavgledkvqnkannLSGGQKQRVCIARALVNNPQI 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 165 IFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-212 |
1.15e-47 |
|
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: 156.15 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 5 EAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVlnktrn 84
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 85 eefGFVFQQ------FFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:cd03235 71 ---GYVPQRrsidrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDR 212
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEyFDR 201
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
1.42e-47 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 157.33 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvln 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 ktRNEEFGFVFQqffmnaKD------TVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:COG4525 74 --PGADRGVVFQ------KDallpwlNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
1.73e-47 |
|
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: 154.52 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 5 EAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRn 84
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 85 eefGFVFQqffmnakdtvlnnvllplkiggisgskrkkmaldALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQI 164
Cdd:cd03214 76 ---AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 165 IFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
2.86e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 163.78 E-value: 2.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIkkSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:COG4987 332 PSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TrneeFGFVFQQ--FFMnakDTVLNNvllpLKIGGISGSKRKkmALDALKAVGLEDKVQN-----------KANNLSGGQ 148
Cdd:COG4987 410 R----IAVVPQRphLFD---TTLREN----LRLARPDATDEE--LWAALERVGLGDWLAAlpdgldtwlgeGGRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-203 |
1.51e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 154.19 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvlnKTR 83
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRV------HAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHD 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
2.27e-46 |
|
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: 161.08 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtr 83
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neEFGFVFQQ--FFmnaKDTVLNNVLLplkigGISGSKRKKMAlDALKAVGLEDKVQN-----------KANNLSGGQKQ 150
Cdd:COG4988 412 --QIAWVPQNpyLF---AGTIRENLRL-----GRPDASDEELE-AALEAAGLDEFVAAlpdgldtplgeGGRGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 151 RVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIV 550
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-222 |
4.90e-46 |
|
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: 152.84 E-value: 4.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI-----RKKV 78
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktrneefGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDK--VQNKANNLSGGQKQRVCIAR 156
Cdd:cd03295 78 ---------GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-222 |
7.13e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 152.47 E-value: 7.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIY-----------LNGKNVT 72
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdfsqkPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 73 SIRKKVlnktrneefGFVFQQFFMNAKDTVLNNVL-LPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQR 151
Cdd:COG4161 79 LLRQKV---------GMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 152 VCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLAARCDRQV-HVRDGLIV 222
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVvYMEKGRII 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-221 |
1.33e-45 |
|
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: 149.47 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtr 83
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVFQQFFMNAKDTVLNNVllplkiggisgskrkkmaldalkavgledkvqnkanNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03230 75 ---IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDRQVHVRDGLI 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-223 |
2.34e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 158.79 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLnktR 83
Cdd:COG1132 340 IEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---R 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMnAKDTVLNNVLLplkigGISGSKRKKMaLDALKAVGLEDKVQNKAN-----------NLSGGQKQRV 152
Cdd:COG1132 414 -RQIGVVPQDTFL-FSGTIRENIRY-----GRPDATDEEV-EEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIVG 223
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
2.52e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 152.02 E-value: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI--RKKV 78
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 LNKtrneefgfVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:PRK09452 88 VNT--------VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLI 221
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-224 |
2.75e-44 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 147.71 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRnEEFGFVFQQFFMNAKDT 101
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKK 181
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488286249 182 IEELLFDLNKnKGITLIIVTHDPDLAARCD-RQVHVRDGLIVGG 224
Cdd:PRK10908 176 ILRLFEEFNR-VGVTVLMATHDIGLISRRSyRMLTLSDGHLHGG 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
4.31e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 148.41 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG------------- 68
Cdd:COG4598 7 PALEVRDLHKSFGDLEV----LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 69 -----KNVTSIRKKVlnktrneefGFVFQQFFMNAKDTVLNNVLL-PLKIGGISGSKRKKMALDALKAVGLEDKVQNKAN 142
Cdd:COG4598 83 vpadrRQLQRIRTRL---------GMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 143 NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSatgkkieELLFDLNK------NKGITLIIVTHDPDLAarcdRQV-- 214
Cdd:COG4598 154 HLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEVLKvmrdlaEEGRTMLVVTHEMGFA----RDVss 222
|
..
gi 488286249 215 HV 216
Cdd:COG4598 223 HV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
1.78e-43 |
|
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: 152.92 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKS-TFMHILALLDQP---TSGDIYLNGKNVTSIRK 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVLNKTRNEEFGFVFQQFfMnakdTVLNnvllPLK-IG-----------GISGSKRKKMALDALKAVGLEDkVQNKAN-- 142
Cdd:COG4172 84 RELRRIRGNRIAMIFQEP-M----TSLN----PLHtIGkqiaevlrlhrGLSGAAARARALELLERVGIPD-PERRLDay 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 143 --NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRqVHV-RD 218
Cdd:COG4172 154 phQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADR-VAVmRQ 232
|
....
gi 488286249 219 GLIV 222
Cdd:COG4172 233 GEIV 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-222 |
1.79e-43 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 146.16 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:COG4555 1 MIEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rneefGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNP 162
Cdd:COG4555 77 -----GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVV 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-222 |
4.33e-43 |
|
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: 144.43 E-value: 4.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVlnktr 83
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLIV 222
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRII 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-222 |
6.90e-43 |
|
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: 143.93 E-value: 6.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirkKVLNKTR 83
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT----DLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeeFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03301 73 D--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLIV 222
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQIQ 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
7.68e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 145.61 E-value: 7.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfDALKGVDLKVEKGESVAIIGKSGSGKST-FMHILALLdQPTSGDIYLNGKNVtSIRKKVLNK 81
Cdd:PRK13639 1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTlFLHFNGIL-KPTSGEVLIKGEPI-KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRnEEFGFVFQ----QFFmnaKDTVLNNVLL-PLKIGgISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIAR 156
Cdd:PRK13639 76 VR-KTVGIVFQnpddQLF---APTVEEDVAFgPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAARCDRQVHV-RDGLIVGG 224
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVmSDGKIIKE 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-221 |
8.33e-43 |
|
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: 144.40 E-value: 8.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvlnKTR 83
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGS------KRKKMALdaLKAVGLEDKVQNKANNLSGGQKQRVCIARA 157
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaeiRAKVHEL--LKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLI 221
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
1.46e-42 |
|
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: 140.86 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtrneEFGFVFQQFFMNAKDTV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 103 LNNVLLPLKIGGISGSKRKKMALDALKAVGLED----KVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-221 |
2.14e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 144.05 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 7 KNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvlNKTRnee 86
Cdd:PRK11247 16 NAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR----EDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 87 fgFVFQQFFMNAKDTVLNNVLLplkigGISGSKRKKmALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIF 166
Cdd:PRK11247 85 --LMFQDARLLPWKKVIDNVGL-----GLKGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 167 ADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLI 221
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-219 |
3.48e-42 |
|
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: 142.26 E-value: 3.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neefGFVFQqffmnaKD------TVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARA 157
Cdd:cd03263 78 ----GYCPQ------FDalfdelTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGItlIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEAlCDRIAIMSDG 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-219 |
6.66e-42 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 142.84 E-value: 6.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALL--DQPTSGDIYLNGKNVTSIRK--K 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVQREGRlaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VLNKTRNEEfGFVFQQFFMNAKDTVLNNVLlplkIGGISGS------------KRKKMALDALKAVGLEDKVQNKANNLS 145
Cdd:PRK09984 80 DIRKSRANT-GYIFQQFNLVNRLSVLENVL----IGALGSTpfwrtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 146 GGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-222 |
8.78e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.08 E-value: 8.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDalkgVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG-----------KNVT 72
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD----ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 73 SIRKKVlnktrneefGFVFQQFFMNAKDTVLNNVL-LPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQR 151
Cdd:PRK11124 79 ELRRNV---------GMVFQQYNLWPHLTVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 152 VCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-222 |
1.08e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.43 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGknETKFDAlkgvDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI----RKkvl 79
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaeRP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 nktrneeFGFVFQQ--FFMNAkdTVLNNVLLPLKIGG-ISGSKRKKMAlDALKAVGLEDKVQNKANNLSGGQKQRVCIAR 156
Cdd:COG3840 73 -------VSMLFQEnnLFPHL--TVAQNIGLGLRPGLkLTAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 157 ALVNNPQIIFADEPTGNLDSAtgKKIE--ELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIA 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-222 |
2.28e-41 |
|
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: 147.14 E-value: 2.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSY-------GKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTF-MHILALLdqPTSGDIYLNGKNVTSI 74
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVLNKTRnEEFGFVFQQFF--MNAKDTVLNNVLLPLKI--GGISGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQK 149
Cdd:COG4172 353 SRRALRPLR-RRMQVVFQDPFgsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHdpDLA---ARCDRQVHVRDGLIV 222
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH--DLAvvrALAHRVMVMKDGKVV 505
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-222 |
1.60e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.11 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTS-----GDIYLNGKNVTSIR 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTV----LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKVLNKTRnEEFGFVFQQFFMNAKDTVLNNVLL-PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:PRK11264 77 KGLIRQLR-QHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGiTLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
4.03e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.59 E-value: 4.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGK-----NVTSIRK 76
Cdd:PRK13632 6 VMIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskeNLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVlnktrneefGFVFQ----QFFmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRV 152
Cdd:PRK13632 84 KI---------GIIFQnpdnQFI---GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDR 212
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADK 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-222 |
6.06e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.22 E-value: 6.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG-----KNVTSIRKK 77
Cdd:PRK13635 5 IIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VlnktrneefGFVFQ----QFfmnAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVC 153
Cdd:PRK13635 83 V---------GMVFQnpdnQF---VGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 154 IARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
9.36e-40 |
|
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: 142.63 E-value: 9.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQ--PTSGDIYLN-------------- 67
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 68 ---------GKNVTSIRKKVLNKTRNEEFGF------VFQQFF-MNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAV 131
Cdd:TIGR03269 77 kvgepcpvcGGTLEPEEVDFWNLSDKLRRRIrkriaiMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 132 GLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-C 210
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlS 236
|
250
....*....|..
gi 488286249 211 DRQVHVRDGLIV 222
Cdd:TIGR03269 237 DKAIWLENGEIK 248
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-222 |
9.63e-40 |
|
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: 136.31 E-value: 9.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvlnKTR 83
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL------PPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD-PDLAARCDRQVHVRDGLIV 222
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-222 |
1.42e-39 |
|
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: 135.08 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 5 EAKNIKKSYGKNEtkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirkkvlNKTRN 84
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 85 EEFGFVFQ----QFFMnakDTVLNNVLLPLKIGgisgSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:cd03226 71 KSIGYVMQdvdyQLFT---DSVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 161 NPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-222 |
1.57e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 136.89 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKN-----ETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIR 75
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 kkvlNKTRNEEFGFVFQqffmnakDTvlNNVLLP-LKIGGI-----------SGSKRKKMALDALKAVGL-EDKVQNKAN 142
Cdd:COG4167 82 ----YKYRCKHIRMIFQ-------DP--NTSLNPrLNIGQIleeplrlntdlTAEEREERIFATLRLVGLlPEHANFYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 143 NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAArcdrqvHVRDGLIV 222
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVK------HISDKVLV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-209 |
2.51e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 135.81 E-value: 2.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALL-----DQPTSGDIYLNGKN----- 70
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEV----LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDifkmd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 71 VTSIRKKVlnktrneefGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRK--KMALDALKAVGLEDKVQNK----ANNL 144
Cdd:PRK14247 77 VIELRRRV---------QMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLWDEVKDRldapAGKL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 145 SGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAAR 209
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAAR 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-216 |
3.17e-39 |
|
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: 135.26 E-value: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtr 83
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFV--FQ--QFFMNAkdTVLNNVLLPLKI---GGISGSKRKKM-------ALDALKAVGLEDKVQNKANNLSGGQK 149
Cdd:cd03219 75 ---LGIGrtFQipRLFPEL--TVLENVMVAAQArtgSGLLLARARREerearerAEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDRqVHV 216
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSlADR-VTV 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-218 |
3.40e-39 |
|
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: 134.14 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKkvlnk 81
Cdd:COG4133 1 MMLEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKkmALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:COG4133 72 DYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLNKNKGItLIIVTHDPdLAARCDRQVHVRD 218
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQP-LELAAARVLDLGD 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
6.00e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 134.78 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTS-----IR 75
Cdd:COG0411 2 DPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphrIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKVLNKTrneefgfvFQ--QFFMNAkdTVLNNVLLPL----KIGGISGSKRKKM-----------ALDALKAVGLEDKVQ 138
Cdd:COG0411 78 RLGIART--------FQnpRLFPEL--TVLENVLVAAharlGRGLLAALLRLPRarreerearerAEELLERVGLADRAD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 139 NKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRqVHV 216
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADR-IVV 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-203 |
6.17e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.79 E-value: 6.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFD-------ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIR 75
Cdd:COG4608 7 LLEVRDLKKHFPVRGGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKVLNKTRnEEFGFVFQQFF--MNAKDTVLNNVLLPLKIGGI-SGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQKQR 151
Cdd:COG4608 87 GRELRPLR-RRMQMVFQDPYasLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488286249 152 VCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-222 |
6.34e-39 |
|
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: 137.48 E-value: 6.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKvln 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 kTRNeeFGFVFQQF--FMNAkdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:TIGR03265 75 -KRD--YGIVFQSYalFPNL--TVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLIV 222
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVIE 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-209 |
1.05e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 134.20 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALL-----DQPTSGDIYLNGKNVTS----- 73
Cdd:PRK14267 5 IETVNLRVYYGSNHV----IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 74 --IRKKVlnktrneefGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKkmaLD-----ALKAVGLEDKVQNKAN---- 142
Cdd:PRK14267 81 ieVRREV---------GMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKE---LDervewALKKAALWDEVKDRLNdyps 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 143 NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAAR 209
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAAR 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-225 |
1.56e-38 |
|
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: 132.80 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVE---KGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQQFFMNAK 99
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNVLLPLKigGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATG 179
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488286249 180 KKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIVGGD 225
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-207 |
4.07e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.79 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEaknIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRK---- 76
Cdd:PRK10619 6 LNVID---LHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 -KVLNKTR----NEEFGFVFQQFFMNAKDTVLNNVL-LPLKIGGISGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQK 149
Cdd:PRK10619 79 lKVADKNQlrllRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLA 207
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFA 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-222 |
6.17e-38 |
|
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: 131.08 E-value: 6.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDalkgvdLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI---RKKVln 80
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFD------LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppaDRPV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 ktrneefGFVFQQFFMNAKDTVLNNVLLPLKIG-GISGSKRKKMAlDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:cd03298 73 -------SMLFQENNLFAHLTVEQNVGLGLSPGlKLTAEDRQAIE-VALARVGLAGLEKRLPGELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARC-DRQVHVRDGLIV 222
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-222 |
6.45e-38 |
|
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: 134.16 E-value: 6.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 38 IIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvlnKTRNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISG 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV------PPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 118 SKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITL 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*.
gi 488286249 198 IIVTHDPDLA-ARCDRQVHVRDGLIV 222
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIA 180
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-219 |
6.86e-38 |
|
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: 129.64 E-value: 6.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:cd03246 1 LEVENVSFRYPGAEPP--VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVFQqffmnakdtvlnNVLLplkiggISGSKRKkmaldalkavgledkvqnkaNNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03246 78 ---VGYLPQ------------DDEL------FSGSIAE--------------------NILSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-222 |
9.81e-38 |
|
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: 131.19 E-value: 9.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNktr 83
Cdd:cd03254 3 IEFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMNAkDTVLNNVLLplkigGISGSKRKKMALdALKAV-----------GLEDKVQNKANNLSGGQKQRV 152
Cdd:cd03254 77 -SMIGVVLQDTFLFS-GTIMENIRL-----GRPNATDEEVIE-AAKEAgahdfimklpnGYDTVLGENGGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-222 |
2.20e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 131.35 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSY------GKNETKfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI 74
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVLnKTRNEEFGFVFQQFF--MNAKDTVLNNVLLPLK-IGGISGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQKQ 150
Cdd:PRK10419 80 NRAQR-KAFRRDIQMVFQDSIsaVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 151 RVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-222 |
2.45e-37 |
|
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: 129.63 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYgkNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtr 83
Cdd:cd03245 3 IEFRNVSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neEFGFVFQQ---FFMNAKDTVL--------NNVLLPLKIGGISgskrkkmALDALKAVGLEDKVQNKANNLSGGQKQRV 152
Cdd:cd03245 79 --NIGYVPQDvtlFYGTLRDNITlgapladdERILRAAELAGVT-------DFVNKHPNGLDLQIGERGRGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
2.58e-37 |
|
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: 129.89 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlnktRNEEFGFVFQQFFMNAKDTV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE---------PGPDRMVVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNVLLPLK--IGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGK 180
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488286249 181 KIEELLFDLNKNKGITLIIVTHDPDLAA-RCDRQVHVRDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
2.77e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 132.13 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYG-KNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDI---YLNGKNVTSIRKK- 77
Cdd:PRK13651 3 IKVKNIVKIFNkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIeHLNALL-LPDTGTIewiFKDEKNKKKTKEKe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 ------VLNKTRNEEF----------GFVFQ----QFFmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGL-EDK 136
Cdd:PRK13651 82 kvleklVIQKTRFKKIkkikeirrrvGVVFQfaeyQLF---EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 137 VQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLA-ARCDRQVH 215
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVlEWTKRTIF 237
|
....*..
