|
Name |
Accession |
Description |
Interval |
E-value |
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-223 |
2.30e-143 |
|
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: 399.50 E-value: 2.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQ 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARVRAAHVGFVFQSFQLLDSLDALENVMLPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAA 160
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 161 EPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLID 223
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-223 |
1.53e-117 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 333.93 E-value: 1.53e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 3 ASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRA 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 83 RVRAAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAA 160
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 161 EPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLID 223
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-221 |
2.98e-108 |
|
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: 310.19 E-value: 2.98e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-221 |
2.74e-94 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 275.12 E-value: 2.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRAR 83
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 VRAAHVGFVFQSFQLLDSLDALENVMLPLELEGRAD--ARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAE 161
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSrqSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 162 PDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-223 |
6.92e-84 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 248.43 E-value: 6.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGsaeGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaH 88
Cdd:COG2884 5 ENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNReRGTTLVLVTHDERLAHRCR-RLIRLESGRLID 223
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPkRVLELEDGRLVR 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-221 |
4.26e-82 |
|
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: 244.18 E-value: 4.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARV 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-209 |
2.85e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 230.75 E-value: 2.85e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDq 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 rarvraahVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAF 158
Cdd:COG1116 82 --------RGVVFQEPALLPWLTVLDNVALGLELRGvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 159 AAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD--E--RLAHR 209
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvdEavFLADR 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-222 |
9.56e-74 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.88 E-value: 9.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaH 88
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD----ERLAHRCrrlIRLESGRLI 222
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvvRRICDRV---AVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-222 |
5.29e-73 |
|
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: 221.30 E-value: 5.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARV 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAaHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPLEIAGvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-222 |
6.68e-70 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 213.70 E-value: 6.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKvvgsAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDlDEDQRARV 84
Cdd:COG1126 1 MIEIENLHK----SFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAaHVGFVFQSFQLLDSLDALENVMLPLEL---EGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAE 161
Cdd:COG1126 76 RR-KVGMVFQQFNLFPHLTVLENVTLAPIKvkkMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 162 PDVLFADEPTGNLD-SATGErISDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG1126 155 PKVMLFDEPTSALDpELVGE-VLDVMRDL-AKEGMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-209 |
2.23e-69 |
|
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: 211.56 E-value: 2.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldedQRARVR 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---------EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD--E--RLAHR 209
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDidEavFLADR 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
1.31e-67 |
|
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: 207.91 E-value: 1.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQ 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARVRAaHVGFVFQSFQLLDSLDALENVMLPLELEGR---ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARA 157
Cdd:COG1127 77 LYELRR-RIGMLFQGGALFDSLTVFENVAFPLREHTDlseAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 158 FAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-203 |
1.00e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 206.87 E-value: 1.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQ 80
Cdd:COG3842 1 MAMPALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RarvraaHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAF 158
Cdd:COG3842 77 R------NVGMVFQDYALFPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 159 AAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
24-220 |
3.85e-65 |
|
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: 200.55 E-value: 3.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaHVGFVFQSFQLLDSLD 103
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR-RIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEGR--ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGER 181
Cdd:TIGR02673 96 VYENVALPLEVRGKkeREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSER 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598053 182 ISDLLFELNReRGTTLVLVTHDERLAHRCR-RLIRLESGR 220
Cdd:TIGR02673 176 ILDLLKRLNK-RGTTVIVATHDLSLVDRVAhRVIILDDGR 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
4.36e-65 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 201.20 E-value: 4.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVgsAEGKLT--ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDE 78
Cdd:PRK11629 1 MNKILLQCDNLCKRY--QEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 79 DQRARVRAAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIAR 156
Cdd:PRK11629 79 AAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 157 AFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLID 223
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-216 |
7.32e-65 |
|
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: 199.76 E-value: 7.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAH 88
Cdd:TIGR03608 2 KNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEGRA--DARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSkkEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRErGTTLVLVTHDERLAHRCRRLIRL 216
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-226 |
5.09e-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: 198.87 E-value: 5.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDldedQRARVR 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AAHVGFVFQsfqllDSLDAL-------ENVMLPLELEGRADARQRARELLERVGLGQRLGH-YPRQLSGGEQQRVAIARA 157
Cdd:COG1124 78 RRRVQMVFQ-----DPYASLhprhtvdRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 158 FAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERL-AHRCRRLIRLESGRLIDRVE 226
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVvAHLCDRVAVMQNGRIVEELT 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
9-221 |
6.50e-64 |
|
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: 197.93 E-value: 6.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaH 88
Cdd:TIGR02982 5 RNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRR-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELE---GRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:TIGR02982 84 IGYIFQAHNLLGFLTARQNVQMALELQpnlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 166 FADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:TIGR02982 164 LADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
9.27e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 198.36 E-value: 9.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGsaeGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRAR 83
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 VRAaHVGFVFQSFQLLDSLDALENVMLpleleGR---------------ADARQRARELLERVGLGQRLGHYPRQLSGGE 148
Cdd:COG3638 78 LRR-RIGMIFQQFNLVPRLSVLTNVLA-----GRlgrtstwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 149 QQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-222 |
3.87e-62 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 204.96 E-value: 3.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 3 ASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRA 82
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 83 RVRAAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAA 160
Cdd:PRK10535 82 QLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 161 EPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHRCRRLIRLESGRLI 222
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-222 |
5.59e-61 |
|
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: 190.41 E-value: 5.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRaRV 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAAHVGFVFQsfqllDSLDAL-------ENVMLPLELEGRADARQRARE----LLERVGLG-QRLGHYPRQLSGGEQQRV 152
Cdd:cd03257 80 RRKEIQMVFQ-----DPMSSLnprmtigEQIAEPLRIHGKLSKKEARKEavllLLVGVGLPeEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 153 AIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERL-AHRCRRLIRLESGRLI 222
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVvAKIADRVAVMYAGKIV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-222 |
2.10e-60 |
|
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: 189.25 E-value: 2.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaHVGFVFQSFQLL 99
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-RMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLELEGRADA---RQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:cd03261 90 DSLTVFENVAFPLREHTRLSEeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:cd03261 170 IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-203 |
5.97e-60 |
|
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: 187.35 E-value: 5.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKvvgsAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgDLDEDQRARVR 85
Cdd:cd03262 1 IEIKNLHK----SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AaHVGFVFQSFQLLDSLDALENVML-PLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLaPIKVKGmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRErGTTLVLVTHD 203
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHE 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
1.26e-59 |
|
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: 195.51 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKV-VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDED 79
Cdd:COG1123 256 AAEPLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 80 QRARVRAaHVGFVFQS-FQLLDSLD-ALENVMLPLELEG---RADARQRARELLERVGLGQRLGH-YPRQLSGGEQQRVA 153
Cdd:COG1123 336 SLRELRR-RVQMVFQDpYSSLNPRMtVGDIIAEPLRLHGllsRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 154 IARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-209 |
2.10e-59 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 189.49 E-value: 2.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQP---SGGEVRLAGHALGDLDEDQR 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 82 ARVRAAHVGFVFQsfqllDSLDAL-------ENVMLPLEL---EGRADARQRARELLERVGL---GQRLGHYPRQLSGGE 148
Cdd:COG0444 81 RKIRGREIQMIFQ-----DPMTSLnpvmtvgDQIAEPLRIhggLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 149 QQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD----ERLAHR 209
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlgvvAEIADR 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-224 |
7.04e-59 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 188.86 E-value: 7.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaH 88
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR-Q 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLIDR 224
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-203 |
1.16e-58 |
|
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: 184.26 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaH 88
Cdd:cd03259 4 KGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR------N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHD 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-221 |