gi 488286249 216 VRDGLIV 222
Cdd:PRK13651 238 FKDGKII 244
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-221 |
3.19e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 132.90 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvlnkTR 83
Cdd:PRK10851 3 IEIANIKKSFGRTQV----LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------AR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIggISGSKRKKMALDALKAVGLEDKVQ--NKAN----NLSGGQKQRVCIARA 157
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRERPNAAAIKAKVTQLLEMVQlaHLADrypaQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLI 221
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-222 |
4.16e-37 |
|
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: 128.85 E-value: 4.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNetkfDALKGVDLKVEKGESvAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG----KNVTSIRKKVl 79
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlKQPQKLRRRI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 nktrneefGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:cd03264 75 --------GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHD-PDLAARCDRQVHVRDGLIV 222
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-216 |
1.40e-36 |
|
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: 134.34 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTrneeFGFVFQQFFMNAkDT 101
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ----IAWVPQHPFLFA-GT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLPLKIGGISGSKRKKMALDALKAV-----GLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDS 176
Cdd:TIGR02857 412 IAENIRLARPDASDAEIREALERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488286249 177 ATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHV 216
Cdd:TIGR02857 492 ETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-203 |
2.01e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.99 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNeTKFDALkgvDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlNKTR 83
Cdd:PRK11432 7 VVLKNITKRFGSN-TVIDNL---NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAV---GLEDKVqnkANNLSGGQKQRVCIARALVN 160
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVdlaGFEDRY---VDQISGGQQQRVALARALIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488286249 161 NPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
2.17e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.22 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT------SI 74
Cdd:COG1129 2 EPLLEMRGISKSFGGVK----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVlnktrneefGFVFQQF----FMnakdTVLNNVLL---PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGG 147
Cdd:COG1129 78 AAGI---------AIIHQELnlvpNL----SVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTGNLDSAtgkkiE-ELLFDLN---KNKGITLIIVTHD-PDLAARCDRqVHV-RDGLI 221
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTER-----EvERLFRIIrrlKAQGVAIIYISHRlDEVFEIADR-VTVlRDGRL 218
|
..
gi 488286249 222 VG 223
Cdd:COG1129 219 VG 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-222 |
2.24e-36 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 128.77 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSY------GKNETKfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIR 75
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfGAKQRA-PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKVLNKTRnEEFGFVFQQFF--MNAKDTVLNNVLLPLK-IGGISGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQKQR 151
Cdd:TIGR02769 80 RKQRRAFR-RDVQLVFQDSPsaVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKlPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 152 VCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
3.56e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 127.58 E-value: 3.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQ-----PTSGDIYLNGKNVTSIRK 76
Cdd:PRK14239 4 PILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVLNKTRneEFGFVFQQ---FFMnakdTVLNNVLLPLKIGGIsgskRKKMALDA-----LKAVGLEDKVQNK----ANNL 144
Cdd:PRK14239 80 DTVDLRK--EIGMVFQQpnpFPM----SIYENVVYGLRLKGI----KDKQVLDEaveksLKGASIWDEVKDRlhdsALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 145 SGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAARcdrqVHVRDGLIVGG 224
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASR----ISDRTGFFLDG 223
|
.
gi 488286249 225 D 225
Cdd:PRK14239 224 D 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-223 |
5.34e-36 |
|
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: 124.46 E-value: 5.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT------SIRKK 77
Cdd:cd03216 1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfasprdARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VlnktrneefGFVFQqffmnakdtvlnnvllplkiggisgskrkkmaldalkavgledkvqnkannLSGGQKQRVCIARA 157
Cdd:cd03216 77 I---------AMVYQ---------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIVG 223
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVG 162
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-222 |
5.51e-36 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 126.58 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYgknETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG---KNVT--SIRKKV 78
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTldSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktrneefGFVFQqffmnakDTVLNN--VLLPLKIGGISGSKRKkmALDALKAVGLEDKVQN-----------KANNLS 145
Cdd:cd03253 78 ---------GVVPQ-------DTVLFNdtIGYNIRYGRPDATDEE--VIEAAKAAQIHDKIMRfpdgydtivgeRGLKLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 146 GGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-222 |
5.59e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 128.67 E-value: 5.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNktR 83
Cdd:COG1125 2 IEFENVTKRYPDGTV---AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELR--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeeFGFVFQQ--FF--MnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKA--NNLSGGQKQRVCIARA 157
Cdd:COG1125 77 R--IGYVIQQigLFphM----TVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRypHELSGGQQQRVGVARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPD----LAarcDRQVHVRDGLIV 222
Cdd:COG1125 151 LAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDealkLG---DRIAVMREGRIV 216
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-222 |
8.17e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 133.45 E-value: 8.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNktR 83
Cdd:TIGR03375 464 IEFRNVSFAYPGQETP--ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLR--R 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeeFGFVFQqffmnakDTVLnnvllplkiggISGSKRKKMALD-----------ALKAVGLEDKVQNKAN---------- 142
Cdd:TIGR03375 540 N--IGYVPQ-------DPRL-----------FYGTLRDNIALGapyaddeeilrAAELAGVTEFVRRHPDgldmqigerg 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 143 -NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:TIGR03375 600 rSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
.
gi 488286249 222 V 222
Cdd:TIGR03375 678 V 678
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-209 |
8.38e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.83 E-value: 8.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNeTKF--DALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDIYL---------NGKNV 71
Cdd:PRK13634 3 ITFQKVEHRYQYK-TPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLqHLNGLL-QPTSGTVTIgervitagkKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 72 TSIRKKVlnktrneefGFVFQ----QFFmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKAN-NLSG 146
Cdd:PRK13634 81 KPLRKKV---------GIVFQfpehQLF---EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 147 GQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR 209
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-203 |
3.31e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.20 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlnktRNEEFGFVFQQFFMNAKDT 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---------PGAERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKK 181
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 488286249 182 IEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-222 |
1.54e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.07 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQQFFMNAKDT 101
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKK 181
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488286249 182 IEELLFDLNKNKGITLIIVTHDPDLAARC-DRQVHVRDGLIV 222
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVV 244
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-222 |
8.65e-34 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 123.65 E-value: 8.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYgkNETKfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKvlnkTR 83
Cdd:NF040840 2 IRIENLSKDW--KEFK---LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE----KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeeFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:NF040840 73 G--IAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLIV 222
Cdd:NF040840 151 LLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEAlSLADRVGIMLNGRLS 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-203 |
1.78e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 123.03 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYgknETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvln 80
Cdd:PRK11650 1 MAGLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:PRK11650 72 EPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286249 161 NPQIIFADEPTGNLDSatgK-----KIEelLFDLNKNKGITLIIVTHD 203
Cdd:PRK11650 152 EPAVFLFDEPLSNLDA---KlrvqmRLE--IQRLHRRLKTTSLYVTHD 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-222 |
2.88e-33 |
|
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: 119.64 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGknvTSIRKKVLNKTR 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEeFGFVFQQFFMnAKDTVLNNVLLplkigGISGSKRKKmALDALKAVGLEDKVQNKAN-----------NLSGGQKQRV 152
Cdd:cd03251 76 RQ-IGLVSQDVFL-FNDTVAENIAY-----GRPGATREE-VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-203 |
5.35e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.22 E-value: 5.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSY------GKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI 74
Cdd:PRK11308 3 QPLLQAIDLKKHYpvkrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVLnKTRNEEFGFVFQQFF--MNAKDTVLNNVLLPLKIG-GISGSKRKKMALDALKAVGLE-DKVQNKANNLSGGQKQ 150
Cdd:PRK11308 83 DPEAQ-KLLRQKIQIVFQNPYgsLNPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286249 151 RVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-210 |
1.06e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.58 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLDQP--TSGDIYLNGKNVTSI---RKKVlnktrneefGFVFQQFFM 96
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALpaeQRRI---------GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 97 NAKDTVLNNVL--LPlkiGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNL 174
Cdd:COG4136 88 FPHLSVGENLAfaLP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 488286249 175 DSATGKKIEELLFDLNKNKGITLIIVTHDPD---LAARC 210
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEdapAAGRV 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-216 |
1.34e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.07 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYgKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTS-----IRKK 77
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VlnktrneefGFVFQ----QFFmnaKDTVLNNVLL-PLKIGgISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRV 152
Cdd:PRK13647 81 V---------GLVFQdpddQVF---SSTVWDDVAFgPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLAARCDRQVHV 216
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIV 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-221 |
1.82e-32 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 116.88 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 27 DLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvlnKTRNEEFGFVFQQFFMNAKDTVLNNV 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL------APYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 107 LLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELL 186
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 488286249 187 FDLNKNKGITLIIVTHDP-DLAARCDRQVHVRDGLI 221
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLsDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
1.99e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.68 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG-----KNVTSIR 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKVlnktrneefGFVFQQ---FFMNAkdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRV 152
Cdd:PRK13650 81 HKI---------GMVFQNpdnQFVGA--TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-222 |
2.01e-32 |
|
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: 117.47 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 25 GVDLKVEKGESVAIIGKSGSGKS-TFMHILALLDQ---PTSGDIYLNGKNVTSIRkkvlnkTRNEEFGFVFQQFfMNAKD 100
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPgltQTSGEILLDGRPLLPLS------IRGRHIATIMQNP-RTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVL---NNVLLPLKIGGISGSKRKKMALDALKAVGLEDK---VQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNL 174
Cdd:TIGR02770 77 PLFtmgNHAIETLRSLGKLSKQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488286249 175 DSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHV-RDGLIV 222
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVmDDGRIV 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-202 |
2.58e-32 |
|
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: 115.49 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvLNKTR 83
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD-----LEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAkDTVLNNVLLPlkiggisgskrkkmaldalkavgledkvqnkannLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03247 74 SSLISVLNQRPYLFD-TTLRNNLGRR----------------------------------FSGGERQRLALARILLQDAP 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTH 202
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITH 155
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-222 |
2.89e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.27 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNE--TKFDALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDIYLNG------KNVTS 73
Cdd:PRK13633 4 MIKCKNVSYKYESNEesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAkHMNALL-IPSEGKVYVDGldtsdeENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 74 IRKKVlnktrneefGFVFQqffmNAKDT-----VLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQ 148
Cdd:PRK13633 83 IRNKA---------GMVFQ----NPDNQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-204 |
2.89e-32 |
|
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: 115.73 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDA--LKGVDLKVEKGESVAIIGKSGSGKSTFMHILA--LLDQPTSGDIYLNGKNVT--SI 74
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDkrSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVlnktrneefGFVFQQFFMNAKDTVLNNVLLPLKIGGIsgskrkkmaldalkavgledkvqnkannlSGGQKQRVCI 154
Cdd:cd03213 81 RKII---------GYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSI 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDP 204
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQP 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-222 |
3.56e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.23 E-value: 3.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKN---ETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDIYLNGKNVTS------ 73
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKK--ALDNVNIEIEDGEFVGLIGHTGSGKSTLIqHLNGLL-KPTSGKIIIDGVDITDkkvkls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 74 -IRKKVlnktrneefGFVFQ----QFFmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLE-DKVQNKAN-NLSG 146
Cdd:PRK13637 80 dIRKKV---------GLVFQypeyQLF---EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPfELSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 147 GQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD-PDLAARCDRQVHVRDGLIV 222
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-205 |
4.40e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.01 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnETKFDA--LKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDIYLNGKNVTS-IRKKVL 79
Cdd:PRK13641 3 IKFENVDYIYSP-GTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMqHFNALL-KPSSGTITIAGYHITPeTGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 NKTRnEEFGFVFQ----QFFMNakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKAN-NLSGGQKQRVCI 154
Cdd:PRK13641 81 KKLR-KKVSLVFQfpeaQLFEN---TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPD 205
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMD 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-203 |
5.39e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 119.36 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKfdalKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKvln 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVIS----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 ktrNEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:PRK11000 74 ---ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488286249 161 NPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-208 |
7.91e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 118.31 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKS-TFMHILALLDQP---TSGDIYLNGKNVTSIRK 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVLNKTRNEEFGFVFQQFF--MNAKDTVLNNVLLPLKI--GGiSGSKRKKMALDALKAVGLED---KVQNKANNLSGGQK 149
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMtsLNPCYTVGFQIMEAIKVhqGG-NKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAA 208
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVA 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-222 |
7.97e-32 |
|
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: 115.01 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlNKTR 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK------NIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFV--FQQFFMNAkdTVLNNVLLPLKIGGIsgskRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:cd03268 71 LRRIGALieAPGFYPNL--TARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHD-PDLAARCDRQVHVRDGLIV 222
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
2.37e-31 |
|
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: 114.45 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTS------IRKK 77
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppherARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VlnktrneefGFVFQ--QFFMNAkdTVLNNVLLPLKIGGISGSKRkkmALDALKAV--GLEDKVQNKANNLSGGQKQRVC 153
Cdd:cd03224 77 I---------GYVPEgrRIFPEL--TVEENLLLGAYARRRAKRKA---RLERVYELfpRLKERRKQLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 154 IARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-222 |
2.52e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.21 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:COG4559 2 LEAENLSVRLGGRTL----LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 -----NEEFGFVFqqffmnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:COG4559 78 avlpqHSSLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 159 V-------NNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQyADRILLLHQGRLV 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-222 |
2.86e-31 |
|
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: 114.13 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvLNKTR 83
Cdd:cd03244 3 IEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQqffmnakDTVLnnvllplkiggISGSKRK----------KMALDALKAVGLEDKVQNKA-----------N 142
Cdd:cd03244 78 -SRISIIPQ-------DPVL-----------FSGTIRSnldpfgeysdEELWQALERVGLKEFVESLPggldtvveeggE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 143 NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFdlNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:cd03244 139 NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-202 |
8.73e-31 |
|
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: 113.40 E-value: 8.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYgknETKFD--ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNvtsIRKKVLNK 81
Cdd:cd03249 1 IEFKNVSFRY---PSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEeFGFVFQQ---FFMnakdTVLNNVLLplkigGISGSKRKKMALDALKA------VGLEDK----VQNKANNLSGGQ 148
Cdd:cd03249 75 LRSQ-IGLVSQEpvlFDG----TIAENIRY-----GKPDATDEEVEEAAKKAnihdfiMSLPDGydtlVGERGSQLSGGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnkNKGITLIIVTH 202
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAH 196
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-225 |
9.13e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 9.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYgkNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGD--------IYLNGKNVTSI 74
Cdd:PRK13640 5 IVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVlnktrneefGFVFQQ---FFMNAkdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQR 151
Cdd:PRK13640 83 REKV---------GIVFQNpdnQFVGA--TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 152 VCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIVGGD 225
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-219 |
1.27e-30 |
|
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: 111.79 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 15 KNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFmhILALLD--QPTSGDIYLNGKnvtsirkkvlnktrneeFGFVFQ 92
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSL--LSALLGelEKLSGSVSVPGS-----------------IAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 93 Q-FFMNAkdTVLNNVLLplkiggisGSK-RKKMALDALKAVGLEDKVQN-----------KANNLSGGQKQRVCIARALV 159
Cdd:cd03250 74 EpWIQNG--TIRENILF--------GKPfDEERYEKVIKACALEPDLEIlpdgdlteigeKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLF--DLNKNKgiTLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNK--TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-222 |
2.11e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.98 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 27 DLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI---RKKVlnktrneefGFVFQQFFMNAKDTVL 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsRRPV---------SMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 104 NNVLLPLKIG-GISGSKRKKMAlDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKI 182
Cdd:PRK10771 90 QNIGLGLNPGlKLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488286249 183 EELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-204 |
2.20e-30 |
|
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: 117.08 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTrneeFGFVFQQFFMNAKdT 101
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLPLkiGGISGSKrkkmALDALKAVGLED-----------KVQNKANNLSGGQKQRVCIARALVNNPQIIFADEP 170
Cdd:TIGR02868 425 VRENLRLAR--PDATDEE----LWAALERVGLADwlralpdgldtVLGEGGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....*
gi 488286249 171 TGNLDSATGkkiEELLFDLNK-NKGITLIIVTHDP 204
Cdd:TIGR02868 499 TEHLDAETA---DELLEDLLAaLSGRTVVLITHHL 530
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-203 |
2.27e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.87 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGK---NETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsiRKKVLN 80
Cdd:COG1101 2 LELKNLSKTFNPgtvNEKR--ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRNeeFGFVFQQFFMN-AKD-TVLNNVLLPLKIGG----ISGSKRKKMAL--DALKAV--GLEDKVQNKANNLSGGQKQ 150
Cdd:COG1101 78 RAKY--IGRVFQDPMMGtAPSmTIEENLALAYRRGKrrglRRGLTKKRRELfrELLATLglGLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286249 151 RVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-219 |
5.63e-30 |
|
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: 113.67 E-value: 5.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 26 VDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQQFFMNAKDTVLNN 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 106 VLLPLKigGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEEL 185
Cdd:TIGR02142 96 LRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190
....*....|....*....|....*....|....*
gi 488286249 186 LFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-222 |
5.77e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNK 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TR-----NEEFGFVFqqffmnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIAR 156
Cdd:PRK13548 77 RRavlpqHSSLSFPF---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 157 ALV------NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-222 |
6.83e-30 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 111.33 E-value: 6.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSG-DIYLNGK-----NVTSI 74
Cdd:COG1119 1 DPLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggeDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVlnktrneefGFV---FQQFFmNAKDTVLNNVLlplkiGGISGS---------KRKKMALDALKAVGLEDKVQNKAN 142
Cdd:COG1119 77 RKRI---------GLVspaLQLRF-PRDETVLDVVL-----SGFFDSiglyreptdEQRERARELLELLGLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 143 NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARC-DRQVHVRDGLI 221
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
.