1.67e-57 |
|
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: 181.45 E-value: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 13 KVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaHVGFV 92
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 93 FQSFQLLDSLDALENVMLPLEL--EGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598053 171 TGNLDSATGERISDLLFELNReRGTTLVLVTHDERLAHRCR-RLIRLESGRL 221
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-203 |
9.79e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 183.74 E-value: 9.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaH 88
Cdd:COG3839 7 ENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR------N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-222 |
1.64e-56 |
|
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: 179.07 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 19 EGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRARVRAaHVGFVFQS--F 96
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK---DITKKNLRELRR-KVGLVFQNpdD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSlDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:COG1122 87 QLFAP-TVEEDVAFGPENLGlpREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 175 DSATGERISDLLFELNRErGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:COG1122 166 DPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRIV 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
24-220 |
3.33e-55 |
|
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: 175.35 E-value: 3.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSF--QLLdS 101
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR----KVGLVFQNPddQFF-G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATG 179
Cdd:cd03225 91 PTVEEEVAFGLENLGlpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 180 ERISDLLFELNRErGTTLVLVTHD-ERLAHRCRRLIRLESGR 220
Cdd:cd03225 171 RELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
2.50e-54 |
|
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: 181.64 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 3 ASILNAQNLSkvVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSG---GEVRLAGHALGDLDED 79
Cdd:COG1123 2 TPLLEVRDLS--VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 80 QRARvraaHVGFVFQSFQL-LDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIAR 156
Cdd:COG1123 80 LRGR----RIGMVFQDPMTqLNPVTVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 157 AFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIV 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-221 |
6.16e-54 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 172.97 E-value: 6.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAhvGFVFQSFQLL 99
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEA--GMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVML-PLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK09493 90 PHLTALENVMFgPLRVRGasKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598053 177 ATGERISDLLFELNRErGTTLVLVTHDERLAHRC-RRLIRLESGRL 221
Cdd:PRK09493 170 ELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVaSRLIFIDKGRI 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-222 |
1.44e-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: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASIlnaQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQ 80
Cdd:COG1118 1 MSIEV---RNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARVRaaHVGFVFQSFQLLDSLDALENVM--LPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAF 158
Cdd:COG1118 71 PPRER--RVGFVFQHYALFPHMTVAENIAfgLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 159 AAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-221 |
1.49e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.15 E-value: 1.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLD-EDQRARV 84
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 raahvGFVFQSFQLL-DSLdaLENVMLPLELEGRADARQRARELLERVGLGQRLGHYP-RQLSGGEQQRVAIARAFAAEP 162
Cdd:COG4619 77 -----AYVPQEPALWgGTV--RDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRL 221
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-222 |
1.13e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.47 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDldedQRARVR 85
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AaHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:COG1131 73 R-RIGYVPQEPALYPDLTVRENLRFFARLYGlpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-222 |
2.95e-52 |
|
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: 169.07 E-value: 2.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLdedqRARV 84
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL----SRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAAHVGFVFQSFQLLDSLDALENVML-------PLELEGRADaRQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARA 157
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 158 FAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIV 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-222 |
4.06e-52 |
|
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: 168.52 E-value: 4.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEgklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVR 85
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AaHVGFVFQSFQLLDSLDALENVMLP-----------LELEGRADaRQRARELLERVGLGQRlgHYPR--QLSGGEQQRV 152
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEE-KQRALAALERVGLLDK--AYQRadQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 153 AIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-209 |
5.46e-52 |
|
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: 175.64 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKS----TLLGLLAGLDQPSGGEVRLAGHALGDL 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 DEDQRARVRAAHVGFVFQsfQLLDSLDAL----ENVMLPLELE---GRADARQRARELLERVGL---GQRLGHYPRQLSG 146
Cdd:COG4172 82 SERELRRIRGNRIAMIFQ--EPMTSLNPLhtigKQIAEVLRLHrglSGAAARARALELLERVGIpdpERRLDAYPHQLSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 147 GEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD----ERLAHR 209
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRRFADR 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-203 |
2.18e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 167.35 E-value: 2.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQrar 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 vraahvGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAE 161
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRLRGvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 162 PDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-207 |
3.52e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 166.51 E-value: 3.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAL-------GDL-- 76
Cdd:COG4598 9 LEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 -DEDQRARVRAaHVGFVFQSFQLLDSLDALENVML-PLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRV 152
Cdd:COG4598 85 aDRRQLQRIRT-RLGMVFQSFNLWSHMTVLENVIEaPVHVLGrpKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 153 AIARAFAAEPDVLFADEPTGNLDSatgERISDLLF---ELNRErGTTLVLVTHDERLA 207
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDP---ELVGEVLKvmrDLAEE-GRTMLVVTHEMGFA 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-220 |
6.50e-51 |
|
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: 163.13 E-value: 6.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVR 85
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aaHVGFVFQSFQLLDSLDALENVMLPLelegradarqrarellervglgqrlghyprqlSGGEQQRVAIARAFAAEPDVL 165
Cdd:cd03229 77 --RIGMVFQDFALFPHLTVLENIALGL--------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 166 FADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGR 220
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-209 |
1.32e-50 |
|
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: 165.51 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQSFQLLDSLDA 104
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:cd03294 120 LENVAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190
....*....|....*....|....*....|.
gi 15598053 183 SDLLFELNRERGTTLVLVTHD----ERLAHR 209
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDldeaLRLGDR 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-222 |
5.61e-50 |
|
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: 163.29 E-value: 5.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 2 SASILNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQR 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 82 AR---VRAahvgfvFQSFQLLDSLDALENVML-----------------PLELEGRADARQRARELLERVGLGQRLGHYP 141
Cdd:COG0411 77 ARlgiART------FQNPRLFPELTVLENVLVaaharlgrgllaallrlPRARREEREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 142 RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGR 220
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGR 230
|
..
gi 15598053 221 LI 222
Cdd:COG0411 231 VI 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-203 |
1.53e-48 |
|
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: 159.39 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAEgklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaH 88
Cdd:cd03295 4 ENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGL--GQRLGHYPRQLSGGEQQRVAIARAFAAEPDV 164
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKwpKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598053 165 LFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD 195
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-222 |
2.30e-48 |
|
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: 159.00 E-value: 2.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEgklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARV 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAaHVGFVFQSFQLLDSLDALENVMLP-----------LELEGRADaRQRARELLERVGLGQRlgHYPR--QLSGGEQQR 151
Cdd:TIGR02315 78 RR-RIGMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEED-KERALSALERVGLADK--AYQRadQLSGGQQQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 152 VAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-222 |
3.10e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 155.42 E-value: 3.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL-----DQPSGGEVRLAGHALGDLDEDqRARVRAAhVGFVFQ 94
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVD-VLELRRR-VGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDsLDALENVMLPLELEG---RADARQRARELLERVGL----GQRLGhyPRQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:cd03260 89 KPNPFP-GSIYDNVAYGLRLHGiklKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 168 DEPTGNLDSATGERISDLLFELNRErgTTLVLVTHDERLAHRC-RRLIRLESGRLI 222
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLV 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-221 |
6.06e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 6.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGdldedqRARVRaahVGFVFQSFQLL 99
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR------RARRR---IGYVPQRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DS--LDALENVML-------PLELEGRADaRQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:COG1121 88 WDfpITVRDVVLMgrygrrgLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598053 171 TGNLDSATGERISDLLFELNRErGTTLVLVTHD-ERLAHRCRRLIRLESGRL 221
Cdd:COG1121 167 FAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-222 |
6.84e-47 |
|
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: 156.07 E-value: 6.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaHVGFVFQsF---QLLdS 101
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQ-FpehQLF-E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVML-PLEL-EGRADARQRARELLERVGLGQR-LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:TIGR04521 98 ETVYKDIAFgPKNLgLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 179 GERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-209 |
6.87e-47 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 156.79 E-value: 6.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGsaeGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaH 88
Cdd:COG1125 5 ENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGL--GQRLGHYPRQLSGGEQQRVAIARAFAAEPDV 164
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGwdKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 165 LFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD--E--RLAHR 209
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidEalKLGDR 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-204 |
1.76e-46 |
|
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: 153.55 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaHVGFVFQSFQLL 99
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR------PVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:cd03300 85 PHLTVFENIAFGLRLKKlpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180
....*....|....*....|....*..
gi 15598053 178 TGERISDLLFELNRERGTTLVLVTHDE 204
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQ 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-213 |
1.81e-46 |
|
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: 152.63 E-value: 1.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvr 85
Cdd:COG4133 3 LEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aaHVGFVFQSFQLLDSLDALENVMLPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:COG4133 76 --RLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598053 166 FADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHRCRRL 213
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARVL 200
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-224 |
2.15e-46 |
|
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: 161.47 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 19 EGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQL 98
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR----RIAVVPQRPHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 LD-SLdaLENVMLpleleGRADA-RQRARELLERVGLGQ-----------RLGHYPRQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:COG4987 421 FDtTL--RENLRL-----ARPDAtDEELWAALERVGLGDwlaalpdgldtWLGEGGRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598053 166 FADEPTGNLDSATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLIDR 224
Cdd:COG4987 494 LLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-224 |
5.60e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 152.98 E-value: 5.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLaghalGDLDED-------QRARVRA--AHVGFVF 93
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-----GDITIDtarslsqQKGLIRQlrQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 94 QSFQLLDSLDALENVM---LPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:PRK11264 92 QNFNLFPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 171 TGNLD-SATGERISDL--LFELNRergtTLVLVTHDERLAHR-CRRLIRLESGRLIDR 224
Cdd:PRK11264 172 TSALDpELVGEVLNTIrqLAQEKR----TMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-223 |
9.85e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 152.09 E-value: 9.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRA--AHVGFVFQSFQ 97
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLlrQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 98 LLDSLDALENVM-LPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:COG4161 93 LWPHLTVMENLIeAPCKVLGlsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 175 DSATGERISDLLFELNrERGTTLVLVTHDERLAHR-CRRLIRLESGRLID 223
Cdd:COG4161 173 DPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKvASQVVYMEKGRIIE 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-222 |
1.74e-45 |
|
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: 151.05 E-value: 1.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKvvgsAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvr 85
Cdd:cd03219 1 LEVRGLTK----RFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aAHVGFVFQSFQLLDSLDALENVMLPLEL------------EGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVA 153
Cdd:cd03219 75 -LGIGRTFQIPRLFPELTVLENVMVAAQArtgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 154 IARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDmDVVMSLADRVTVLDQGRVI 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-223 |
6.72e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.78 E-value: 6.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASIlnaQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgDL---- 76
Cdd:PRK11124 1 MSIQL---NGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFsktp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 DEDQRARVRAaHVGFVFQSFQLLDSLDALENVM-LPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVA 153
Cdd:PRK11124 73 SDKAIRELRR-NVGMVFQQYNLWPHLTVQQNLIeAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 154 IARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGRLID 223
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-204 |
1.21e-44 |
|
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: 148.56 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaHVGFVFQSFQLL 99
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR------DIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKvpKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180
....*....|....*....|....*..
gi 15598053 178 TGERISDLLFELNRERGTTLVLVTHDE 204
Cdd:cd03301 165 LRVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
24-220 |
1.15e-43 |
|
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: 144.45 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLL-DSL 102
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK----NIAYVPQDPFLFsGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 daLENVmlplelegradarqrarellervglgqrlghyprqLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:cd03228 93 --RENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598053 183 SDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGR 220
Cdd:cd03228 136 LEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-207 |
1.67e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 149.46 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASIlnaQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLdedq 80
Cdd:PRK10851 1 MSIEI---ANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARVRaaHVGFVFQSFQLLDSLDALENV-----MLPL-ELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAI 154
Cdd:PRK10851 70 HARDR--KVGFVFQHYALFRHMTVFDNIafgltVLPRrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 155 ARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLA 207
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-207 |
2.58e-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: 145.94 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaH 88
Cdd:cd03296 6 RNVSKRFGDF----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER------N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEGR------ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRserppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLA 207
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-222 |
4.14e-43 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 145.33 E-value: 4.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgdldEDQRARVRAAHVGFVFQSFQLL 99
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ------DATRVHARDRKIGFVFQHYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLELEGRADARQRAR--ELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:TIGR00968 85 KHLTVRDNIAFGLEIRKHPKAKIKARveELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598053 178 TGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEvADRIVVMSNGKIE 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-203 |
9.52e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.80 E-value: 9.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSK-------VVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAL 73
Cdd:COG4608 3 MAEPLLEVRDLKKhfpvrggLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 74 GDLDEDQRARVRAaHVGFVFQsfqllDSLDAL-------ENVMLPLELEG---RADARQRARELLERVGLGQR-LGHYPR 142
Cdd:COG4608 83 TGLSGRELRPLRR-RMQMVFQ-----DPYASLnprmtvgDIIAEPLRIHGlasKAERRERVAELLELVGLRPEhADRYPH 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 143 QLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-171 |
1.34e-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: 141.25 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLLDSLDA 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 105 LENVMLPLELEG--RADARQRARELLERVGLG----QRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGlsKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-204 |
1.45e-42 |
|
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: 147.11 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvr 85
Cdd:TIGR03265 5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aaHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:TIGR03265 77 --DYGIVFQSYALFPNLTVADNIAYGLKNRGmgRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDE 204
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQ 195
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-222 |
2.12e-42 |
|
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: 141.42 E-value: 2.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSfqll 99
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR----KIAYVPQA---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 dsldalenvmlplelegradarqrarelLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATG 179
Cdd:cd03214 82 ----------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 180 ERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-210 |
3.78e-42 |
|
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: 142.57 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSAsILNAQNLSK-----VVGSAEgkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAgHALGD 75
Cdd:COG4778 1 MTT-LLEVENLSKtftlhLQGGKR--LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 76 LD-----EDQRARVRAAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGH-YPRQLSGG 147
Cdd:COG4778 77 VDlaqasPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGvdREEARARARELLARLNLPERLWDlPPATFSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 148 EQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD----ERLAHRC 210
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDeevrEAVADRV 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-222 |
9.40e-42 |
|
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: 140.89 E-value: 9.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 26 HDLSLDL-ARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQSFQLLDSLDA 104
Cdd:cd03297 13 FTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISD 184
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598053 185 LLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQ 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-224 |
1.61e-41 |
|
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: 149.60 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLL-DSL 102
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR----QIGVVLQDVFLFsGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 daLENVMLpleleGRADA-RQRARELLERVGLGQ-----------RLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:COG2274 566 --RENITL-----GDPDAtDEEIIEAARLAGLHDfiealpmgydtVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598053 171 TGNLDSATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLIDR 224
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-223 |
2.80e-41 |
|
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: 141.41 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 19 EGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhaLGDLDEDQRARVRAaHVGFVFQS--F 96
Cdd:TIGR04520 12 ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRK-KVGMVFQNpdN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSL---D---ALENVMLPlelegRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:TIGR04520 89 QFVGATvedDvafGLENLGVP-----REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 171 TGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLID 223
Cdd:TIGR04520 164 TSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVA 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-224 |
3.21e-41 |
|
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: 147.21 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 11 LSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVG 90
Cdd:COG4988 339 LEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR----QIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 91 FVFQSFQLL-DSLdaLENVMLpleleGRADA-RQRARELLERVGLGQ-----------RLGHYPRQLSGGEQQRVAIARA 157
Cdd:COG4988 415 WVPQNPYLFaGTI--RENLRL-----GRPDAsDEELEAALEAAGLDEfvaalpdgldtPLGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 158 FAAEPDVLFADEPTGNLDSATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLIDR 224
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-220 |
1.81e-40 |
|
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: 135.84 E-value: 1.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 8 AQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraa 87
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 88 HVGFVFQsfqlldsldalenvmlplelegradarqrarellervglgqrlghyprqLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598053 168 DEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGR 220
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-203 |
2.25e-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: 138.24 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEgkltiLHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvr 85
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aaHVGFVFQSFQLLDSLDALENVM--LPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03299 72 --DISYVPQNYALFPHMTVYKNIAygLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-221 |
2.33e-40 |
|
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: 135.99 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvr 85
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aahVGFVFQSFQLLDSLDALENVmlplelegradarqrarellervglgqrlghyprQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:cd03230 75 ---IGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 166 FADEPTGNLDSATGERISDLLFELNRErGTTLVLVTHDERLAHR-CRRLIRLESGRL 221
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-221 |
2.72e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 137.70 E-value: 2.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaHVGFVFQSFQLLDSLDA 104
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLPLELEGRA--DARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:PRK10908 97 YDNVAIPLIIAGASgdDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598053 183 SDLLFELNRErGTTLVLVTHDERL-AHRCRRLIRLESGRL 221
Cdd:PRK10908 177 LRLFEEFNRV-GVTVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-203 |
3.30e-40 |
|
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: 136.89 E-value: 3.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldedQRARVRAAHVGFVFQSFQLLDS- 101
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---------KPLEKERKRIGYVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 -LDALENVMLPLELEG------RADARQRARELLERVGLGQrLGHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:cd03235 84 pISVRDVVLMGLYGHKglfrrlSKADKAKVDEALERVGLSE-LADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190
....*....|....*....|....*....|
gi 15598053 174 LDSATGERISDLLFELNRErGTTLVLVTHD 203
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHD 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-223 |
5.79e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 137.90 E-value: 5.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGS-----AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDE 78
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 79 DQRARVRAAhVGFVFQsfqllDSLDA----------LENVMLPLELEGRADARQRARELLERVGL----GQRLghyPRQL 144
Cdd:PRK10419 82 AQRKAFRRD-IQMVFQ-----DSISAvnprktvreiIREPLRHLLSLDKAERLARASEMLRAVDLddsvLDKR---PPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 145 SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLID 223
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-203 |
1.29e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.73 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVrLAGHA-LGDLDEDQRarvraahvgFVFQSFQL 98
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTApLAEAREDTR---------LMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 LDSLDALENVMLPLelegRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:PRK11247 93 LPWKKVIDNVGLGL----KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180
....*....|....*....|....*
gi 15598053 179 GERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK11247 169 RIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-210 |
1.40e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.04 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 29 SLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvraahVGFVFQSFQLLDSLDALENV 108
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP------VSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 109 MLPLELEGRADARQRAR--ELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLL 186
Cdd:COG3840 93 GLGLRPGLKLTAEQRAQveQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180
....*....|....*....|....*...