gi 488286249 222 V 222
Cdd:COG1119 222 V 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-214 |
7.03e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.63 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 21 DALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGdiylngknvtsirkkVLNKTRNEEFGFVFQQ------F 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------------TVRRAGGARVAYVPQRsevpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 95 FMNAKDTVlnnvllplKIG--GISGSKRKKMALD------ALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIF 166
Cdd:NF040873 71 PLTVRDLV--------AMGrwARRGLWRRLTRDDraavddALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286249 167 ADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAARCDRQV 214
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCV 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-222 |
1.45e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLnGKNVtsirkkvlnkt 82
Cdd:COG0488 315 VLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rneEFGFVFQ-QFFMNAKDTVLNNvllplkIGGISGSKRKKMALDALKAVGL-EDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:COG0488 379 ---KIGYFDQhQEELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 161 NPQIIFADEPTGNLDSATgkkIEELLFDLNKNKGiTLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG0488 450 PPNVLLLDEPTNHLDIET---LEALEEALDDFPG-TVLLVSHDRYFLDRvATRILEFEDGGVR 508
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-225 |
1.58e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.92 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:PRK11160 339 LTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVFQQFFMNAkDTVLNNVLLplkigGISGSKRKKMaLDALKAVGLEDKVQNKA----------NNLSGGQKQRVC 153
Cdd:PRK11160 416 ---ISVVSQRVHLFS-ATLRDNLLL-----AAPNASDEAL-IEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 154 IARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRqVHVRDG--LIVGGD 225
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDR-ICVMDNgqIIEQGT 556
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-222 |
1.60e-29 |
|
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: 114.90 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKF-DALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIY--LNGKNVTSIRKKVL 79
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 NKTRNEEF-GFVFQQFFMNAKDTVLNNVL------LPLKIGgisgsKRKkmALDALKAVGLEDK----VQNK-ANNLSGG 147
Cdd:TIGR03269 359 GRGRAKRYiGILHQEYDLYPHRTVLDNLTeaigleLPDELA-----RMK--AVITLKMVGFDEEkaeeILDKyPDELSEG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIV 507
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-212 |
2.07e-29 |
|
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: 109.73 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtrneeFGFVFQQFFMNAKD- 100
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-----IGVVFGQKTQLWWDl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVLNNVLLPLKIGGISGSKRKKmALDAL-KAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATG 179
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKK-RLDELsELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190
....*....|....*....|....*....|....
gi 488286249 180 KKIEELLFDLNKNKGITLIIVTHD-PDLAARCDR 212
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYmKDIEALARR 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-222 |
2.48e-29 |
|
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: 108.91 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKkvlnktr 83
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03269 70 -NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-202 |
3.36e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 109.35 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI------ 74
Cdd:COG1137 1 MMTLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVlnktrneefGF------VFQqffmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQ 148
Cdd:COG1137 77 RLGI---------GYlpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTH 202
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDH 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-224 |
5.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.83 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYgKNETKFD--ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG---------KNVT 72
Cdd:PRK13649 3 INLQNVSYTY-QAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 73 SIRKKVlnktrneefGFVFQ----QFFmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKAN-NLSGG 147
Cdd:PRK13649 82 QIRKKV---------GLVFQfpesQLF---EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLAARCDRQVHVRDG--LIVGG 224
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKgkLVLSG 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
6.31e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYgKNETKFdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKt 82
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rneEFGFVFQ----QFfmnAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:PRK13648 84 ---HIGIVFQnpdnQF---VGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-202 |
7.00e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.81 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT------SIRK 76
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVlnktrneefGFVFQQF-----FmnakdTVLNNVLL---PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQ 148
Cdd:COG3845 81 GI---------GMVHQHFmlvpnL-----TVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLdsaTGKKIEELLFDLN--KNKGITLIIVTH 202
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRrlAAEGKSIIFITH 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-219 |
7.82e-29 |
|
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: 107.91 E-value: 7.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKS---YGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKN-------- 70
Cdd:COG4778 3 TLLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 71 ----VTSIRKKVLnktrneefGFVFQqfFMN------AKDTVLNnvllPLKIGGISGSKRKKMALDALKAVGLEDKV-QN 139
Cdd:COG4778 83 spreILALRRRTI--------GYVSQ--FLRviprvsALDVVAE----PLLERGVDREEARARARELLARLNLPERLwDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 140 KANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRD 218
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAvADRVVDVTP 227
|
.
gi 488286249 219 G 219
Cdd:COG4778 228 F 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-222 |
8.18e-29 |
|
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: 113.30 E-value: 8.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTR 83
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NeefgFVFQQFFMNAkDTVLNNVLLplkiggisGSKRKKMALDALKAV--------------GLEDKVQNKANNLSGGQK 149
Cdd:TIGR01193 551 N----YLPQEPYIFS-GSILENLLL--------GAKENVSQDEIWAACeiaeikddienmplGYQTELSEEGSSISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-207 |
8.89e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.08 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSY-GKNetkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI--RKKVL 79
Cdd:PRK11607 19 LLEIRNLTKSFdGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 NktrneefgFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:PRK11607 94 N--------MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLA 207
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-222 |
9.64e-29 |
|
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: 107.45 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtr 83
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVFQQFFMNAKDTVLNNVLLplkIGGISGSKRK--KMALDAL-KAVGLEDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:cd03266 80 ---LGFVSDSTGLYDRLTARENLEY---FAGLYGLKGDelTARLEELaDRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 161 NPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-221 |
1.02e-28 |
|
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: 107.63 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirKKVLNKTR 83
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT---KLPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHD-PDLAARCDRQVHVRDGLI 221
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNvRETLSITDRAYIIYEGKV 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-209 |
1.39e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 108.33 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQ--PT---SGDIYLNGKNV------ 71
Cdd:PRK14243 10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyapdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 72 -TSIRKKVlnktrneefGFVFQQFFMNAKdTVLNNVLLPLKIGGISGSkRKKMALDALKAVGLEDKVQNKAN----NLSG 146
Cdd:PRK14243 86 pVEVRRRI---------GMVFQKPNPFPK-SIYDNIAYGARINGYKGD-MDELVERSLRQAALWDEVKDKLKqsglSLSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 147 GQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAAR 209
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-222 |
1.95e-28 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 112.12 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvLNKTR 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRDR--PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEeFGFVFQQFFMnAKDTVLNNVllplKIGGISGSKRKKMaLDALKAVGLEDKVQN-----------KANNLSGGQKQRV 152
Cdd:TIGR02203 406 RQ-VALVSQDVVL-FNDTIANNI----AYGRTEQADRAEI-ERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-203 |
3.46e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.04 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTS-----GDIYLNGKNVTSiRKKV 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 LNKTRnEEFGFVFQQ---FFMnakdTVLNNVLLPLKIGGIsgskRKKMALD-----ALKAVGLEDKVQNK----ANNLSG 146
Cdd:PRK14258 83 LNRLR-RQVSMVHPKpnlFPM----SVYDNVAYGVKIVGW----RPKLEIDdivesALKDADLWDEIKHKihksALDLSG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 147 GQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
5.52e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.32 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT- 82
Cdd:COG4604 2 IEIKNVSKRYGGKVV----LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 ---RneefgfvfQQFFMNAKDTVLNNVLL---PLKIGGISGSKRKKMAlDALKAVGLEDkVQNK-ANNLSGGQKQRVCIA 155
Cdd:COG4604 78 ailR--------QENHINSRLTVRELVAFgrfPYSKGRLTAEDREIID-EAIAYLDLED-LADRyLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-222 |
8.42e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNeeFGFVFQ----QFFmn 97
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRES--VGMVFQdpdnQLF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 aKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSA 177
Cdd:PRK13636 97 -SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286249 178 TGKKIEELLFDLNKNKGITLIIVTHDPDLAA-RCDRQVHVRDGLIV 222
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVI 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-222 |
9.46e-28 |
|
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: 109.84 E-value: 9.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTrneeFGFVFQ--QFFmnaKD 100
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQdvELF---DG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVLNNvllplkI---GGISGSKrkkmALDALKAVGLEDKVQNKAN-----------NLSGGQKQRVCIARALVNNPQIIF 166
Cdd:COG4618 421 TIAEN------IarfGDADPEK----VVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 167 ADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-222 |
1.38e-27 |
|
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: 104.68 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLN 80
Cdd:COG0410 1 MPMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 K--------TRNeefgfVFQQFfmnakdTVLNNvllpLKIGGISGSKRKKMAlDALKAVG-----LEDKVQNKANNLSGG 147
Cdd:COG0410 77 RlgigyvpeGRR-----IFPSL------TVEEN----LLLGAYARRDRAEVR-ADLERVYelfprLKERRRQRAGTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTgnldsaTG------KKIEELLFDLNKnKGITLIIVTHDPDLAAR-CDRQVHVRDGL 220
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPS------LGlaplivEEIFEIIRRLNR-EGVTILLVEQNARFALEiADRAYVLERGR 213
|
..
gi 488286249 221 IV 222
Cdd:COG0410 214 IV 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-212 |
1.56e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNE-----------------TKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIY 65
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 66 LNGKNVTSIRKKVLNKtrneeFGFVF---QQFFMNakdtvlnnvlLPL--------KIGGISGSKRKKmALDALKAV-GL 133
Cdd:COG4586 81 VLGYVPFKRRKEFARR-----IGVVFgqrSQLWWD----------LPAidsfrllkAIYRIPDAEYKK-RLDELVELlDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 134 EDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDP-DLAARCDR 212
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMdDIEALCDR 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-222 |
1.68e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 104.53 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 5 EAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTS------IRKKV 78
Cdd:TIGR03410 2 EVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlppherARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktrneefGFVFQ--QFFmnAKDTVLNNVLLplkigGISGSKRKKMALD----ALKAVgLEDKVQNKANNLSGGQKQRV 152
Cdd:TIGR03410 78 ---------AYVPQgrEIF--PRLTVEENLLT-----GLAALPRRSRKIPdeiyELFPV-LKEMLGRRGGDLSGGQQQQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARC-DRQVHVRDGLIV 222
Cdd:TIGR03410 141 AIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELaDRYYVMERGRVV 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-222 |
3.24e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 108.66 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYgKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKt 82
Cdd:TIGR00958 478 LIEFQDVSFSY-PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rneEFGFVFQQFFMNAKdTVLNNVLLPLKiggisgSKRKKMALDALKAVGLEDKVQN-----------KANNLSGGQKQR 151
Cdd:TIGR00958 556 ---QVALVGQEPVLFSG-SVRENIAYGLT------DTPDEEIMAAAKAANAHDFIMEfpngydtevgeKGSQLSGGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 152 VCIARALVNNPQIIFADEPTGNLDSAtgkkIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-222 |
7.59e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.09 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 19 KFDALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILALLdQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQ----Q 93
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIqNINALL-KPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 94 FFmnaKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKAN-NLSGGQKQRVCIARALVNNPQIIFADEPTG 172
Cdd:PRK13646 98 LF---EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286249 173 NLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHV-RDGLIV 222
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVmKEGSIV 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-202 |
8.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQ----QFFmn 97
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpesQLF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 aKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKAN-NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDS 176
Cdd:PRK13643 99 -EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180
....*....|....*....|....*..
gi 488286249 177 ATgkKIEEL-LFDLNKNKGITLIIVTH 202
Cdd:PRK13643 178 KA--RIEMMqLFESIHQSGQTVVLVTH 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-209 |
1.46e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQ------PTSGDIYLNGKNVTSIRKKVLNKtrneEFGFVFQQFFM 96
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 97 NAKDTVLNNVLLPLKIGGISGSKR-KKMALDALKAVGL----EDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREiKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 488286249 172 GNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAAR 209
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVAR 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-219 |
1.54e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 6 AKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIylngknvtSIRKkvlnktrNE 85
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPK-------GL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 86 EFGFVFQQFFMNAKDTVLNNVLLPLK-----------------------------------IGGISGSKRKKMALDALka 130
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDGDAelraleaeleeleaklaepdedlerlaelqeefeaLGGWEAEARAEEILSGL-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 131 vGLEDKVQNKA-NNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLfdlnKNKGITLIIVTHDPD-LAA 208
Cdd:COG0488 140 -GFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDRYfLDR 214
|
250
....*....|.
gi 488286249 209 RCDRQVHVRDG 219
Cdd:COG0488 215 VATRILELDRG 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-216 |
1.87e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.48 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRnEEFGFVFQQFF--MNAK 99
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPYasLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNVLLPLKIGGI-SGSKRKKMALDALKAVGLE-DKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSA 177
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190
....*....|....*....|....*....|....*....
gi 488286249 178 TGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHV 216
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-215 |
2.31e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKvlnkTRNEEFGFVFQQ--FFmnaKD 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE----IYRQQVSYCAQTptLF---GD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVLNNVLLPLKIGGISgSKRKKMALDaLKAVGLEDKVQNKA-NNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATG 179
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQ-PDPAIFLDD-LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 488286249 180 KKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVH 215
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVIT 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-222 |
3.17e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.49 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlnKT 82
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------ED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RN------EEFGfvfqqffMNAKDTVLNNV--LLPLKigGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:COG4152 70 RRrigylpEERG-------LYPKMKVGEQLvyLARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEElCDRIVIINKGRKV 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-221 |
4.31e-26 |
|
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: 100.62 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYgKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNkt 82
Cdd:cd03248 11 IVKFQNVTFAY-PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rnEEFGFVFQQFFMNAKdTVLNNVLLPLkiGGISGSKRKKMALDA-------LKAVGLEDKVQNKANNLSGGQKQRVCIA 155
Cdd:cd03248 88 --SKVSLVGQEPVLFAR-SLQDNIAYGL--QSCSFECVKEAAQKAhahsfisELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-223 |
7.28e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.48 E-value: 7.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neEFGFVFQQFFMNAKDTVLNNV----LLPLKIGGISGSKRKKMALDA---LKAVGLEDKVQNKANNLSGGQKQRVCIAR 156
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLyigrHLTKKVCGVNIIDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 157 ALVNNPQIIFADEPTGNLdsaTGKKIEELLFDLN--KNKGITLIIVTHD-PDLAARCDRQVHVRDGLIVG 223
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKlAEIRRICDRYTVMKDGSSVC 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-201 |
8.95e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.02 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKF-----DALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkk 77
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 vlnktrnEEFGFVFQQFFMNAKD--TVLN------NVL-LPLKIG-GISGSKRKKMALDALKAVGL-EDKVQNKANNLSG 146
Cdd:PRK15112 80 -------GDYSYRSQRIRMIFQDpsTSLNprqrisQILdFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 147 GQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVT 201
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-204 |
1.21e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 99.65 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 21 DALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQP---TSGDIYLNGKNVTsiRKKVLnktrnEEFGFVFQQFFMN 97
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK--PDQFQ-----KCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 AKDTV------LNNVLLPLKIggiSGSKRKKMALD-ALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEP 170
Cdd:cd03234 94 PGLTVretltyTAILRLPRKS---SDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|....*
gi 488286249 171 TGNLDSATGKKIEELLFDLNKNKGItlIIVT-HDP 204
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRI--VILTiHQP 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYgknETKFDALKGVDLKVEKGESVAIIGKSGSGKST-FMHILALLdQPTSGDIYLNG-----KNVTSI 74
Cdd:PRK13652 1 MHLIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTlFRHFNGIL-KPTSGSVLIRGepitkENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 75 RKKVlnktrneefGFVFQ----QFFmnaKDTVLNNVLL-PLKIGgISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQK 149
Cdd:PRK13652 77 RKFV---------GLVFQnpddQIF---SPTVEQDIAFgPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRD-GLIVG 223
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDkGRIVA 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-222 |
2.50e-25 |
|
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: 99.10 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtr 83
Cdd:cd03252 1 ITFEHVRFRYKPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neEFGFVFQQffmnakdtvlnNVLLPLKIGGISGSKRKKMALDALKAV---------------GLEDKVQNKANNLSGGQ 148
Cdd:cd03252 77 --QVGVVLQE-----------NVLFNRSIRDNIALADPGMSMERVIEAaklagahdfiselpeGYDTIVGEQGAGLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-222 |
2.79e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKnETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirKKVLNKT 82
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA--ENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RneEFGFVFQQ---FFMNAkdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:PRK13642 81 R--KIGMVFQNpdnQFVGA--TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEII 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-222 |
4.65e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.40 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSY-GKNETkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNvtsIRKKVLNKT 82
Cdd:PRK11176 342 IEFRNVTFTYpGKEVP---ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEeFGFVFQQFFMnAKDTVLNNVLLPLK----IGGISGSKRKKMALDALKAV--GLEDKVQNKANNLSGGQKQRVCIAR 156
Cdd:PRK11176 416 RNQ-VALVSQNVHL-FNDTIANNIAYARTeqysREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-212 |
5.08e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.18 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKS-TFMHILALL--DQPTSGDIYLNGKNVTSIRKK 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLaaNGRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VLNKTRNEEFGFVFQ------QFFMNAKDTvLNNVLLPLKigGISGS----KRKKMaLDALKAVGLEDKVQNKANNLSGG 147
Cdd:PRK09473 90 ELNKLRAEQISMIFQdpmtslNPYMRVGEQ-LMEVLMLHK--GMSKAeafeESVRM-LDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPD-LAARCDR 212
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDK 231
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-202 |
6.00e-25 |
|
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: 97.85 E-value: 6.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNetkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsiRKKVlnktr 83
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT--RKDL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 nEEFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKrkkmALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:TIGR03740 70 -HKIGSLIESPPLYENLTARENLKVHTTLLGLPDSR----IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTH 202
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSF-PEQGITVILSSH 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-203 |
6.35e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.78 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEeFGFVFQQFF--MNAK 99
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQDPLasLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNVLLPLKI--GGISGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDS 176
Cdd:PRK15079 115 MTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180
....*....|....*....|....*..
gi 488286249 177 ATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-222 |
7.80e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 98.23 E-value: 7.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 24 KGVDLKVEKGESVAIIGKSGSGKStfMHILALLD------QPTSGDIYLNGKNV--TSIR-KKVLNKTRNEEFGFvfqqf 94
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVapCALRgRKIATIMQNPRSAF----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 95 fmNAKDTVLNNVLLPLKIGGISGSKRKkmALDALKAVGLEDK---VQNKANNLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:PRK10418 93 --NPLHTMHTHARETCLALGKPADDAT--LTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488286249 172 GNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRD-GLIV 222
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMShGRIV 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-219 |
1.76e-24 |
|
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: 99.02 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 26 VDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKnvtsirkkVLNKTRNEEF--------GFVFQqffmn 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE--------VLQDSARGIFlpphrrriGYVFQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 akD-------TVLNNVLLplkigGISGSKRKKMALDALKAV---GLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFA 167
Cdd:COG4148 85 --EarlfphlSVRGNLLY-----GRKRAPRAERRISFDEVVellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286249 168 DEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQG 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-219 |
2.46e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 93.67 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIylngknvtsirkkvlNKTR 83
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------TWGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQqffmnakdtvlnnvllplkiggisgskrkkmaldalkavgledkvqnkannLSGGQKQRVCIARALVNNPQ 163
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLfdlnKNKGITLIIVTHDPDLAAR-CDRQVHVRDG 219
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-222 |
3.43e-24 |
|
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: 95.68 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSY------------------GKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIY 65
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 66 LNGKnVTSIrkkvlnktrneeFGFvfqQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLS 145
Cdd:cd03220 81 VRGR-VSSL------------LGL---GGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 146 GGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-222 |
3.50e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 96.44 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETKFDalkgVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKN--------VTS 73
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRD----VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 74 IRKKVLNKTrneEFGFVFQqffmNAKDTVLNNVLL-------PLKIGGISGSKRKKMALDALKAVGLE-DKVQNKANNLS 145
Cdd:TIGR02323 78 AERRRLMRT---EWGFVHQ----NPRDGLRMRVSAganigerLMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 146 GGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAA-RCDRQVHVRDGLIV 222
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-216 |
3.82e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.95 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 20 FDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI-----------RKkvlnktrneefg 88
Cdd:COG4674 23 FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLdeheiarlgigRK------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 89 F----VFQQFfmnakdTVLNNVLLPLKIG---------GISGSKRKKMAlDALKAVGLEDKVQNKANNLSGGQKQRVCIA 155
Cdd:COG4674 91 FqkptVFEEL------TVFENLELALKGDrgvfaslfaRLTAEERDRIE-EVLETIGLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHV 216
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-222 |
5.73e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.32 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 37 AIIGKSGSGKSTFMHILALLDQPTSG-----DIYLNGKNVTSIRKKVLNKTRneeFGFVFQQ---FFMNAKDTVLNNV-- 106
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRR---VGMLFQRpnpFPMSIMDNVLAGVra 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 107 --LLPLK-IGGISGSKRKKMAL-DALKavgleDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKI 182
Cdd:PRK14271 128 hkLVPRKeFRGVAQARLTEVGLwDAVK-----DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488286249 183 EELLFDLNKNkgITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK14271 203 EEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLV 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
5.93e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MA-VIEAKNIKKSY------------------GKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTS 61
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 62 GDIYLNGKnVTSIrkkvLnktrneEFGFVFQQFFmnakdTVLNNVLLplkIGGISGSKRKKMAlDALKAV----GLEDKV 137
Cdd:COG1134 81 GRVEVNGR-VSAL----L------ELGAGFHPEL-----TGRENIYL---NGRLLGLSRKEID-EKFDEIvefaELGDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 138 QNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHV 216
Cdd:COG1134 141 DQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRAIWL 219
|
....*.
gi 488286249 217 RDGLIV 222
Cdd:COG1134 220 EKGRLV 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-212 |
7.45e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTS----IRKK 77
Cdd:PRK13537 6 APIDFRNVEKRYGDKLV----VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSrarhARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VlnktrneefGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARA 157
Cdd:PRK13537 82 V---------GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDR 212
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERlCDR 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-203 |
1.23e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.06 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI-RKKVLNKtrneefGFV--FQQFFMNA 98
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARM------GVVrtFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 99 KDTVLNNVLLP----LKIGGISG---------SKRKKMALDA--LKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQ 163
Cdd:PRK11300 94 EMTVIENLLVAqhqqLKTGLFSGllktpafrrAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-219 |
1.45e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.96 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGknvtsiRKKVLnktrneefgFVFQQFFMNAkDTV 102
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA------GARVL---------FLPQRPYLPL-GTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNVLLPLKIGGISgskrKKMALDALKAVGLE------DKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDS 176
Cdd:COG4178 443 REALLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488286249 177 ATGKKIEELLfdLNKNKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:COG4178 519 ENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-203 |
3.96e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.06 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 26 VDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRnEEFGFVFQQFFMNAKDTVLNN 105
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 106 VLLPLKI-GGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEE 184
Cdd:PRK11831 105 VAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170
....*....|....*....
gi 488286249 185 LLFDLNKNKGITLIIVTHD 203
Cdd:PRK11831 185 LISELNSALGVTCVVVSHD 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-203 |
4.34e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 25 GVDLKVEKGESVAIIGKSGSGKS-TFMHILALLDQP----TSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQQ--FFMN 97
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 AKDTV---LNNVLLpLKIGGISGSKRKKMaLDALKAVGLEDKVQNKAN---NLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:PRK15134 107 PLHTLekqLYEVLS-LHRGMRREAARGEI-LNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190
....*....|....*....|....*....|..
gi 488286249 172 GNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-222 |
5.37e-23 |
|
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: 92.09 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvLNKTR 83
Cdd:cd03369 7 IEVENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEeFGFVFQQ--FFMNakdTVLNNVllplkigGISGSKRKKMALDALKavgledkVQNKANNLSGGQKQRVCIARALVNN 161
Cdd:cd03369 82 SS-LTIIPQDptLFSG---TIRSNL-------DPFDEYSDEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 162 PQIIFADEPTGNLDSATGKKIEELLFDLNKNkgITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-221 |
1.08e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 95.49 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIkkSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKT 82
Cdd:TIGR01842 316 HLSVENV--TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rneeFGFVFQ--QFFmnaKDTVLNNV------LLPLKIggisgskrkkmaLDALKAVGLEDKVQNKAN-----------N 143
Cdd:TIGR01842 394 ----IGYLPQdvELF---PGTVAENIarfgenADPEKI------------IEAAKLAGVHELILRLPDgydtvigpggaT 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 144 LSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-223 |
1.56e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.70 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 21 DALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT------SIRKKV--LNKTRNEEfGFVFQ 92
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAGIayVPEDRKGE-GLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 93 QffmnakdTVLNNVLLPL-----KIGGISGSKRKKMALDA-----LKAVGLEDKVQnkanNLSGGQKQRVCIARALVNNP 162
Cdd:COG1129 345 L-------SIRENITLASldrlsRGGLLDRRRERALAEEYikrlrIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHD-PDLAARCDRQVHVRDGLIVG 223
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSElPELLGLSDRILVMREGRIVG 474
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-204 |
1.64e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQP---TSGDIYLNGKNVTSIRKKVLNktrneefGFVFQQ--FF-- 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS-------AYVQQDdlFIpt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 96 MNAKDTVLNNVLLPLKiGGISGSKRKKMALDALKAVGLED------KVQNKANNLSGGQKQRVCIARALVNNPQIIFADE 169
Cdd:TIGR00955 114 LTVREHLMFQAHLRMP-RRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190
....*....|....*....|....*....|....*
gi 488286249 170 PTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDP 204
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQP 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-225 |
2.00e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 33 GESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKtrneEFGFVFQQFFMNAKDTVLNNVllplKI 112
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEGMTVRELV----AI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 113 G--------GISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEE 184
Cdd:PRK10575 109 GrypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488286249 185 LLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDG-LIVGGD 225
Cdd:PRK10575 189 LVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGeMIAQGT 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-222 |
2.14e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 6 AKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKN--------VTSIRKK 77
Cdd:PRK11701 9 VRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyaLSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VLNKTrneEFGFVFQqffmNAKD------TVLNNVLLPLKIGGIS--GSKRKKmALDALKAVGLE-DKVQNKANNLSGGQ 148
Cdd:PRK11701 85 RLLRT---EWGFVHQ----HPRDglrmqvSAGGNIGERLMAVGARhyGDIRAT-AGDWLERVEIDaARIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHdpDLA-AR--CDRQVHVRDGLIV 222
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH--DLAvARllAHRLLVMKQGRVV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-222 |
2.68e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMhiLALLDQ-PTSGDIYLNGKNVTSIRKKVLNKTRNEeFGFVFQQFF--MNA 98
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTG--LALLRLiNSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 99 KDTVLNNVLLPLKI--GGISGSKRKKMALDALKAVGLEDKVQNK-ANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLD 175
Cdd:PRK15134 378 RLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286249 176 SATGKKIEELLFDLNKNKGITLIIVTHDPDLA-ARCDRQVHVRDGLIV 222
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEVV 505
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-204 |
5.33e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVtsirkkvlnktrneEFGFVFQQF-------F 95
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--------------DDPDVAEAChylghrnA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 96 MNAKDTVLNNVLLPLKIGGISGSkrkkMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLD 175
Cdd:PRK13539 84 MKPALTVAENLEFWAAFLGGEEL----DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|
gi 488286249 176 SATGKKIEELLFD-LNKNkGItLIIVTHDP 204
Cdd:PRK13539 160 AAAVALFAELIRAhLAQG-GI-VIAATHIP 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-223 |
5.40e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHIL-ALLDQPT-SGDIYLNGKNVT--SIRK 76
Cdd:PRK13549 3 EYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsGVYPHGTyEGEIIFEGEELQasNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 kvlnktrNEEFGFV-FQQFFMNAKD-TVLNNVLLPLKI--GGIsgSKRKKMALDA---LKAVGLEDKVQNKANNLSGGQK 149
Cdd:PRK13549 79 -------TERAGIAiIHQELALVKElSVLENIFLGNEItpGGI--MDYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLdsaTGKKIEELL---FDLnKNKGITLIIVTHDPD-LAARCDRQVHVRDGLIVG 223
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASL---TESETAVLLdiiRDL-KAHGIACIYISHKLNeVKAISDTICVIRDGRHIG 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-199 |
6.18e-22 |
|
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: 93.35 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTfmhILALL----DqPTSGDIYLNGKNVTSIRKKVLNKTrneeFGFVFQqffmna 98
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKST---LARLLfrfyD-VTSGRILIDGQDIRDVTQASLRAA----IGIVPQ------ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 99 kDTVLNNVLLPLKIG-GISGSKRKKMAlDALKAVGLEDKVQN--------------KannLSGGQKQRVCIARALVNNPQ 163
Cdd:COG5265 440 -DTVLFNDTIAYNIAyGRPDASEEEVE-AAARAAQIHDFIESlpdgydtrvgerglK---LSGGEKQRVAIARTLLKNPP 514
|
170 180 190
....*....|....*....|....*....|....*.