gi 15598053 187 FELNRERGTTLVLVTHD----ERLAHRC 210
Cdd:COG3840 173 DELCRERGLTVLMVTHDpedaARIADRV 200
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-223 |
1.79e-39 |
|
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: 136.86 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGS-----AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDE 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 79 DQRARVRAaHVGFVFQsfqllDSLDAL-------ENVMLPLE-LEGRADARQRAR--ELLERVGL-GQRLGHYPRQLSGG 147
Cdd:TIGR02769 81 KQRRAFRR-DVQLVFQ-----DSPSAVnprmtvrQIIGEPLRhLTSLDESEQKARiaELLDMVGLrSEDADKLPRQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 148 EQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLID 223
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-203 |
4.86e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 135.21 E-value: 4.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldedQRARVRAAHVGFVFQSFQLLDSLD 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---------KPVEGPGAERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGER 181
Cdd:PRK11248 87 VQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 15598053 182 ISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-222 |
6.15e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.86 E-value: 6.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVR 85
Cdd:COG4559 2 LEAENLSVRLGGR----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 A-----AHVGFVFQsfqlldsldALENVMLPLE--LEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAF 158
Cdd:COG4559 78 AvlpqhSSLAFPFT---------VEEVVALGRAphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 159 A-------AEPDVLFADEPTGNLDSATGERISDLLFELNReRGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQyADRILLLHQGRLV 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-207 |
7.56e-39 |
|
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: 136.47 E-value: 7.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 40 IVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaHVGFVFQSFQLLDSLDALENVMLPLEL--EGR 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR------HINMVFQSYALFPHMTVEENVAFGLKMrkVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 118 ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTL 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170
....*....|
gi 15598053 198 VLVTHDERLA 207
Cdd:TIGR01187 155 VFVTHDQEEA 164
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-204 |
7.67e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.77 E-value: 7.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKvvgSAEGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQ 80
Cdd:PRK09452 10 SLSPLVELRGISK---SFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RarvraaHVGFVFQSFQLLDSLDALENVMLPLELEGR--ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAF 158
Cdd:PRK09452 86 R------HVNTVFQSYALFPHMTVFENVAFGLRMQKTpaAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598053 159 AAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDE 204
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQ 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-227 |
1.76e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 133.94 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAL------- 73
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 74 GDL---DEDQRARVRAaHVGFVFQSFQLLDSLDALENVM-LPLELEG--RADARQRARELLERVGLGQRL-GHYPRQLSG 146
Cdd:PRK10619 77 GQLkvaDKNQLRLLRT-RLTMVFQHFNLWSHMTVLENVMeAPIQVLGlsKQEARERAVKYLAKVGIDERAqGKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 147 GEQQRVAIARAFAAEPDVLFADEPTGNLDSatgERISDLLFELNR--ERGTTLVLVTHDERLA-HRCRRLIRLESGRLID 223
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQlaEEGKTMVVVTHEMGFArHVSSHVIFLHQGKIEE 232
|
....
gi 15598053 224 RVEP 227
Cdd:PRK10619 233 EGAP 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-203 |
2.98e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 133.42 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSAsILNAQNLSKVVGSAEG-----KLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGD 75
Cdd:COG4167 1 MSA-LLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 76 LDEDQRARvraaHVGFVFQ----SF-------QLLDsldalenvmLPLELEGRADARQRAR---ELLERVGL-GQRLGHY 140
Cdd:COG4167 80 GDYKYRCK----HIRMIFQdpntSLnprlnigQILE---------EPLRLNTDLTAEEREErifATLRLVGLlPEHANFY 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 141 PRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:COG4167 147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-222 |
3.21e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.97 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVR 85
Cdd:PRK13548 3 LEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 A-----AHVGFVFQsfqlldsldALENVML---PLELeGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARA 157
Cdd:PRK13548 79 AvlpqhSSLSFPFT---------VEEVVAMgraPHGL-SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 158 FA------AEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-222 |
1.16e-37 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 134.05 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKvvgsaEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArv 84
Cdd:NF040840 1 MIRIENLSK-----DWKEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 raahVGFVFQSFQLLDSLDALENVMLPLELE--GRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:NF040840 74 ----IAYVYQNYMLFPHKTVFENIAFGLKLRkvPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTH--DERLAHRCRRLIRLeSGRLI 222
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHnfEEALSLADRVGIML-NGRLS 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-220 |
1.35e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.63 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraAHVGFVFQSFQLL 99
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR---AGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENvmlpLELEGRADARQRARELLERV-----GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:cd03224 88 PELTVEEN----LLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598053 175 DSATGERISDLLFELNRErGTTLVLVTHDERLA-HRCRRLIRLESGR 220
Cdd:cd03224 164 APKIVEEIFEAIRELRDE-GVTILLVEQNARFAlEIADRAYVLERGR 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-209 |
3.42e-37 |
|
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: 135.97 E-value: 3.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSK-------VVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTL-LGLLaGLdQPSGGEVRLAGHALGDL 76
Cdd:COG4172 275 LLEARDLKVwfpikrgLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 DEDQRARVRAaHVGFVFQsfqllD---SLD----ALENVMLPLELEG----RADARQRARELLERVGLGQRLGH-YPRQL 144
Cdd:COG4172 353 SRRALRPLRR-RMQVVFQ-----DpfgSLSprmtVGQIIAEGLRVHGpglsAAERRARVAEALEEVGLDPAARHrYPHEF 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598053 145 SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD----ERLAHR 209
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlavvRALAHR 495
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-219 |
3.92e-37 |
|
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: 128.91 E-value: 3.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 11 LSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldEDQRARVRAAHVG 90
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 91 FVFQS--FQLLDSLDALEnvmLPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFAD 168
Cdd:cd03226 75 YVMQDvdYQLFTDSVREE---LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598053 169 EPTGNLDSATGERISDLLFELNRErGTTLVLVTHDERLAHR-CRRLIRLESG 219
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKvCDRVLLLANG 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-222 |
1.22e-36 |
|
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: 127.61 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvraahVGFVFQSFQLLDSLDALE 106
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 107 NVMLPLE--LEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISD 184
Cdd:cd03298 90 NVGLGLSpgLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598053 185 LLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRIA 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-203 |
1.86e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.47 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKV------VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALG 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHypvkrgLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 75 DLDEDQRARVRAAhVGFVFQSfqLLDSL-------DALENvmlPLELE---GRADARQRARELLERVGLgqRLGH---YP 141
Cdd:PRK11308 81 KADPEAQKLLRQK-IQIVFQN--PYGSLnprkkvgQILEE---PLLINtslSAAERREKALAMMAKVGL--RPEHydrYP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 142 RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-224 |
1.58e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.83 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRARVRaAHVGFVFQSFQLLdSLD 103
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV---DIRDLTLESLR-RQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLpleleGRADA-RQRARELLERV-----------GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:COG1132 430 IRENIRY-----GRPDAtDEEVEEAAKAAqahefiealpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 172 GNLDSATGERISDLLFELNRERgtTLVLVTHdeRLA--HRCRRLIRLESGRLIDR 224
Cdd:COG1132 505 SALDTETEALIQEALERLMKGR--TTIVIAH--RLStiRNADRILVLDDGRIVEQ 555
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-203 |
1.70e-35 |
|
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: 125.27 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvraahvgfVFQSFQLLDSLDA 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLPLE--LEGRADARQRA--RELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGE 180
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 15598053 181 RISDLLFELNRERGTTLVLVTHD 203
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHD 174
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-220 |
1.75e-35 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 127.92 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKS----TLLGLLAGlDQPSGGEVRLAGHALGDL 76
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 DEDQRARVRAAHVGFVFQsfqllDSLDAL-------ENVMLPLELE---GRADARQRARELLERVGLG---QRLGHYPRQ 143
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQ-----DPMTSLnpymrvgEQLMEVLMLHkgmSKAEAFEESVRMLDAVKMPearKRMKMYPHE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 144 LSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGR 220
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR 239
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-222 |
2.05e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 125.36 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKvvgsAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGdlDEDQRARvr 85
Cdd:COG4555 2 IEVENLSK----KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--KEPREAR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGlfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHImQEVEALCDRVVILHKGKVV 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-222 |
2.06e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.67 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQ--SFQLLDSL 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVMLPLELE-GRADARQRARELLERVGLGQR-LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGE 180
Cdd:PRK13634 103 VEKDICFGPMNFGvSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598053 181 RISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTVF 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-222 |
2.98e-35 |
|
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: 127.91 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDldeDQRARVRAAH---VGFVFQSFQLLDSLD 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD---SARGIFLPPHrrrIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERIS 183
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598053 184 DLLFELNRERGTTLVLVTHD----ERLAhrcRRLIRLESGRLI 222
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSldevARLA---DHVVLLEQGRVV 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-204 |
3.37e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.13 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAG-LDQP--SGGEVRLAGHALGDLDEDQRarvraaHVGFVFQSFQLL 99
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQR------RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPL-ELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:COG4136 89 PHLSVGENLAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180
....*....|....*....|....*.
gi 15598053 179 GERISDLLFELNRERGTTLVLVTHDE 204
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-222 |
3.85e-35 |
|
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: 124.02 E-value: 3.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 8 AQNLSKVVGSAEGkltiLHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgdlDEDQRARVRAA 87
Cdd:cd03265 3 VENLVKKYGDFEA----VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH-----DVVREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 88 HVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWENLYIHARLYGvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 166 FADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRII 211
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-227 |
3.98e-35 |
|
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: 124.40 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 26 HDLSLDLARGDSLAIVGSSGSGKST----LLGLLAGLDQPSGGEVRLAGHALGDLdedqraRVRAAHVGFVFQ----SFQ 97
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQnprtAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 98 LLDSL--DALENVMLPLELEgrADARQRARELLERVGLGQR---LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:TIGR02770 77 PLFTMgnHAIETLRSLGKLS--KQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 173 NLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRC-RRLIRLESGRLIDRVEP 227
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRIVERGTV 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-227 |
6.57e-35 |
|
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: 129.54 E-value: 6.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQ-----------------------PS 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 63 ---------GGEVRLAGHALGDLDEDQRARVRAaHVGFVFQ-SFQLLDSLDALENVMLPLELEGRA--DARQRARELLER 130
Cdd:TIGR03269 77 kvgepcpvcGGTLEPEEVDFWNLSDKLRRRIRK-RIAIMLQrTFALYGDDTVLDNVLEALEEIGYEgkEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 131 VGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTH-DERLAHR 209
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPEVIEDL 235
|
250
....*....|....*...
gi 15598053 210 CRRLIRLESGRLIDRVEP 227
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTP 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-227 |
8.85e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.74 E-value: 8.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdlDEDQRARVRAaHVGFVFQS--FQLL--- 99
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRR-QVGMVFQNpdNQFVgat 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 ---DSLDALENVMLPlelegRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK13635 99 vqdDVAFGLENIGVP-----REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13635 174 RGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-225 |
1.37e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.88 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEGkltiLHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAG-----HALGD 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 76 LDEDQRARVRAAHVGFVFQsfqllDSLDALE-------NVMLPLELEGR---ADARQRARELLERVGLGQ-RLGHYPRQL 144
Cdd:PRK11701 78 LSEAERRRLLRTEWGFVHQ-----HPRDGLRmqvsaggNIGERLMAVGArhyGDIRATAGDWLERVEIDAaRIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 145 SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD----ERLAHrcrRLIRLESGR 220
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlavaRLLAH---RLLVMKQGR 229
|
250
....*....|
gi 15598053 221 -----LIDRV 225
Cdd:PRK11701 230 vvesgLTDQV 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-221 |
2.45e-34 |
|
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: 120.78 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 18 AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQ 97
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD----HVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 98 LLDSLDAlENVmlplelegradarqrarellervglgqrlghyprqLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:cd03246 87 LFSGSIA-ENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 178 TGERISDLLFELnRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:cd03246 131 GERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-204 |
7.78e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.06 E-value: 7.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaHVGFVFQSFQLL 99
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR------DICMVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLELEGRADA--RQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:PRK11432 91 PHMSLGENVGYGLKMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180
....*....|....*....|....*..
gi 15598053 178 TGERISDLLFELNRERGTTLVLVTHDE 204
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-207 |
9.16e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.56 E-value: 9.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKvvgSAEGKLTIlHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArv 84
Cdd:PRK11607 19 LLEIRNLTK---SFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 raahVGFVFQSFQLLDSLDALENVMLPLELE--GRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:PRK11607 93 ----INMMFQSYALFPHMTVEQNIAFGLKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLA 207
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-221 |
1.29e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 121.27 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGSAEGkltiLHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL---DQPSGGEVRLAGHAL---GDLD 77
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVqreGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 78 EDQRARvrAAHVGFVFQSFQLLDSLDALENVMLP-----------LELEGRADaRQRARELLERVGLGQRLGHYPRQLSG 146
Cdd:PRK09984 79 RDIRKS--RANTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 147 GEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRL 221
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-204 |
1.49e-33 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 123.60 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 15 VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvraahVGFVFQ 94
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGakKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190
....*....|....*....|....*....|..
gi 15598053 173 NLDSATGERISDLLFELNRERGTTLVLVTHDE 204
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-210 |
3.02e-33 |
|
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: 120.09 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL-DQPSG----GEVRLAGHALGDLDED 79
Cdd:TIGR00972 1 AIEIENLNLFYG----EKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPGvrieGKVLFDGQDIYDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 80 QRArVRAaHVGFVFQSFQLLdSLDALENVMLPLELEG---RADARQRARELLERVGL----GQRLGHYPRQLSGGEQQRV 152
Cdd:TIGR00972 77 VVE-LRR-RVGMVFQKPNPF-PMSIYDNIAYGPRLHGikdKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 153 AIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERgTTLVLVTHDERLAHRC 210
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKK-YTIVIVTHNMQQAARI 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
23-202 |
3.34e-33 |
|
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: 119.80 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQP-SGGEVRLAGHALG--DLDEdqrarVRAaHVGFVfqSFQLL 99
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGgeDVWE-----LRK-RIGLV--SPALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVM------------LPLELEgrADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:COG1119 89 LRFPRDETVLdvvlsgffdsigLYREPT--DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190
....*....|....*....|....*....|....*
gi 15598053 168 DEPTGNLDSATGERISDLLFELNRERGTTLVLVTH 202
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-209 |
7.53e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.59 E-value: 7.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 2 SASILNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdldedQR 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGV----KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV------RF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 82 ARVRAAH---VGFVFQSFQLLDSLDALENVMLPLELEG-----RADARQRARELLERVGL----GQRLGHyprqLSGGEQ 149
Cdd:COG1129 71 RSPRDAQaagIAIIHQELNLVPNLSVAENIFLGREPRRgglidWRAMRRRARELLARLGLdidpDTPVGD----LSVAQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598053 150 QRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTH--DE--RLAHR 209
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHrlDEvfEIADR 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-222 |
7.94e-33 |
|
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: 117.77 E-value: 7.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDqrarvr 85
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aaHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03269 71 --RIGYLPEERGLYPKMKVIDQLVYLAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-222 |
1.12e-32 |
|
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: 118.20 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdLDEDQRARVRAAHVGFVF-QSFQLLDSLD 103
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGER 181
Cdd:cd03267 112 VIDSFYLLAAIYDlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 182 ISDLLFELNRERGTTLVLVTHDER-LAHRCRRLIRLESGRLI 222
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLL 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-222 |
1.92e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.81 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRARVRaaHVGFVF-QSFQLLDSLD 103
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY---VPFKRRKEFAR--RIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENvmlpLELEGR------ADARQRARELLERVGLGQRLgHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:COG4586 113 AIDS----FRLLKAiyripdAEYKKRLDELVELLDLGELL-DTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTHD----ERLahrCRRLIRLESGRLI 222
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDmddiEAL---CDRVIVIDHGRII 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-209 |
3.44e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.12 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKS-TLLGLLAGLDQPS----GGEVRLAGHALGD 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 76 LDEDQRARVRAAHVGFVFQsfQLLDSLDALENV------MLPLELEGRAD-ARQRARELLERVGLGQ---RLGHYPRQLS 145
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQ--EPMVSLNPLHTLekqlyeVLSLHRGMRREaARGEILNCLDRVGIRQaakRLTDYPHQLS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 146 GGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD----ERLAHR 209
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlsivRKLADR 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-210 |
3.92e-32 |
|
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: 116.45 E-value: 3.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSaeGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGdldeDQRARVR 85
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELNRERgtTLVLVTHD----ERLAHRC 210
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSmdeaEALCDRI 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-227 |
7.67e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.90 E-value: 7.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgDLDEDQ 80
Cdd:COG3845 1 MMPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RArvRAAHVGFVFQSFQLLDSLDALENVMLPLE-----LEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIA 155
Cdd:COG3845 76 DA--IALGIGMVHQHFMLVPNLTVAENIVLGLEptkggRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 156 RAFAAEPDVLFADEPTGNLdsaTGERISDLLFELNR--ERGTTLVLVTH--DE--RLAHRC---RRlirlesGRLIDRVE 226
Cdd:COG3845 154 KALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHklREvmAIADRVtvlRR------GKVVGTVD 224
|
.