gi 488286249 164 IIFADEPTGNLDSATGKKIEELLFDLNKNKgITLII 199
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGR-TTLVI 549
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-222 |
9.13e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVtsirKKVLNK 81
Cdd:PRK10253 6 ARLRGEQLTLGYGK----YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI----QHYASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEEFGFVFQQFFMNAKDTVLNNVL---LPLKIGGISGSKRKKMALD-ALKAVGLEDKVQNKANNLSGGQKQRVCIARA 157
Cdd:PRK10253 78 EVARRIGLLAQNATTPGDITVQELVArgrYPHQPLFTRWRKEDEEAVTkAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIV 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
1.89e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirKKVLN 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAV----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRneeFGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:PRK13536 113 RAR---IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286249 161 NPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDR 212
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERlCDR 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-219 |
2.00e-21 |
|
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: 87.10 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 21 DALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT--SIRKKVLnktrneefgfvfqqffmna 98
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrSPRDAIR------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 99 kdtvlnnvllpLKIGGISGSkRKKMALdalkaVGLEDKVQNKANN--LSGGQKQRVCIARALVNNPQIIFADEPTGNLDS 176
Cdd:cd03215 75 -----------AGIAYVPED-RKREGL-----VLDLSVAENIALSslLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488286249 177 ATGKKIEELLFDLnKNKGITLIIVTHD-PDLAARCDRQVHVRDG 219
Cdd:cd03215 138 GAKAEIYRLIREL-ADAGKAVLLISSElDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-216 |
4.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 8 NIKKSYGKNET-KFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHIL-ALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNE 85
Cdd:PRK13645 11 NVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGQTIVGDYAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 86 EFGFVFQ----QFFmnaKDTVLNNVLL-PLKIGGISGSKRKKMAlDALKAVGL-EDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:PRK13645 91 EIGLVFQfpeyQLF---QETIEKDIAFgPVNLGENKQEAYKKVP-ELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHV 216
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-222 |
5.79e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvLNKT 82
Cdd:PRK15439 11 LLCARSISKQYSGVEV----LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-----LTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEEFG--FVFQQFFMNAKDTVLNNVLLPLKigGISGSKRKKMALdaLKAVGLEDKVQNKANNLSGGQKQRVCIARALVN 160
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENILFGLP--KRQASMQKMKQL--LAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 161 NPQIIFADEPTGNLDSATG----KKIEELLfdlnkNKGITLIIVTHD-PDLAARCDRQVHVRDGLIV 222
Cdd:PRK15439 158 DSRILILDEPTASLTPAETerlfSRIRELL-----AQGVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-202 |
6.35e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 90.55 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNEtkfDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVfQQFFMNAKDTVLNNVLLPLKIGgisgskrKKMALDALKAV-----------GLEDKVQNKANNLSGGQKQRV 152
Cdd:PRK10790 417 ---VAMV-QQDPVVLADTFLANVTLGRDIS-------EEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTH 202
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAH 533
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-199 |
1.39e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.64 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTrneeFGFVFQQFFMNAKdT 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN----IAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNvllpLKIGGISGSKRKKM-------ALD--ALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTG 172
Cdd:PRK13657 425 IEDN----IRVGRPDATDEEMRaaaeraqAHDfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180
....*....|....*....|....*..
gi 488286249 173 NLDSATGKKIEELLFDLNKNKgITLII 199
Cdd:PRK13657 501 ALDVETEAKVKAALDELMKGR-TTFII 526
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-219 |
1.63e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 89.26 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNetKFdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlnKTR 83
Cdd:PRK10522 323 LELRNVTFAYQDN--GF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-------EQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEefgfvFQQFFmnakDTVLNNVLLPLKIGGISGSKRKKMALDA-LKAVGLEDKVQNKAN-----NLSGGQKQRVCIARA 157
Cdd:PRK10522 393 ED-----YRKLF----SAVFTDFHLFDQLLGPEGKPANPALVEKwLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-202 |
1.89e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYG-KNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSG-----DIYLNGKNVTSIRK 76
Cdd:PRK13631 21 ILRVKNLYCVFDeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVLNKTRNEEF-------GFVFQ----QFFmnaKDTVLNNVLL-PLKIGgISGSKRKKMALDALKAVGLEDKVQNKAN-N 143
Cdd:PRK13631 101 TNPYSKKIKNFkelrrrvSMVFQfpeyQLF---KDTIEKDIMFgPVALG-VKKSEAKKLAKFYLNKMGLDDSYLERSPfG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 144 LSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDlNKNKGITLIIVTH 202
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITH 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-222 |
4.16e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.45 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTr 83
Cdd:PRK11231 3 LRTENLTVGYGTKRI----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 neeFGFVFQQFFMNAKDTVLNNV------LLPLkIGGISGSKRKKMAlDALKAVGLEDKVQNKANNLSGGQKQRVCIARA 157
Cdd:PRK11231 78 ---LALLPQHHLTPEGITVRELVaygrspWLSL-WGRLSAEDNARVN-QAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 158 LVNNPQIIFADEPTGNLDSATGKKIEELLFDLNkNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRyCDHLVVLANGHVM 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-204 |
6.75e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.56 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKvlnktRNEEFGFVFQQFFMNAKDT 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLPLKIGGISgskrKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKK 181
Cdd:TIGR01189 90 ALENLHFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|...
gi 488286249 182 IEELLFDLNKNKGITlIIVTHDP 204
Cdd:TIGR01189 166 LAGLLRAHLARGGIV-LLTTHQD 187
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-222 |
9.28e-20 |
|
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: 87.16 E-value: 9.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 26 VDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlnKTRN---EEFGFVFQQF--FmnakD 100
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-------DNREayrQLFSAVFSDFhlF----D 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVLnnvllplkigGISGSKRKKMALDALKAVGLEDKVQNKAN-----NLSGGQKQRVCIARALVNNPQIIFADE------ 169
Cdd:COG4615 420 RLL----------GLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDEwaadqd 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 170 PtgnldsaTGKKI--EELLFDLnKNKGITLIIVTHDP---DLAarcDRQVHVRDGLIV 222
Cdd:COG4615 490 P-------EFRRVfyTELLPEL-KARGKTVIAISHDDryfDLA---DRVLKMDYGKLV 536
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-222 |
9.71e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.21 E-value: 9.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKN--IKKSYGKNetkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLdqPTSGDIYLNGK-----NVTSIR 75
Cdd:PRK11174 350 IEAEDleILSPDGKT-----LAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIelrelDPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKVlnktrneefGFVFQ--QFFmnaKDTVLNNVLLplkiGGISGSKRK-KMALDALKA--------VGLEDKVQNKANNL 144
Cdd:PRK11174 423 KHL---------SWVGQnpQLP---HGTLRDNVLL----GNPDASDEQlQQALENAWVseflpllpQGLDTPIGDQAAGL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 145 SGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-219 |
1.38e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSY-GKNetkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKnvtsirkkvl 79
Cdd:PRK11288 2 SPYLSFDGIGKTFpGVK-----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 nktrneefgfvfQQFFMNAKD-------------------TVLNNVLL---PLKIGGISGSKRKKMALDALKAVGLEDKV 137
Cdd:PRK11288 67 ------------EMRFASTTAalaagvaiiyqelhlvpemTVAENLYLgqlPHKGGIVNRRLLNYEAREQLEHLGVDIDP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 138 QNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSatgKKIEEL--LFDLNKNKGITLIIVTHDPD-LAARCDRQV 214
Cdd:PRK11288 135 DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA---REIEQLfrVIRELRAEGRVILYVSHRMEeIFALCDAIT 211
|
....*
gi 488286249 215 HVRDG 219
Cdd:PRK11288 212 VFKDG 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-206 |
1.59e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.08 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIkksyGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHIL--ALLDQPTSGDIYLNGKNVTSirkkv 78
Cdd:COG2401 28 AIVLEAFGV----ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGR----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktrneefgfvfqqffmnaKDTVLNNVllplkigGISGSKrkKMALDALKAVGLEDKVQNKA--NNLSGGQKQRVCIAR 156
Cdd:COG2401 99 --------------------EASLIDAI-------GRKGDF--KDAVELLNAVGLSDAVLWLRrfKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDL 206
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-219 |
3.72e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 82.38 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMhiLALLD--QPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQQ-FFMNAk 99
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGemQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKpWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 dTVLNNVLLplkiGGISGSKRKKMALDA--------LKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:cd03290 94 -TVEENITF----GSPFNKQRYKAVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488286249 172 GNLD-SATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:cd03290 169 SALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-212 |
4.08e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.56 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT----SIRKKV 78
Cdd:NF033858 266 AIEARGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagdiATRRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnktrneefGFVFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARAL 158
Cdd:NF033858 342 ---------GYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAV 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDR 212
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDR 466
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-204 |
4.42e-19 |
|
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: 81.77 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVlnktrNEEFGFVFQQFFMNAKDTV 102
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNVLLPLKIGGISGskrkkmALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKI 182
Cdd:cd03231 91 LENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|..
gi 488286249 183 EELLFDLNKNKGItLIIVTHDP 204
Cdd:cd03231 165 AEAMAGHCARGGM-VVLTTHQD 185
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-222 |
5.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNG------KNVTSIRKKVlnktrneefGFVFQ--- 92
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLV---------GIVFQnpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 93 -QFFMNAKDTVL-----NNVLLPLKIggisgskrKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIF 166
Cdd:PRK13644 88 tQFVGRTVEEDLafgpeNLCLPPIEI--------RKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 167 ADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-226 |
9.95e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLD--QPTSGDIYLNGKNVTSI------RKKVlnktrneefGFVFQQ- 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELspderaRAGI---------FLAFQYp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 94 ---------FFMNakdTVLNNVLLPLkiggISGSKRKKMALDALKAVGLEDKVQNKANN--LSGGQKQRVCIARALVNNP 162
Cdd:COG0396 87 veipgvsvsNFLR---TALNARRGEE----LSAREFLKLLKEKMKELGLDEDFLDRYVNegFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 163 QIIFADEPTGNLD----SATGKKIEELlfdlnKNKGITLIIVTH--------DPDlaarcdrQVHV-RDGLIV--GGDE 226
Cdd:COG0396 160 KLAILDETDSGLDidalRIVAEGVNKL-----RSPDRGILIITHyqrildyiKPD-------FVHVlVDGRIVksGGKE 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-224 |
7.56e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvLN 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRV----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRNEEFGFVFQQFFMNAKDTVLNNVLLPLKI-GGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHD-PDLAARCDRQVHVRDG-LIVGG 224
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNvRETLAVCERAYIVSQGhLIAHG 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-223 |
7.97e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.41 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLdQPT---SGDIYLNGKnvtSIRKKVL 79
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGS---PLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 NKTRNEEFGFVFQQFFMNAKDTVLNNVLLPLKI---GGIsgskrkkMALDA--LKAVGLEDKVQNKANN-------LSGG 147
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLGNEItlpGGR-------MAYNAmyLRAKNLLRELQLDADNvtrpvgdYGGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPD-LAARCDRQVHVRDGLIVG 223
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNeVKAVCDTICVIRDGQHVA 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-222 |
1.07e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.49 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALlDQPTS---------GDIYLNGKNVTSI-------RKKVLNKTRNEE 86
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIdaprlarLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 87 FGFvfqqffmNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVN------ 160
Cdd:PRK13547 96 FAF-------SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 161 ---NPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIV 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
1.13e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLN 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTV----LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 ktrneefgfvfQQFFMNAKDTVLN---NVLLPLKIG--------GISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQK 149
Cdd:PRK09536 77 -----------RRVASVPQDTSLSfefDVRQVVEMGrtphrsrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286249 150 QRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLI 221
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARyCDELVLLADGRV 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-203 |
1.22e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKS-TFMHILALLDQP----TSGDIYLNGKNVTSIR-- 75
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSRQVIEls 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 ---KKVLNKTRNEEFGFVFQQFFmnakdTVLNNVL-----------LPLKIGGISGSKRKKMALDALKAVGLEDKVQNKA 141
Cdd:PRK10261 92 eqsAAQMRHVRGADMAMIFQEPM-----TSLNPVFtvgeqiaesirLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 142 NNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-215 |
1.60e-17 |
|
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: 76.42 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYlngknvtsirkkvlnKTRNEEFGFVFQQFFMNAkDTV 102
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------------MPEGEDLLFLPQRPYLPL-GTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNVLLPLkiggisgskrkkmaldalkavgleDKVqnkannLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATgkki 182
Cdd:cd03223 81 REQLIYPW------------------------DDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES---- 126
|
170 180 190
....*....|....*....|....*....|...
gi 488286249 183 EELLFDLNKNKGITLIIVTHDPDLAARCDRQVH 215
Cdd:cd03223 127 EDRLYQLLKELGITVISVGHRPSLWKFHDRVLD 159
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-203 |
6.25e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.02 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLD---QPTSGDIYLNGKNVTSI----RKKVLNKtrneEFGFVFQ- 92
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLspreRRKIIGR----EIAMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 93 -QFFMNAKDTVLNNVLLPLKIGGISGS------KRKKMALDALKAVGLED--KVQNK-ANNLSGGQKQRVCIARALVNNP 162
Cdd:COG4170 98 pSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfkWRKKRAIELLHRVGIKDhkDIMNSyPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488286249 163 QIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-221 |
9.73e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSygknetKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT------SIRK 76
Cdd:PRK09700 265 VFEVRNVTSR------DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVLNKTRNE-EFGFvFQQFFMNAKDTVLNNvllpLKIGGISG-------SKRKKMALDALKAVGLE-DKVQNKANNLSGG 147
Cdd:PRK09700 339 GMAYITESRrDNGF-FPNFSIAQNMAISRS----LKDGGYKGamglfheVDEQRTAENQRELLALKcHSVNQNITELSGG 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHD-PDLAARCDRQVHVRDGLI 221
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-226 |
1.64e-16 |
|
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: 74.87 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLD--QPTSGDIYLNGKNVTsirkkvlNKTRNEEF----GFVFQQffm 96
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT-------DLPPEERArlgiFLAFQY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 97 nakdtvlnnvllPLKIGGISgskrkkmaldalkavgLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLD- 175
Cdd:cd03217 86 ------------PPEIPGVK----------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDi 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 176 ---SATGKKIEELlfdlnKNKGITLIIVTHDPDLAA--RCDRqVHV-RDGLIV--GGDE 226
Cdd:cd03217 138 dalRLVAEVINKL-----REEGKSVLIITHYQRLLDyiKPDR-VHVlYDGRIVksGDKE 190
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
3.98e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKnetkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKvln 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRNEEFGFVFQQFFMNAKDTVLNNvllpLKIGGISGSK-----RKKMALDALKAVgLEDKVQnKANNLSGGQKQRVCIA 155
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEEN----LAMGGFFAERdqfqeRIKWVYELFPRL-HERRIQ-RAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAAR-CDRQVHVRDGLIV 222
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-203 |
8.28e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGdiylngknvtsirkkVLNKT 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRV----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG---------------VIKRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEEFGFVFQQFFMNAKdtvlnnvlLPLKIGG---ISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:PRK09544 65 GKLRIGYVPQKLYLDTT--------LPLTVNRflrLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHD 203
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-224 |
1.07e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKK--VLNKTRNEEFGFVFQQFfmnAK 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEVDWSFPVL---VE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATG 179
Cdd:PRK15056 99 DVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286249 180 KKIEELLFDLnKNKGITLIIVTHD-PDLAARCDRQVHVRDGLIVGG 224
Cdd:PRK15056 179 ARIISLLREL-RDEGKTMLVSTHNlGSVTEFCDYTVMVKGTVLASG 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-202 |
1.08e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYG--KnetkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLdQPT---SGDIYLNGKNVT--SIR 75
Cdd:NF040905 1 ILEMRGITKTFPgvK------ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRfkDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KkvlnktrNEEFGFVF--QQFFMNAKDTVLNNVLL---PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQ 150
Cdd:NF040905 74 D-------SEALGIVIihQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488286249 151 RVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTH 202
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-207 |
1.09e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.44 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkVLNKTRnEEFGFVFQQFFMNAKDT 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVR-QSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKK 181
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180
....*....|....*....|....*.