gi 15598053 227 P 227
Cdd:COG3845 225 T 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-222 |
1.38e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 115.46 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraAHVGFVFQSFQLL 99
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR---LGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLElegRADARQRARELLERVG-----LGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:COG0410 91 PSLTVEENLLLGAY---ARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 175 DSATGERISDLLFELNRErGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:COG0410 168 APLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEiADRAYVLERGRIV 215
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
18-227 |
2.77e-31 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 117.40 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 18 AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSG--GEVRLAGHALGDLDEDQRarvraaHVGFVFQS 95
Cdd:TIGR03258 14 AYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKR------GLALLFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 96 FQLLDSLDALENVMLPLELE--GRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:TIGR03258 88 YALFPHLKVEDNVAFGLRAQkmPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 174 LDSATGERISDLLFELNRE-RGTTLVLVTHDERLA-HRCRRLIRLESGRLIDRVEP 227
Cdd:TIGR03258 168 LDANIRANMREEIAALHEElPELTILCVTHDQDDAlTLADKAGIMKDGRLAAHGEP 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-216 |
2.86e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 119.70 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 11 LSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVG 90
Cdd:TIGR02857 324 FSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD----QIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 91 FVFQSFQLLDSLDAlENVMLpleleGRADARQRA-RELLERVGLGQ-----------RLGHYPRQLSGGEQQRVAIARAF 158
Cdd:TIGR02857 400 WVPQHPFLFAGTIA-ENIRL-----ARPDASDAEiREALERAGLDEfvaalpqgldtPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 159 AAEPDVLFADEPTGNLDSATGERISDLLFELnrERGTTLVLVTHDERLAHRCRRLIRL 216
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-202 |
8.26e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.98 E-value: 8.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL--DQPSG---GEVRLAGHALGDLDEDQrARVRAaHVGFVFQ 94
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYDPDVDV-VELRR-RVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 S--------FqlldsldalENVMLPLELEG---RADARQRARELLERVGLGQ----RLGHYPRQLSGGEQQRVAIARAFA 159
Cdd:COG1117 100 KpnpfpksiY---------DNVAYGLRLHGiksKSELDEIVEESLRKAALWDevkdRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598053 160 AEPDVLFADEPTGNLDSATGERISDLLFELNRERgtTLVLVTH 202
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTH 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-221 |
1.08e-30 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 118.31 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLskVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvr 85
Cdd:COG4618 331 LSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aaHVGFVFQSFQLLDSLDAlENV-MLPlELEGRA--DARQRAR--ELLERV--GLGQRLGHYPRQLSGGEQQRVAIARAF 158
Cdd:COG4618 407 --HIGYLPQDVELFDGTIA-ENIaRFG-DADPEKvvAAAKLAGvhEMILRLpdGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 159 AAEPDVLFADEPTGNLDSAtGER-----ISDLlfelnRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDE-GEAalaaaIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-203 |
1.08e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.86 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 8 AQNLSKVVGsaeGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHA-LG------DLDEDQ 80
Cdd:COG0488 1 LENLSKSFG---GR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrIGylpqepPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARvraahvGFVFQSF----QLLDSLDALENVMLPLELEGRA--------------DARQRARELLERVGLGQRLGHYP- 141
Cdd:COG0488 77 TVL------DTVLDGDaelrALEAELEELEAKLAEPDEDLERlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPv 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 142 RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLfelnRERGTTLVLVTHD 203
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-222 |
1.30e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 114.41 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 22 LTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEV----------RLAGHALGDLDED--QRARVRAA-- 87
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLviQKTRFKKIkk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 88 ------HVGFVFQ--SFQLLDSlDALENVML-PLEL-EGRADARQRARELLERVGLGQR-LGHYPRQLSGGEQQRVAIAR 156
Cdd:PRK13651 100 ikeirrRVGVVFQfaEYQLFEQ-TIEKDIIFgPVSMgVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 157 AFAAEPDVLFADEPTGNLDSATGERISDLLFELNRErGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFFKDGKII 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-222 |
1.93e-30 |
|
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: 111.86 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldedqraRVR---AAHVGFvfqsf 96
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSsllGLGGGF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 qlLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLgHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:cd03220 96 --NPELTGRENIYLNGRLLGlsRKEIDEKIDEIIEFSELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 174 LDSATGERISDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:cd03220 173 GDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-222 |
2.13e-30 |
|
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: 111.91 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDedqrARVRAAHVGFVFQSFQLL-DSLD 103
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADLRRNIGYVPQDVTLFyGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 alENVMLpleleGRADAR-QRARELLERVGLGQRLGHYP-----------RQLSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:cd03245 96 --DNITL-----GAPLADdERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 172 GNLDSATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLI 222
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-216 |
2.18e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlaghalgdldedqraRVRAAHVGFVFQSFQLLDSL 102
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------------RAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DA--LENVML----PLELEGRADARQRAR--ELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:NF040873 71 PLtvRDLVAMgrwaRRGLWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 175 DSATGERISDLLFELnRERGTTLVLVTHDERLAHRCRRLIRL 216
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-223 |
3.57e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 113.68 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKS-TLLGLLAGLDQP---SGGEVRLAGHALGDLDED 79
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 80 QRARVRAAHVGFVFQS------------FQLLDSLDALENvmlplelEGRADARQRARELLERVGL---GQRLGHYPRQL 144
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDpmtslnpcytvgFQIMEAIKVHQG-------GNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 145 SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERL-AHRCRRLIRLESGRLID 223
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQVVE 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-227 |
6.19e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 6.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQ--SFQLLDSl 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVML-PLELEGRAD-ARQRARELLERVGLGQRL-GHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATG 179
Cdd:PRK13641 102 TVLKDVEFgPKNFGFSEDeAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 180 ERISDLLFELNRErGTTLVLVTHD-ERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13641 182 KEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-222 |
9.77e-30 |
|
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: 109.98 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGsaegKLTILHDLSLDLARGdSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDldedQRARVR 85
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AaHVGFVFQSFQLLDSLDALENVMLPLELEGRADARQRAR--ELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03264 72 R-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARvdEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELNRERgtTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-223 |
1.44e-29 |
|
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: 110.69 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 3 ASILNAQNLSKVVGSAEGkltiLHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRL-----AGHALGDLD 77
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 78 EDQRARVRAAHVGFVFQSFQ--LLDSLDALENV---MLPLELEGRADARQRARELLERVGLGQ-RLGHYPRQLSGGEQQR 151
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRdgLRMRVSAGANIgerLMAIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 152 VAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAH-RCRRLIRLESGRLID 223
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVE 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-202 |
1.47e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL-----DQPSGGEVRLAGHALGDLD- 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 78 EDQRARVRaahvgFVFQSFQLLDSLDALENVMLPLEL----EGRADARQRARELLERVGLGQ----RLGHYPRQLSGGEQ 149
Cdd:PRK14247 78 IELRRRVQ-----MVFQIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 150 QRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRErgTTLVLVTH 202
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTH 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-222 |
1.50e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLS-KVVGSAEGKLTI-LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRA 82
Cdd:PRK13633 4 MIKCKNVSyKYESNEESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 83 RVRAahvGFVFQS--FQLL------DSLDALENVMLPLElegraDARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAI 154
Cdd:PRK13633 84 RNKA---GMVFQNpdNQIVativeeDVAFGPENLGIPPE-----EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 155 ARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLI 222
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
1.61e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 111.35 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDedqrarv 84
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 rAAHVGFV------FQSFQLLDSLDALenvmlpLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIAR 156
Cdd:COG4152 70 -RRRIGYLpeerglYPKMKVGEQLVYL------ARLKGlsKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 157 AFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD----ERLahrCRRLIRLESGRLI 222
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQmelvEEL---CDRIVIINKGRKV 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-209 |
2.20e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.32 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL-----DQPSGGEVRLAGHALGDLDEDQrARVRAaHVGFVFQ 94
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDP-IEVRR-EVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDSLDALENVMLPLELEGRADARQrarELLERVG-----------LGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLVKSKK---ELDERVEwalkkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELNRErgTTLVLVTHDERLAHR 209
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAAR 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-227 |
2.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.60 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQ--SFQLLDSl 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVMLPLELEG--RADARQRARELLERVGLGQRL-GHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATG 179
Cdd:PRK13649 102 TVLKDVAFGPQNFGvsQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 180 ERISDLLFELNrERGTTLVLVTH--DErLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13649 182 KELMTLFKKLH-QSGMTIVLVTHlmDD-VANYADFVYVLEKGKLVLSGKP 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
2.61e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.18 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVV--GSAEGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRA 82
Cdd:COG1101 1 MLELKNLSKTFnpGTVNEK-RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 83 RvraaHVGFVFQsfqllD-------SLDALENVML------PLELEGRADARQRA--RELLERVGLG--QRLGHYPRQLS 145