gi 488286249 182 IEELLfdLNKNKGITLIIVTHDPDLA 207
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEA 1123
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-204 |
1.28e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 8 NIKKSYGKNETKFDA---------LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTS--GDIYLNGKNVTsirK 76
Cdd:PLN03211 60 NIKRILGHKPKISDEtrqiqertiLNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT---K 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 77 KVLNKTrneefGFVFQQFFM----NAKDTVLNNVLLPLKiGGISGSKRKKMALDALKAVGLEdKVQNKA------NNLSG 146
Cdd:PLN03211 137 QILKRT-----GFVTQDDILyphlTVRETLVFCSLLRLP-KSLTKQEKILVAESVISELGLT-KCENTIignsfiRGISG 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 147 GQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDP 204
Cdd:PLN03211 210 GERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQP 266
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-225 |
1.59e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLdQPTSGDIYLNGKNVTSIRKKVLNKTRneefGFVFQQ----FFMna 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQQqsppFAM-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 99 kdTVLNnvLLPLKIGGISGSKRKKMALDAL-KAVGLEDKVQNKANNLSGGQKQRVCIARALV-----NNP--QIIFADEP 170
Cdd:COG4138 85 --PVFQ--YLALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 171 TGNLD----SATGKKIEELlfdlnKNKGITLIIVTHDPDLAAR-CDRQVHVRDG-LIVGGD 225
Cdd:COG4138 161 MNSLDvaqqAALDRLLREL-----CQQGITVVMSSHDLNHTLRhADRVWLLKQGkLVASGE 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-222 |
7.42e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILAllDQP----TSGDIYLNGKNVTSIRKkv 78
Cdd:CHL00131 7 ILEIKNLHASVNENEI----LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 lnKTRNEEFGFVFQQFfmnakdtvlnnvllPLKIGGISG---------SKRKKMAL-------------DALKAVGLEDK 136
Cdd:CHL00131 79 --EERAHLGIFLAFQY--------------PIEIPGVSNadflrlaynSKRKFQGLpeldplefleiinEKLKLVGMDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 137 VQNKANN--LSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDL-NKNKGItlIIVTH--------DPD 205
Cdd:CHL00131 143 FLSRNVNegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmTSENSI--ILITHyqrlldyiKPD 220
|
250
....*....|....*...
gi 488286249 206 LaarcdrqVHV-RDGLIV 222
Cdd:CHL00131 221 Y-------VHVmQNGKII 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-175 |
1.13e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 12 SYGKNETKFdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirkkvlNKTRNEEFGFVF 91
Cdd:PRK13543 18 AFSRNEEPV--FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-------RGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 92 QQFFMNAKDTVLNNVLLplkIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:PRK13543 89 HLPGLKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....
gi 488286249 172 GNLD 175
Cdd:PRK13543 166 ANLD 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-202 |
1.17e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.83 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 20 FDALkgvDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvlnktrnEEFgfvFQQFF---- 95
Cdd:PRK13538 17 FSGL---SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR---------DEY---HQDLLylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 96 MNA-KD--TVLNNVLLPLKIGGISGSKRkkmALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTG 172
Cdd:PRK13538 82 QPGiKTelTALENLRFYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|
gi 488286249 173 NLDSATGKKIEElLFDLNKNKGITLIIVTH 202
Cdd:PRK13538 159 AIDKQGVARLEA-LLAQHAEQGGMVILTTH 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-222 |
1.25e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.50 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHilALLDQ--PTSGDIYlngknvtsirkkvlnktRNEEFGFVFQQ-FFMNAk 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLLSQfeISEGRVW-----------------AERSIAYVPQQaWIMNA- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 dTVLNNVLL--PLKIGGISGSKR-KKMALD-ALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLD 175
Cdd:PTZ00243 736 -TVRGNILFfdEEDAARLADAVRvSQLEADlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488286249 176 SATGKKIEELLFdLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLIV 222
Cdd:PTZ00243 815 AHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-221 |
1.44e-14 |
|
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: 72.29 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDA-----------LKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLDQpTSGDIYLNGknv 71
Cdd:TIGR00957 624 IERRTIKPGEGNSITVHNAtftwardlpptLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 72 tsirkkvlnktrneEFGFVFQQFFMNaKDTVLNNVLLplkiGGISGSKRKKMALDALKAV--------GLEDKVQNKANN 143
Cdd:TIGR00957 700 --------------SVAYVPQQAWIQ-NDSLRENILF----GKALNEKYYQQVLEACALLpdleilpsGDRTEIGEKGVN 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 144 LSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKI-EELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-216 |
1.77e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKST-FMHILALLdQPTSGDIYLNGKNVTSIRKKVLnkTRNEEFGFVFQ----QFFMN 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTlFMNLSGLL-RPQKGAVLWQGKPLDYSKRGLL--ALRQQVATVFQdpeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 AKDTvlnNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSA 177
Cdd:PRK13638 94 DIDS---DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 488286249 178 TGKKIEELLFDLnKNKGITLIIVTHDPDLAARCDRQVHV 216
Cdd:PRK13638 171 GRTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYV 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-175 |
2.02e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 37 AIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQQFFMNAKDTVLNNvllpLKIGgis 116
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGN----LRYG--- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 117 gsKRKKMALDALKAV---GLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLD 175
Cdd:PRK11144 101 --MAKSMVAQFDKIVallGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-203 |
2.25e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 30 VEKGESVAIIGKSGSGKSTFMHILA-LLdqPTSGDIYLNGKNVTSIRKKVLNKTRneefGFVFQQ----FFMNakdtVLN 104
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAgLL--PGSGSIQFAGQPLEAWSAAELARHR----AYLSQQqtppFAMP----VFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 105 NVLLPLKIGGISGSKRKkmALDAL-KAVGLEDKVQNKANNLSGGQKQRVCIARAL-----VNNP--QIIFADEPTGNLDS 176
Cdd:PRK03695 89 YLTLHQPDKTRTEAVAS--ALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*..
gi 488286249 177 ATGKKIEELLFDLNKnKGITLIIVTHD 203
Cdd:PRK03695 167 AQQAALDRLLSELCQ-QGIAVVMSSHD 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-203 |
3.86e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGkNETKFDALkgvDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLnGKNVtsirkkvlnkt 82
Cdd:TIGR03719 322 VIEAENLTKAFG-DKLLIDDL---SFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rneEFGFVFQQF-FMNAKDTVLNNV---LLPLKIGGISGSKRKKMALDALKAVgleDKvQNKANNLSGGQKQRVCIARAL 158
Cdd:TIGR03719 386 ---KLAYVDQSRdALDPNKTVWEEIsggLDIIKLGKREIPSRAYVGRFNFKGS---DQ-QKKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELLFDLnknKGITLIIvTHD 203
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVI-SHD 499
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-202 |
4.68e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 21 DALKGVDLKVEKGESVAIIGKSGSGKSTfmhILALLDQP---TSGDIYLNGKNVTSIRkkvLNKTRNEeFGFVFQQFFMN 97
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKST---LLSLIQRHfdvSEGDIRFHDIPLTKLQ---LDSWRSR-LAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 AkDTVLNNVLLplkiGGISGSKRKKMALDALKAV---------GLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFAD 168
Cdd:PRK10789 402 S-DTVANNIAL----GRPDATQQEIEHVARLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190
....*....|....*....|....*....|....*
gi 488286249 169 EPTGNLDSATGKKIeelLFDLNK-NKGITLIIVTH 202
Cdd:PRK10789 477 DALSAVDGRTEHQI---LHNLRQwGEGRTVIISAH 508
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-223 |
5.46e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 15 KNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT--SIRKKVLNKT------RNEE 86
Cdd:COG3845 266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglSPRERRRLGVayipedRLGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 87 fGFVfqqffMNAkdTVLNNVLL------PLKIGG-ISGSKRKKMALDAL-----KAVGLEDKVQnkanNLSGGQKQRVCI 154
Cdd:COG3845 346 -GLV-----PDM--SVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIeefdvRTPGPDTPAR----SLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPD-LAARCDRqVHV-RDGLIVG 223
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDeILALSDR-IAVmYEGRIVG 482
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-202 |
5.84e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 7 KNIKKSYGKN-----ETKFDA--LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGK------NVTS 73
Cdd:PTZ00265 378 KDIKKIQFKNvrfhyDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdiNLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 74 IRKKV----------LNKTRN-------------------EEFGFVFQQFfMNAKDTV-------LNNVLLPLKIGGISG 117
Cdd:PTZ00265 458 WRSKIgvvsqdpllfSNSIKNnikyslyslkdlealsnyyNEDGNDSQEN-KNKRNSCrakcagdLNDMSNTTDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 118 SKRKKMALDALKAVGLEDKV-----------------QNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGK 180
Cdd:PTZ00265 537 MRKNYQTIKDSEVVDVSKKVlihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|..
gi 488286249 181 KIEELLFDLNKNKGITLIIVTH 202
Cdd:PTZ00265 617 LVQKTINNLKGNENRITIIIAH 638
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-203 |
6.99e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.59 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 7 KNIKKSYGKNETKFDALKGvdlKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirkkvlnktrnee 86
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 87 fgfvFQQFFMNAKDTVLNNVLLPLKIGGISGSKRKKMalDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIF 166
Cdd:cd03237 65 ----YKPQYIKADYEGTVRDLLSSITKDFYTHPYFKT--EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488286249 167 ADEPTGNLDS----ATGKKIEEllFDLNKNKgiTLIIVTHD 203
Cdd:cd03237 139 LDEPSAYLDVeqrlMASKVIRR--FAENNEK--TAFVVEHD 175
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-204 |
2.78e-13 |
|
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: 65.73 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILAL--LDQPTSGDIYLNGKNvtsirkkvLNKTRNEEFGFVFQQFFMNAKD 100
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRP--------LDKNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVLNNVLLPLKIGGISGSKRKkmaldalkavgledkvqnkannlsggqkqRVCIARALVNNPQIIFADEPTGNLDSATGK 180
Cdd:cd03232 95 TVREALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|....
gi 488286249 181 KIEELLFDLnKNKGITLIIVTHDP 204
Cdd:cd03232 146 NIVRFLKKL-ADSGQAILCTIHQP 168
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
120-203 |
5.97e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.75 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 120 RKKMALDALKAVGLEDK---VQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGIT 196
Cdd:PRK15093 132 RKRRAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTT 211
|
....*..
gi 488286249 197 LIIVTHD 203
Cdd:PRK15093 212 ILLISHD 218
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-206 |
6.71e-13 |
|
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: 67.08 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 30 VEKGESVAIIGKSGSGKSTFMHILA--------LLDQPTSGDI-YLNGK---NVTSIRKKVLNKTRNEEFgfvfqqFFMN 97
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLfYVPQRpymTLGTLRDQIIYPDSSEDM------KRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 98 AKDTVLNNVLLPLKIGGIsgskrkkmaldaLKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTgnldSA 177
Cdd:TIGR00954 549 LSDKDLEQILDNVQLTHI------------LEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT----SA 612
|
170 180
....*....|....*....|....*....
gi 488286249 178 TGKKIEELLFDLNKNKGITLIIVTHDPDL 206
Cdd:TIGR00954 613 VSVDVEGYMYRLCREFGITLFSVSHRKSL 641
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-212 |
7.88e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKS----TFMHILALldqpTSGDIYLNGKNVTSIRKKVLNktrneefgfvfQQFFMNA 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKStlllTFMRMVEV----CGGEIRVNGREIGAYGLRELR-----------RQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 99 KDTVLnnvllplkiggISGSKRKKmaLD------------ALKAVGL-----------EDKVQNKANNLSGGQKQRVCIA 155
Cdd:PTZ00243 1391 QDPVL-----------FDGTVRQN--VDpfleassaevwaALELVGLrervasesegiDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 156 RALVNNPQ-IIFADEPTGNLDSATGKKIEELLfdLNKNKGITLIIVTHDPDLAARCDR 212
Cdd:PTZ00243 1458 RALLKKGSgFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQYDK 1513
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-203 |
9.75e-13 |
|
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: 66.50 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLN-GKNVtsirkkvlnktrneefGFVFQQFFMNAKDT 101
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV----------------GYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLplkiggisGSKRKKMALDALKAVG-------------------LEDKVQN----------------------- 139
Cdd:TIGR03719 85 VRENVEE--------GVAEIKDALDRFNEISakyaepdadfdklaaeqaeLQEIIDAadawdldsqleiamdalrcppwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 140 -KANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnknKGiTLIIVTHD 203
Cdd:TIGR03719 157 aDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY---PG-TVVAVTHD 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-203 |
1.23e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGknetkfDA--LKGVDLKVEKGESVAIIGKSGSGKSTFMHILA---LLDQptsGDIYLNGKNVTSIR 75
Cdd:PRK11147 1 MSLISIHGAWLSFS------DAplLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYEQDLIVARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKvlNKTRNEEfGFVFqqffmnakDTVLNNV------------LLPLKIGGISGSKRKKMA-----LDALKAVGLEDKVQ 138
Cdd:PRK11147 72 QQ--DPPRNVE-GTVY--------DFVAEGIeeqaeylkryhdISHLVETDPSEKNLNELAklqeqLDHHNLWQLENRIN 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 139 N-----------KANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnknKGiTLIIVTHD 203
Cdd:PRK11147 141 EvlaqlgldpdaALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QG-SIIFISHD 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-203 |
4.46e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGkNETKFdalKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIylngknvtsirkkvlnK-T 82
Cdd:PRK15064 320 LEVENLTKGFD-NGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------------KwS 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RNEEFGFVFQ----QFfmnAKDTVLnnvllplkIGGISGSKRKKMALDALKAVgL------EDKVQNKANNLSGGQKQRV 152
Cdd:PRK15064 380 ENANIGYYAQdhayDF---ENDLTL--------FDWMSQWRQEGDDEQAVRGT-LgrllfsQDDIKKSVKVLSGGEKGRM 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSatgKKIEELLFDLNKNKGiTLIIVTHD 203
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEKYEG-TLIFVSHD 494
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-219 |
5.35e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGK--NVTSIRKKVLNKTrneefGFVFQQFFMNAK 99
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENGI-----SMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNVLL---PLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLds 176
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286249 177 aTGKKIEELLFDLNK--NKGITLIIVTHDPD-LAARCDRQVHVRDG 219
Cdd:PRK10982 166 -TEKEVNHLFTIIRKlkERGCGIVYISHKMEeIFQLCDEITILRDG 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-203 |
1.05e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGknetkfdalkGVDLKVE-----KGESVAIIGKSGSGKSTFMHILALLDQPTSGDIylngknvtSIRKK 77
Cdd:PRK13409 340 LVEYPDLTKKLG----------DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VLNK---TRNEEFGFVfQQFFMNAKDTVLNNVLLPlkiggisgskrkkmalDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:PRK13409 402 ISYKpqyIKPDYDGTV-EDLLRSITDDLGSSYYKS----------------EIIKPLQLERLLDKNVKDLSGGELQRVAI 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286249 155 ARALVNNPQIIFADEPTGNLD----SATGKKIEELLfdlnKNKGITLIIVTHD 203
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRIA----EEREATALVVDHD 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-219 |
1.20e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTF-MHILALLdQPTSGDIYLNGKNVTSirkkvlnktrneefgfvfQQFFMNAKDT 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLlMMIMGEL-EPSEGKIKHSGRISFS------------------PQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLplkigGISGSKRKKMALdaLKAVGLED---KVQNKAN--------NLSGGQKQRVCIARALVNNPQIIFADEP 170
Cdd:TIGR01271 503 IKDNIIF-----GLSYDEYRYTSV--IKACQLEEdiaLFPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286249 171 TGNLDSATGKKI-EELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:TIGR01271 576 FTHLDVVTEKEIfESCLCKLMSNK--TRILVTSKLEHLKKADKILLLHEG 623
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-214 |
1.77e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 1.77e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286249 143 NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQV 214
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-183 |
2.06e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvLNKTRNeefgfvfqQFFMNAKDTV 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRF--------KITIIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNVLLPLKIGGISGSKRKK--MALD---------ALKAvGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:TIGR00957 1371 LFSGSLRMNLDPFSQYSDEEvwWALElahlktfvsALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170
....*....|..
gi 488286249 172 GNLDSATGKKIE 183
Cdd:TIGR00957 1450 AAVDLETDNLIQ 1461
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-178 |
2.27e-11 |
|
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: 60.74 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 1 MAVIEAKNIKKSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPT---SGDIYLNGKNVtsirKK 77
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY----KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 78 VLNKTRNEeFGFVFQQFFMNAKDTVlnnvllplkiggisgskrkKMALD-ALKAvgledkvqnKANN----LSGGQKQRV 152
Cdd:cd03233 77 FAEKYPGE-IIYVSEEDVHFPTLTV-------------------RETLDfALRC---------KGNEfvrgISGGERKRV 127
|
170 180
....*....|....*....|....*.
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSAT 178
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-219 |
3.51e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.41 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTF-MHILALLdQPTSGDIYLNGKNVTSirkkvlnktrneefgfvfQQFFMNAKDT 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLlMLILGEL-EPSEGKIKHSGRISFS------------------SQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVLLplkigGISGSKRKKMALdaLKAVGLED---KVQNKAN--------NLSGGQKQRVCIARALVNNPQIIFADEP 170
Cdd:cd03291 114 IKENIIF-----GVSYDEYRYKSV--VKACQLEEditKFPEKDNtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286249 171 TGNLDSATGKKI-EELLFDLNKNKgiTLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:cd03291 187 FGYLDVFTEKEIfESCVCKLMANK--TRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-223 |
4.70e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 2 AVIEAKNIKKSYgkneTKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirkkvLNK 81
Cdd:PRK10762 3 ALLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT------FNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 TRNEE---FGFVFQQFFMNAKDTVLNNVLLPLKIGGISGS-KRKKMALDA---LKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:PRK10762 73 PKSSQeagIGIIHQELNLIPQLTIAENIFLGREFVNRFGRiDWKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 155 ARALVNNPQIIFADEPTGNL-DSATG---KKIEELlfdlnKNKGITLIIVTHD-PDLAARCDRQVHVRDGLIVG 223
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALtDTETEslfRVIREL-----KSQGRGIVYISHRlKEIFEICDDVTVFRDGQFIA 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-176 |
7.31e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.40 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 11 KSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILAllDQPTSGdiYLNGknvtSIRKKVLNKtRNEEF--- 87
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTGG--YIEG----DIRISGFPK-KQETFari 954
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 88 -GFVFQQFFMNAKDTVLNNVL------LPLKIggisgSKRKKM----------ALDALK--AVGLEDkvqnkANNLSGGQ 148
Cdd:PLN03140 955 sGYCEQNDIHSPQVTVRESLIysaflrLPKEV-----SKEEKMmfvdevmelvELDNLKdaIVGLPG-----VTGLSTEQ 1024
|
170 180
....*....|....*....|....*...
gi 488286249 149 KQRVCIARALVNNPQIIFADEPTGNLDS 176
Cdd:PLN03140 1025 RKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-223 |
8.39e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 11 KSYGKNETKFDALKG------VDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVT------SIRKKV 78
Cdd:PRK11288 251 RPLGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdAIRAGI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 L--NKTRNEEfGFVfqqffmnAKDTVLNNVLLP-----LKIGG-ISGSKRKKMALDALKAvgLEDKVQN---KANNLSGG 147
Cdd:PRK11288 331 MlcPEDRKAE-GII-------PVHSVADNINISarrhhLRAGClINNRWEAENADRFIRS--LNIKTPSreqLIMNLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 148 QKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHD-PDLAARCDRQVHVRDGLIVG 223
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDlPEVLGVADRIVVMREGRIAG 476
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-203 |
8.77e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGknetkfdalkGVDLKVE-----KGESVAIIGKSGSGKSTFMHILALLDQPTSGDI-----------YL 66
Cdd:COG1245 341 LVEYPDLTKSYG----------GFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 67 NGKNVTSIRKkVLNKTRNEEFGFVFQQffmnakdtvlNNVLLPLkiggisgskrkkmaldalkavGLEDKVQNKANNLSG 146
Cdd:COG1245 411 SPDYDGTVEE-FLRSANTDDFGSSYYK----------TEIIKPL---------------------GLEKLLDKNVKDLSG 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 147 GQKQRVCIARALVNNPQIIFADEPTGNLDS----ATGKKIEELLfdlnKNKGITLIIVTHD 203
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFA----ENRGKTAMVVDHD 515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-221 |
1.05e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 6 AKNIKKSYGKNETKFD--ALKGVDLKVEKGESVAIIGKSGSGKSTFmhILALLDQ-PTsgdiyLNGKNVTsIRKKVlnkt 82
Cdd:PLN03130 614 AISIKNGYFSWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSL--ISAMLGElPP-----RSDASVV-IRGTV---- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 rneefGFVFQ-QFFMNAkdTVLNNVLLplkiGGISGSKRKKMALDA--------LKAVGLEDKVQNKANNLSGGQKQRVC 153
Cdd:PLN03130 682 -----AYVPQvSWIFNA--TVRDNILF----GSPFDPERYERAIDVtalqhdldLLPGGDLTEIGERGVNISGGQKQRVS 750
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 154 IARALVNNPQIIFADEPTGNLDSATGKKI------EELlfdlnknKGITLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVfdkcikDEL-------RGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-219 |
2.02e-10 |
|
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: 59.10 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYgkNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLDqpTSGDIYLNGKNVTSIrkkVLNKT 82
Cdd:cd03289 3 MTVKDLTAKY--TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSV---PLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 83 RnEEFGFVFQQFFMNAKDTVLNnvLLPLkiGGISGSKRKKMALD-ALKAV------GLEDKVQNKANNLSGGQKQRVCIA 155
Cdd:cd03289 76 R-KAFGVIPQKVFIFSGTFRKN--LDPY--GKWSDEEIWKVAEEvGLKSVieqfpgQLDFVLVDGGCVLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 156 RALVNNPQIIFADEPTGNLDSATGKKIEELLfdLNKNKGITLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-186 |
2.17e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLDqpTSGDIYLNGKNVTSIrkkVLNKTRnEEFGFVFQQFFMnakdt 101
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLRLLS--TEGEIQIDGVSWNSV---TLQTWR-KAFGVIPQKVFI----- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 vlnnvllplkiggISGSKRKKmaLD------------ALKAVGLEDKVQNKANN-----------LSGGQKQRVCIARAL 158
Cdd:TIGR01271 1304 -------------FSGTFRKN--LDpyeqwsdeeiwkVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSI 1368
|
170 180
....*....|....*....|....*...
gi 488286249 159 VNNPQIIFADEPTGNLDSATGKKIEELL 186
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTL 1396
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-203 |
2.48e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 30 VEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIylnGKNVTsiRKKVLNKTRneefGFVFQQFFMNAKDTVLNNVLLP 109
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPS--WDEVLKRFR----GTELQNYFKKLYNGEIKVVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 110 LKIGGIS----GSKR--------KKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSA 177
Cdd:PRK13409 167 QYVDLIPkvfkGKVRellkkvdeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180
....*....|....*....|....*.
gi 488286249 178 TGKKIEELLFDLNKNKgiTLIIVTHD 203
Cdd:PRK13409 247 QRLNVARLIRELAEGK--YVLVVEHD 270
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-203 |
2.70e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 39 IGKSGSGKSTFMHILALLDQPTSGDIYLNgknvTSIRkkvLNKTRNEEFGFvfQQFfmnakdTVLNNVL----------- 107
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLD----PNER---LGKLRQDQFAF--EEF------TVLDTVImghtelwevkq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 108 ---------------------LPLKIGGISGSKRKKMALDALKAVGL-EDKVQNKANNLSGGQKQRVCIARALVNNPQII 165
Cdd:PRK15064 98 erdriyalpemseedgmkvadLEVKFAEMDGYTAEARAGELLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 488286249 166 FADEPTGNLDSATGKKIEELlfdLNKNKGiTLIIVTHD 203
Cdd:PRK15064 178 LLDEPTNNLDINTIRWLEDV---LNERNS-TMIIISHD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-178 |
4.30e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 15 KNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILAL-LDQ---PTSGDIYLNGKNVTSIRKK-----VLNKTRNE 85
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDGITPEEIKKHyrgdvVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 86 EFGF--VFQQFFMNAKDTVLNNvllplKIGGIS-GSKRKKMALDALKAVGLEDKVQNKANN-----LSGGQKQRVCIARA 157
Cdd:TIGR00956 149 HFPHltVGETLDFAARCKTPQN-----RPDGVSrEEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEA 223
|
170 180
....*....|....*....|.
gi 488286249 158 LVNNPQIIFADEPTGNLDSAT 178
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSAT 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-203 |
4.51e-10 |
|
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: 57.76 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 12 SYGKNETKFDALKgvdlKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDiYLNGKNVTSIrkkvLNKTRNEEFgfvf 91
Cdd:cd03236 9 RYGPNSFKLHRLP----VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEI----LDEFRGSEL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 92 QQFFMNAKDTVLNNVLLPL-----------KIGGISGSKRKKMALDAL-KAVGLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:cd03236 76 QNYFTKLLEGDVKVIVKPQyvdlipkavkgKVGELLKKKDERGKLDELvDQLELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488286249 160 NNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGiTLIIVTHD 203
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHD 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-203 |
1.03e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 31 EKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIylngKNVTSIrKKVLNKTRNEEFgfvfQQFFMNAKDTVLNNVLLPL 110
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY----DEEPSW-DEVLKRFRGTEL----QDYFKKLANGEIKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 111 KIGGI----SGSKR--------KKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLD--- 175
Cdd:COG1245 168 YVDLIpkvfKGTVRellekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyq 247
|
170 180
....*....|....*....|....*....
gi 488286249 176 -SATGKKIEELLfdlnkNKGITLIIVTHD 203
Cdd:COG1245 248 rLNVARLIRELA-----EEGKYVLVVEHD 271
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-223 |
1.07e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVtsiRKKVLNKTRNEEFGFVFQQ-----FFM 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI---NNHNANEAINHGFALVTEErrstgIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 97 NAkDTVLNNVLLPL-----KIGGISGSKRKK---MALDALKAVglEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFAD 168
Cdd:PRK10982 340 YL-DIGFNSLISNIrnyknKVGLLDNSRMKSdtqWVIDSMRVK--TPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286249 169 EPTGNLDSATGKKIEELLFDL-NKNKGItLIIVTHDPDLAARCDRQVHVRDGLIVG 223
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELaKKDKGI-IIISSEMPELLGITDRILVMSNGLVAG 471
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-203 |
1.07e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYL-NGKNVtsirkkvlnktrneefGFVFQQFFMNAKDT 101
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV----------------GYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 102 VLNNVllplkiggISGSKRKKMALDALKAVG-------------------LEDKVQN----------------------- 139
Cdd:PRK11819 87 VRENV--------EEGVAEVKAALDRFNEIYaayaepdadfdalaaeqgeLQEIIDAadawdldsqleiamdalrcppwd 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 140 -KANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnknKGiTLIIVTHD 203
Cdd:PRK11819 159 aKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY---PG-TVVAVTHD 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-221 |
1.68e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFD--ALKGVDLKVEKGESVAIIGKSGSGKSTFmhILALLdqptsGDIYLNGKNVTSIRKKVlnk 81
Cdd:PLN03232 612 APAISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSL--ISAML-----GELSHAETSSVVIRGSV--- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 82 trneefGFVFQ-QFFMNAkdTVLNNVLLplkiGGISGSKRKKMALDA------LKAVGLEDKVQ--NKANNLSGGQKQRV 152
Cdd:PLN03232 682 ------AYVPQvSWIFNA--TVRENILF----GSDFESERYWRAIDVtalqhdLDLLPGRDLTEigERGVNISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286249 153 CIARALVNNPQIIFADEPTGNLDSATGKKI------EELlfdlnknKGITLIIVTHDPDLAARCDRQVHVRDGLI 221
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQVfdscmkDEL-------KGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-212 |
2.32e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 30 VEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVlnktrNEEFGFVFQqffMNAKDTVLN---NV 106
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV-----HQNMGYCPQ---FDAIDDLLTgreHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 107 LLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELL 186
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|....*..
gi 488286249 187 FDLNKnKGITLIIVTHD-PDLAARCDR 212
Cdd:TIGR01257 2114 VSIIR-EGRAVVLTSHSmEECEALCTR 2139
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-203 |
3.02e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGknetkfDAL--KGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLnGKNVtsirkkvln 80
Cdd:PRK11819 324 VIEAENLSKSFG------DRLliDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 ktrneEFGFVFQQF-FMNAKDTVLNNV---LLPLKIGGISGSKRKKMALDALKAVgleDKvQNKANNLSGGQKQRVCIAR 156
Cdd:PRK11819 388 -----KLAYVDQSRdALDPNKTVWEEIsggLDIIKVGNREIPSRAYVGRFNFKGG---DQ-QKKVGVLSGGERNRLHLAK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnknKGITLIIvTHD 203
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVVI-SHD 501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-203 |
3.18e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSY-GKNetkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILalLDQ--PTSGDIYLNGKnvtsirkkvl 79
Cdd:PRK11147 319 VFEMENVNYQIdGKQ-----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQlqADSGRIHCGTK---------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 80 nktrnEEFGFvFQQF--FMNAKDTVLNNVLLPLKIGGISGSKRK------------KMALDALKAvgledkvqnkannLS 145
Cdd:PRK11147 382 -----LEVAY-FDQHraELDPEKTVMDNLAEGKQEVMVNGRPRHvlgylqdflfhpKRAMTPVKA-------------LS 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 146 GGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLnknKGiTLIIVTHD 203
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY---QG-TVLLVSHD 496
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-217 |
3.86e-09 |
|
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: 54.54 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETKFDalKGVDLkvekgesvaIIGKSGSGKSTfmhILALLDQPTSGDIYLNGKNVTSIRKKVlnkTR 83
Cdd:cd03240 4 LSIRNIRSFHERSEIEFF--SPLTL---------IVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKLI---RE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 84 NEEFGFVFQQFFMNAKDT--------VLNNVLLpLKIGGIsgskrKKMALDALKavgledkvqnkanNLSGGQKQ----- 150
Cdd:cd03240 67 GEVRAQVKLAFENANGKKytitrslaILENVIF-CHQGES-----NWPLLDMRG-------------RCSGGEKVlasli 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286249 151 -RVCIARALVNNPQIIFADEPTGNLDSAT-GKKIEELLFDLNKNKGITLIIVTHDPDLAARCDRQVHVR 217
Cdd:cd03240 128 iRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-210 |
4.12e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTfmhILALL--DQPT--SGDIYLNGKNVTS------ 73
Cdd:PRK10938 261 IVLNNGVVSYNDRPI----LHNLSWQVNPGEHWQIVGPNGAGKST---LLSLItgDHPQgySNDLTLFGRRRGSgetiwd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 74 IRKKVlnktrneefGFVFQQFFMNAK-DTVLNNVLLplkiggiSG------------SKRKKMALDALKAVGLEDKVQNK 140
Cdd:PRK10938 334 IKKHI---------GYVSSSLHLDYRvSTSVRNVIL-------SGffdsigiyqavsDRQQKLAQQWLDILGIDKRTADA 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 141 A-NNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGITLIIVTHDPDLAARC 210
Cdd:PRK10938 398 PfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAC 468
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-212 |
5.95e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILA---LLDQPTSGDIYLNGKNvtsirkkvLNKTRNEEFGFVFQQFFMNAK 99
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRP--------LDSSFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNVL------LPLKIggisgSKRKKMAL--DALKAVGLEDK----VQNKANNLSGGQKQRVCIARALVNNPQ-IIF 166
Cdd:TIGR00956 851 STVRESLRfsaylrQPKSV-----SKSEKMEYveEVIKLLEMESYadavVGVPGEGLNVEQRKRLTIGVELVAKPKlLLF 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286249 167 ADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDP--DLAARCDR 212
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQPsaILFEEFDR 972
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-216 |
6.75e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 54.19 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKST---------------------FMHILALLDQPTSGDIylNGKNVT-SIRKKVLN 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveslsayARQFLGQMDKPDVDSI--EGLSPAiAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRNEEFGFVfqqffmnakdTVLNNVLLPL--KIGGISgskrkkmALDALKAVGLED-KVQNKANNLSGGQKQRVCIARA 157
Cdd:cd03270 89 RNPRSTVGTV----------TEIYDYLRLLfaRVGIRE-------RLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 158 LVNN-PQIIFA-DEPTGNLDSATGKKIEELLFDLnKNKGITLIIVTHDPDLAARCDRQVHV 216
Cdd:cd03270 152 IGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-223 |
7.13e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHIL--ALldQPTSGDIYLNGKNVTSIRKK--------VLNKTRNEEfGFVFQ 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLygAL--PRTSGYVTLDGHEVVTRSPQdglangivYISEDRKRD-GLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 93 qffMNAKDtvlNNVLLPL----KIGGISGSKRKKMAL-DALKAVGLEDKVQNKA-NNLSGGQKQRVCIARALVNNPQIIF 166
Cdd:PRK10762 345 ---MSVKE---NMSLTALryfsRAGGSLKHADEQQAVsDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 167 ADEPTGNLDSATGKKIEELL--FdlnKNKGITLIIVTHD-PDLAARCDRQVHVRDGLIVG 223
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLInqF---KAEGLSIILVSSEmPEVLGMSDRILVMHEGRISG 475
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-217 |
1.05e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.75 E-value: 1.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286249 144 LSGGQKQRVCIARAL----VNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHDPDLAARCDRQVHVR 217
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPELAELADKLIHIK 154
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-212 |
1.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNeefgfVFQQFFMNAKDTV 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS-----IIPQSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNV--LLPLKIGGISGSKRKKMALDALK--AVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSAT 178
Cdd:PLN03232 1327 RFNIdpFSEHNDADLWEALERAHIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190
....*....|....*....|....*....|....