Cdd:COG1101 80 K----YIGRVFQ-----DpmmgtapSMTIEENLALayrrgkRRGLRRGLTKKRRElfRELLATLGLGleNRLDTKVGLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 146 GGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRC-RRLIRLESGRLI 222
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-203 |
2.88e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdlDEDQRARVRAaHVGFVFQ--------SF 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRK-HIGIVFQnpdnqfvgSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSLDALENVMLPLElegraDARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK13648 101 VKYDVAFGLENHAVPYD-----EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180
....*....|....*....|....*..
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHD 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-227 |
2.93e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.08 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 18 AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQrARvraAHVGFVFQS-- 95
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IR---KKIGIIFQNpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 96 FQLL------DSLDALENVMLPlelegRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:PRK13632 94 NQFIgatvedDIAFGLENKKVP-----PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 170 PTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-204 |
3.38e-29 |
|
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: 113.99 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVraahVGFVFQSFQLLDSlD 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLpleleGRADAR-QRARELLERVGLGQ-----------RLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:TIGR02868 425 VRENLRL-----ARPDATdEELWAALERVGLADwlralpdgldtVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 15598053 172 GNLDSATGERISDLLFELnrERGTTLVLVTHDE 204
Cdd:TIGR02868 500 EHLDAETADELLEDLLAA--LSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-222 |
7.38e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.38 E-value: 7.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQrarVRAAhVGFVFQSFQLL-DSL 102
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA-ISVVSQRVHLFsATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DalENvmLPLELEGRADArqRARELLERVGLGQRL----------GHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:PRK11160 431 R--DN--LLLAAPNASDE--ALIEVLQQVGLEKLLeddkglnawlGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 173 NLDSATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLI 222
Cdd:PRK11160 505 GLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-203 |
1.02e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.18 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 21 KLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaHVGFVFQsfqllD 100
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIFQ-----D 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 101 SLDALENVML-------PLELE----GRADARQRARELLERVGLGQRL-GHYPRQLSGGEQQRVAIARAFAAEPDVLFAD 168
Cdd:PRK15079 107 PLASLNPRMTigeiiaePLRTYhpklSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190
....*....|....*....|....*....|....*
gi 15598053 169 EPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-222 |
1.52e-28 |
|
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: 105.86 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDqrarvRAAHVGFVFQSFQLLDSl 102
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPYLFDT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 dalenvmlplelegradarqrarELLERVGlgqrlghypRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:cd03247 90 -----------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598053 183 SDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLI 222
Cdd:cd03247 138 LSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-217 |
1.89e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.21 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlaghalgdldedqraRVRAAHVGFVFQ-SFQLLDS 101
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------------RPAGARVLFLPQrPYLPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDalENVMLPLELEGRADArqRARELLERVGLGQ---RLG---HYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:COG4178 442 LR--EALLYPATAEAFSDA--ELREALEAVGLGHlaeRLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 176 SATGERISDLLfeLNRERGTTLVLVTHDERLAHRCRRLIRLE 217
Cdd:COG4178 518 EENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-223 |
2.48e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKvvgsAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLaGHALgdldedqrarv 84
Cdd:COG0488 315 VLELEGLSK----SYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 raaHVGFvfqsF-QLLDSLDALENVMLPLELEGRADARQRARELLERVGL-GQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:COG0488 379 ---KIGY----FdQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598053 163 DVLFADEPTGNLDSATGERISDLL--FElnrerGtTLVLVTHDERLAHR-CRRLIRLESGRLID 223
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALddFP-----G-TVLLVSHDRYFLDRvATRILEFEDGGVRE 509
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-222 |
7.23e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 107.68 E-value: 7.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPS----GGEVRLAGHALGDLDEDQ 80
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARVRAAHVGFVFQSFQllDSLDA-------LENVMLPLELEGR-----ADARQRARELLERVGLGQR---LGHYPRQLS 145
Cdd:COG4170 83 RRKIIGREIAMIFQEPS--SCLDPsakigdqLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHkdiMNSYPHELT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 146 GGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTITVLYCGQTV 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-227 |
7.65e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.97 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQSFQLLDSLDALE 106
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 107 NVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISD 184
Cdd:PRK10070 126 NTAFGMELAGinAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 185 LLFELNRERGTTLVLVTHDERLAHRC-RRLIRLESGRLIDRVEP 227
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-222 |
9.86e-28 |
|
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: 104.17 E-value: 9.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 3 ASILNAQNLSKVV--GSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSG--GEVRLAGHalgdlde 78
Cdd:cd03213 1 GVTLSFRNLTVTVksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 79 DQRARVRAAHVGFVFQSFQLLDSLDALENVMLPLELegradarqrarellervglgqrlghypRQLSGGEQQRVAIARAF 158
Cdd:cd03213 74 PLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL---------------------------RGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 159 AAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDER--LAHRCRRLIRLESGRLI 222
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSseIFELFDKLLLLSQGRVI 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-209 |
1.25e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.05 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 21 KLTILHD-----LSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldEDQRARVRAAH-VGFVFQ 94
Cdd:PRK10771 6 DITWLYHhlpmrFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-------QDHTTTPPSRRpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDSLDALENVMLPLELEGRADARQRA--RELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGLNPGLKLNAAQREklHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598053 173 NLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR 209
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAAR 195
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-223 |
1.30e-27 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 105.55 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKStlLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQ----SFQLL 99
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQnprsAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDAleNVMLPLELEGRADARQRARELLERVGLGQR---LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK10418 96 HTMHT--HARETCLALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTHD----ERLAHrcrRLIRLESGRLID 223
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDmgvvARLAD---DVAVMSHGRIVE 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-221 |
1.38e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 104.56 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 29 SLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvraahVGFVFQSFQLLDSLDALENV 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 109 MLPLE--LEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLL 186
Cdd:TIGR01277 92 GLGLHpgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598053 187 FELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRL 221
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-223 |
1.40e-27 |
|
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: 109.83 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLLDSlD 103
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ----FINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEGRADARQRARELLE--------RVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:TIGR01193 564 ILENLLLGAKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598053 176 SATGERISDLLFELNRErgtTLVLVTHDERLAHRCRRLIRLESGRLID 223
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-227 |
1.51e-27 |
|
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: 109.12 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAE-GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVR-LAGHALGDLDE---D 79
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMTKpgpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 80 QRARVRAaHVGFVFQSFQLLDSLDALENVM------LPLELegradARQRARELLERVGLGQR-----LGHYPRQLSGGE 148
Cdd:TIGR03269 359 GRGRAKR-YIGILHQEYDLYPHRTVLDNLTeaigleLPDEL-----ARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 149 QQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-221 |
1.58e-27 |
|
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: 107.51 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGD------LDEDQRArvraahVGFVFQSFQLLD 100
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR------IGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 101 SLDALENVMLPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGE 180
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 181 RISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRL 221
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRV 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-209 |
2.21e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.85 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 10 NLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaHV 89
Cdd:PRK11650 5 KLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR------DI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 90 GFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLKIRGmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598053 168 DEPTGNLDSATgeRISDLL--FELNRERGTTLVLVTHDE----RLAHR 209
Cdd:PRK11650 159 DEPLSNLDAKL--RVQMRLeiQRLHRRLKTTSLYVTHDQveamTLADR 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-224 |
2.71e-27 |
|
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: 104.23 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLLDSLD 103
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR----QIGLVSQDVFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 AlENVMLPLELEGRADARQRAR-----ELLERV--GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:cd03251 93 A-ENIAYGRPGATREEVEEAARaanahEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598053 177 ATGERISDLLFELNRERgTTLVlvthderLAHR------CRRLIRLESGRLIDR 224
Cdd:cd03251 172 ESERLVQAALERLMKNR-TTFV-------IAHRlstienADRIVVLEDGKIVER 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-207 |
3.26e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgDLDEDQRARVRAAhVGFVFQSFQllDSLDA 104
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT-VGIVFQNPD--DQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 ---LENVML-PLELE-GRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATG 179
Cdd:PRK13639 94 ptvEEDVAFgPLNLGlSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180
....*....|....*....|....*...