gi 488286249 179 GKKIEELLFDlnKNKGITLIIVTHDPDLAARCDR 212
Cdd:PLN03232 1407 DSLIQRTIRE--EFKSCTMLVIAHRLNTIIDCDK 1438
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-220 |
3.07e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 32 KGESVAIIGKSGSGKSTFMHILA-LLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGfvfqqffmnakdtvlnnvllpl 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALArELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 111 kiggisgskrkkmaldalkavgledkvqnkaNNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEEL----- 185
Cdd:smart00382 59 -------------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488286249 186 LFDLNKNKGITLIIVTHDPD------LAARCDRQVHVRDGL 220
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-206 |
8.28e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLnGKNVtsirkkvlnktrneEFGFVFQ-QF-FMNAKD 100
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI--------------KLGYFAQhQLeFLRADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVLNNvllplkIGGISGSKRKKMALDALKAVGLE-DKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATG 179
Cdd:PRK10636 393 SPLQH------LARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180
....*....|....*....|....*..
gi 488286249 180 KKIEELLFDLNKnkgiTLIIVTHDPDL 206
Cdd:PRK10636 467 QALTEALIDFEG----ALVVVSHDRHL 489
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-202 |
1.18e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNETkfdaLKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLD--QPTSGDIYLNGKNVTSIRKKvln 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAI----LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KTRNEEFGFVFQ----------QFFMNakdTVLNNVllplkiggisgskRKKMALDALKAVGLEDKVQNKANNL------ 144
Cdd:PRK09580 74 DRAGEGIFMAFQypveipgvsnQFFLQ---TALNAV-------------RSYRGQEPLDRFDFQDLMEEKIALLkmpedl 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 145 ---------SGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNKGiTLIIVTH 202
Cdd:PRK09580 138 ltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-223 |
1.53e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTF-MHILA-LLDQPTSGDIYLNGK--NVTSIRKKVLNktrneefGFVF-----QQ 93
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrSYGRNISGTVFKDGKevDVSTVSDAIDA-------GLAYvtedrKG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 94 FFMNAKDTVLNNVLLPlKIGGIS--------------GSKRKKMALdalKAVGledkVQNKANNLSGGQKQRVCIARALV 159
Cdd:NF040905 349 YGLNLIDDIKRNITLA-NLGKVSrrgvideneeikvaEEYRKKMNI---KTPS----VFQKVGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 160 NNPQIIFADEPTGNLDsaTGKKIE--ELLFDL-NKNKGItLIIVTHDPDLAARCDRQVHVRDGLIVG 223
Cdd:NF040905 421 TDPDVLILDEPTRGID--VGAKYEiyTIINELaAEGKGV-IVISSELPELLGMCDRIYVMNEGRITG 484
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-204 |
1.78e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 35 SVAII-GKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLnktrneefGFVFQQFFMNAKDTVLNNVLLPLKIg 113
Cdd:PRK13541 27 AITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC--------TYIGHNLGLKLEMTVFENLKFWSEI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 114 gisgSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFdLNKNK 193
Cdd:PRK13541 98 ----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV-MKANS 172
|
170
....*....|.
gi 488286249 194 GITLIIVTHDP 204
Cdd:PRK13541 173 GGIVLLSSHLE 183
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-206 |
1.86e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 25 GVDLKvekgESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKnvtsIRKKVlnktrneefgfvFQQFFMNAKDTVLN 104
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK----VRMAV------------FSQHHVDGLDLSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 105 NVLLPLKIggISGSKRKKMALDaLKAVGLEDKVQNKA-NNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSatgKKIE 183
Cdd:PLN03073 591 PLLYMMRC--FPGVPEQKLRAH-LGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAVE 664
|
170 180
....*....|....*....|...
gi 488286249 184 ELLFDLNKNKGiTLIIVTHDPDL 206
Cdd:PLN03073 665 ALIQGLVLFQG-GVLMVSHDEHL 686
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-223 |
3.17e-07 |
|
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: 50.21 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKkSYGKNETKFDALKGVDLKVEKGESVAIIGKSGSGKSTFMH-ILALLDQPTSGDIYLNGKNVT------SIR 75
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDirnpaqAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 76 KKVLNKTRNEEFGFVFQQFFMnAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKA-NNLSGGQKQRVCI 154
Cdd:TIGR02633 336 AGIAMVPEDRKRHGIVPILGV-GKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVL 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHD-PDLAARCDRQVHVRDGLIVG 223
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSElAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-213 |
3.85e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRkkvlnKTRNEEFGFVFQQFFMNAKDTV 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDL-----CTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNVLLPLKIGgiSGSkrkkMALDAL-KAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSAT--- 178
Cdd:PRK13540 92 RENCLYDIHFS--PGA----VGITELcRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSllt 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 488286249 179 -GKKIEEllfdlNKNKGITLIIVTHDPDLAARCDRQ 213
Cdd:PRK13540 166 iITKIQE-----HRAKGGAVLLTSHQDLPLNKADYE 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-212 |
4.19e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSirkkvlnktrneeFGFvfqqffmnakdTV 102
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK-------------FGL-----------MD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 103 LNNVL--LPLKIGGISGSKRKKM-------------ALDA--LKAV------GLEDKVQNKANNLSGGQKQRVCIARALV 159
Cdd:PLN03130 1311 LRKVLgiIPQAPVLFSGTVRFNLdpfnehndadlweSLERahLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286249 160 NNPQIIFADEPTGNLDSATG----KKIEEllfdlnKNKGITLIIVTHDPDLAARCDR 212
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDaliqKTIRE------EFKSCTMLIIAHRLNTIIDCDR 1441
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
143-212 |
4.28e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 4.28e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286249 143 NLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnKGITLIIVTHD-PDLAARCDR 212
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSElPEVLGLSDR 474
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-178 |
7.16e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 48.75 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTsirkKVLNKTRNEEFGFVFQ---------Q 93
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS----KLPLHTLRSRLSIILQdpilfsgsiR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 94 FFMNAKDTVLNNVLL-PLKIGGIsgskrkKMALDALKAvGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTG 172
Cdd:cd03288 113 FNLDPECKCTDDRLWeALEIAQL------KNMVKSLPG-GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
....*.
gi 488286249 173 NLDSAT 178
Cdd:cd03288 186 SIDMAT 191
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-219 |
7.96e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 30 VEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVtsirkkvlnktrneefgfvfqqffmnakdtvlnnVLLP 109
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----------------------------------VYKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 110 LKIggisgskrkkmaldalkavgledkvqnkanNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDS----ATGKKIEEL 185
Cdd:cd03222 68 QYI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|....
gi 488286249 186 LFDLNKnkgiTLIIVTHDPDLAARCDRQVHVRDG 219
Cdd:cd03222 118 SEEGKK----TALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-214 |
1.58e-06 |
|
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: 46.93 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFM-HILAlldqpTSGDIYLNGKNVTSIRKKVLnktrneefgFVFQqffmnakd 100
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVnEGLY-----ASGKARLISFLPKFSRNKLI---------FIDQ-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 tvlnnvllplkiggisgskrkkmaLDALKAVGLED-KVQNKANNLSGGQKQRVCIARALVNNPQ--IIFADEPTGNLDSA 177
Cdd:cd03238 68 ------------------------LQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|....*..
gi 488286249 178 TGKKIEELLFDLnKNKGITLIIVTHDPDLAARCDRQV 214
Cdd:cd03238 124 DINQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWII 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-205 |
4.59e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 26 VDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIrkkvlnKTRNE-EFGFVF-----QQFFMNAK 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL------STAQRlARGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNV--LLPLKIGGISGSKRKKMALDAL-KAVGLE-DKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLD 175
Cdd:PRK15439 356 APLAWNVcaLTHNRRGFWIKPARENAVLERYrRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190
....*....|....*....|....*....|
gi 488286249 176 SATGKKIEELLFDLNKnKGITLIIVTHDPD 205
Cdd:PRK15439 436 VSARNDIYQLIRSIAA-QNVAVLFISSDLE 464
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-200 |
1.52e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 27 DLKVEKGESVAIIGKSGSGKSTFMhiLALldqptSGD-IYLNGKNVTSIRKKV------LNKTRNEEFgfvfQQ------ 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALA--RAL-----AGElPLLSGERQSQFSHITrlsfeqLQKLVSDEW----QRnntdml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 94 ------FFMNAKDTVLNNVllplkiggisgskrKKMALDALKA--VGLEDKVQNKANNLSGGQKQRVCIARALVNNPQII 165
Cdd:PRK10938 92 spgeddTGRTTAEIIQDEV--------------KDPARCEQLAqqFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 488286249 166 FADEPTGNLDSATGKKIEELLFDLNKnKGITLIIV 200
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLV 191
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-203 |
1.65e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 15 KNETkFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGK-NVTSIRKKvlnktrneefgfvfqq 93
Cdd:PRK13546 33 KNKT-FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAG---------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 94 ffMNAKDTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGN 173
Cdd:PRK13546 96 --LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190
....*....|....*....|....*....|
gi 488286249 174 LDSATGKKIEELLFDLnKNKGITLIIVTHD 203
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHN 202
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
15-206 |
3.82e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.88 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 15 KNETKFDaLKGVDLKVEKgeSVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSIRKKVLNKTRNEEFGFVFQQ- 93
Cdd:COG1106 14 KDELTLS-MVASGLRLLR--VNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEPSEFEILFLLd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 94 --------------------FFMNAKDTV------------LNNVLLPLKIGGIS-----GSKRKKMALDALKAV--GLE 134
Cdd:COG1106 91 gvryeygfeldkeriisewlYFLSTAAQLnvpllsplydwfDNNISLDTSSDGLTlllkeDESLKEELLELLKIAdpGIE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 135 DKVQNKANNLSGGQKQRV-----------------------CIARALVN---NPQIIFADEPTGNLDSATGKKIEELLFD 188
Cdd:COG1106 171 DIEVEEEEIEDLVERKLIfkhkggnvplplseesdgtkrllALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFLD 250
|
250
....*....|....*...
gi 488286249 189 LNKNKGITLIIVTHDPDL 206
Cdd:COG1106 251 LANKNNAQLIFTTHSTEL 268
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-171 |
5.55e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 3 VIEAKNIKKSYGKNEtkfdALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGKNVTSI--RKKVLN 80
Cdd:NF033858 1 VARLEGVSHRYGKTV----ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 81 KT--------RN-------EE----FGFVFqqffmnakdtvlnnvllplkigGISGSKRKKMALDALKAVGLEDKVQNKA 141
Cdd:NF033858 77 RIaympqglgKNlyptlsvFEnldfFGRLF----------------------GQDAAERRRRIDELLRATGLAPFADRPA 134
|
170 180 190
....*....|....*....|....*....|
gi 488286249 142 NNLSGGQKQRVCIARALVNNPQIIFADEPT 171
Cdd:NF033858 135 GKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-202 |
6.08e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 33 GESVAIIGKSGSGKSTFMHILAL--LDQ-PTSGDIYLNGKNV----TSIRKKVLN----KTR--NEEFGFVFQQffmnaK 99
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAMhaIDGiPKNCQILHVEQEVvgddTTALQCVLNtdieRTQllEEEAQLVAQQ-----R 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 100 DTVLNNVLLPLKIGGISGSKRKKMA---------LDALKAVGLEDK-------------VQNKANN-LSGGQKQRVCIAR 156
Cdd:PLN03073 278 ELEFETETGKGKGANKDGVDKDAVSqrleeiykrLELIDAYTAEARaasilaglsftpeMQVKATKtFSGGWRMRIALAR 357
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286249 157 ALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKnkgiTLIIVTH 202
Cdd:PLN03073 358 ALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-216 |
8.68e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 30 VEKGESVAIIGKSGSGKSTfmhILALLdqptSGDIYLNGKNVT-------------------SIRKKVLNKTRNeefgfv 90
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKST---LLALL----KNEISADGGSYTfpgnwqlawvnqetpalpqPALEYVIDGDRE------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 91 FQQFFMNAKDTVLNN-----VLLPLKIGGISGSKRKKMALDALKAVGL-EDKVQNKANNLSGGQKQRVCIARALVNNPQI 164
Cdd:PRK10636 91 YRQLEAQLHDANERNdghaiATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286249 165 IFADEPTGNLDSATGKKIEELLfdlnKNKGITLIIVTHDPD-LAARCDRQVHV 216
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDfLDPIVDKIIHI 219
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-202 |
1.10e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 22 ALKGVDLKVEKGESVAIIGKSGSGKSTFMHILALLDQPTSGDIYLNGK-NVTSIRKKvlnktrneefgfvfqqffMNAKD 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISSG------------------LNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 101 TVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCIARALVNNPQIIFADEPTGNLDSATGK 180
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180
....*....|....*....|..
gi 488286249 181 KIEELLFDLnKNKGITLIIVTH 202
Cdd:PRK13545 181 KCLDKMNEF-KEQGKTIFFISH 201
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-218 |
2.42e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 4 IEAKNIKKSYGknETKfdALKGVDLKVEKGESVAIIGKSGSGKSTFMhILALLDQPTSGD----IYLNGKNVTSIRKKV- 78
Cdd:NF000106 14 VEVRGLVKHFG--EVK--AVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrpwrF*TWCANRRALRRTIg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 79 ----LNKTRNEEFgfvfqqffmnakdTVLNNVLLPLKIGGISGSKRKKMALDALKAVGLEDKVQNKANNLSGGQKQRVCI 154
Cdd:NF000106 89 *hrpVR*GRRESF-------------SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286249 155 ARALVNNPQIIFADEPTGNLDSATGKKIEELLFDLNKNkGITLIIVTHDPDLAARCDRQVHVRD 218
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVID 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
125-211 |
5.20e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 125 LDALKAVGLED-KVQNKANNLSGGQKQRVCIARALVN---NPQIIFADEPTGNLDSAtgkKIEELLFDLNK--NKGITLI 198
Cdd:cd03271 150 LQTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFH---DVKKLLEVLQRlvDKGNTVV 226
|
90
....*....|...
gi 488286249 199 IVTHDPDLAARCD 211
Cdd:cd03271 227 VIEHNLDVIKCAD 239
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-205 |
6.86e-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: 40.38 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 125 LDALKAVGLED-KVQNKANNLSGGQKQRVCIARAL---VNNPQIIFADEPTGNLDSATGKKIEELLFDLnKNKGITLIIV 200
Cdd:TIGR00630 810 LQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVI 888
|
....*
gi 488286249 201 THDPD 205
Cdd:TIGR00630 889 EHNLD 893
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
19-55 |
2.70e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 38.63 E-value: 2.70e-03
10 20 30
....*....|....*....|....*....|....*..
gi 488286249 19 KFDALKGVDLKVEKGESVAIIGKSGSGKSTFMHILAL 55
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLAL 202
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
145-226 |
4.83e-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: 37.72 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286249 145 SGGQKQ------RVCIARALVNNPQIIFADEPTGNLDSATGKKIEELLFDL----NKNKGITLIIVTHDPDLAARCDRQV 214
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrSQQRNFQLLVITHDEDFVELLGRSE 1280
|
90
....*....|..
gi 488286249 215 HVRDGLIVGGDE 226
Cdd:TIGR00606 1281 YVEKFYRLKKNE 1292
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
23-53 |
9.24e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 36.93 E-value: 9.24e-03
10 20 30
....*....|....*....|....*....|..
gi 488286249 23 LKGVDLKVEKGESVAIIGKSGSGKSTFMH-IL 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| |