gi 15598053 180 ERISDLLFELNRErGTTLVLVTHDERLA 207
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLV 200
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-227 |
3.79e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQ--SFQLLDsl 102
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALE--------NVMLPLElegraDARQRARELLERVGLGQR-LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:PRK13646 101 DTVEreiifgpkNFKMNLD-----EVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 174 LDSATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-224 |
3.93e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.07 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvraaH 88
Cdd:cd03268 4 NDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPLELEGRADARQraRELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFAD 168
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI--DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 169 EPTGNLDSATGERISDLLFELnRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLIDR 224
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSL-RDQGITVLISSHLlSEIQKVADRIGIINKGKLIEE 207
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-200 |
6.21e-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: 102.99 E-value: 6.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSkvvgSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvr 85
Cdd:TIGR03410 1 LEVSNLN----VYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aAHVGFVFQSFQLLDSLDALENVMLPLELEGRADaRQRARELLE-----RVGLGQRLGhyprQLSGGEQQRVAIARAFAA 160
Cdd:TIGR03410 75 -AGIAYVPQGREIFPRLTVEENLLTGLAALPRRS-RKIPDEIYElfpvlKEMLGRRGG----DLSGGQQQQLAIARALVT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598053 161 EPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLV 200
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLV 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-223 |
1.02e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.20 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAL---GDLDEDQRARVRAaHVGFVFQSFQLLD 100
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRK-EVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 101 SLDALENVMLPLELEGRADARQRAR---ELLERVGLGQ----RLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKiveECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 174 LDSATGERISDLLFELNRErgTTLVLVTHDERLAHRCRRLIR-LESGRLID 223
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAfLYNGELVE 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-227 |
1.03e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.55 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGS-AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRAR 83
Cdd:PRK13631 21 ILRVKNLYCVFDEkQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 VRAAH------------VGFVFQ--SFQLLDslDALE-NVML-PLEL-EGRADARQRARELLERVGLGQR-LGHYPRQLS 145
Cdd:PRK13631 101 TNPYSkkiknfkelrrrVSMVFQfpEYQLFK--DTIEkDIMFgPVALgVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 146 GGEQQRVAIARAFAAEPDVLFADEPTGNLDSAtGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLIDR 224
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILKT 257
|
...
gi 15598053 225 VEP 227
Cdd:PRK13631 258 GTP 260
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-222 |
1.05e-26 |
|
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: 102.30 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 17 SAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDedqRARVRaAHVGFVFQSF 96
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-SMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLdSLDALENVML-----PLELEGRADARQRARELLERV--GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:cd03254 87 FLF-SGTIMENIRLgrpnaTDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598053 170 PTGNLDSATGERISDLLFELNRERgTTLVlvthderLAHR------CRRLIRLESGRLI 222
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGR-TSII-------IAHRlstiknADKILVLDDGKII 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-222 |
1.15e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.85 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldedqraRVRA-AHVGFVFQSfqlldS 101
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVSAlLELGAGFHP-----E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVMLPLELEG--RADARQRARELLERVGLGQRLgHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:COG1134 103 LTGRENIYLNGRLLGlsRKEIDEKFDEIVEFAELGDFI-DQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 179 GERISDLLFELnRERGTTLVLVTHDER-LAHRCRRLIRLESGRLI 222
Cdd:COG1134 182 QKKCLARIREL-RESGRTVIFVSHSMGaVRRLCDRAIWLEKGRLV 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-227 |
1.52e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraAHVGFVFQS--FQLL--- 99
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIR---KLVGIVFQNpeTQFVgrt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 ---DSLDALENVMLPlelegRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK13644 95 veeDLAFGPENLCLP-----PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 177 ATGERISDLLFELNrERGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13644 170 DSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEP 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-222 |
1.91e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQ--SFQLLDSl 102
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVMLPLELEG--RADARQRARELLERVGLGQRLGH-YPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATg 179
Cdd:PRK13643 101 TVLKDVAFGPQNFGipKEKAEKIAAEKLEMVGLADEFWEkSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 180 eRISDL-LFELNRERGTTLVLVTH-DERLAHRCRRLIRLESGRLI 222
Cdd:PRK13643 180 -RIEMMqLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHII 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-224 |
5.01e-26 |
|
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: 100.52 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdLDEDQRARV 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEP 162
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLEYFAGLYGlkGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLIDR 224
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-201 |
7.05e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 100.04 E-value: 7.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGgevRLAGHALGDLDEDQRARVRAaHVGFVFQSFQLLDSLD 103
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG---TTSGQILFNGQPRKPDQFQK-CVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENV--MLPLELEGRADARQRARE----LLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:cd03234 98 VRETLtyTAILRLPRKSSDAIRKKRvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....
gi 15598053 178 TGERISDLLFELnrERGTTLVLVT 201
Cdd:cd03234 178 TALNLVSTLSQL--ARRNRIVILT 199
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-227 |
9.52e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.81 E-value: 9.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdldeDQ 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARVRAAHVGFVFQsfqlLDSLDALENVMLPLELEGR------ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAI 154
Cdd:PRK13537 74 RARHARQRVGVVPQ----FDNLDPDFTVRENLLVFGRyfglsaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 155 ARAFAAEPDVLFADEPTGNLDSATG----ERISDLLfelnrERGTTLVLVTHDERLAHR-CRRLIRLESGRLIDRVEP 227
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARhlmwERLRSLL-----ARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAP 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-218 |
2.21e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 15 VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQ 94
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ----QVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLL-DSLdaLENVMLPLELEGRADARQRARELLERVGLGQRLGHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:PRK10247 89 TPTLFgDTV--YDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598053 173 NLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLES 218
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-222 |
2.32e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.31 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgDLDEDQRARVRAAhVGFVFQS--FQLLdSL 102
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES-VGMVFQDpdNQLF-SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVML-PLELEGRAD-ARQRARELLERVGLgQRLGHYPRQ-LSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATG 179
Cdd:PRK13636 99 SVYQDVSFgAVNLKLPEDeVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 180 ERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-227 |
2.65e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 21 KLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL---DQPSGGEVRLAGHALGdldEDQRARVRAaHVGFVFQS-- 95
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT---AKTVWDIRE-KVGIVFQNpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 96 FQLL------DSLDALENVMLPlelegRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:PRK13640 95 NQFVgatvgdDVAFGLENRAVP-----RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 170 PTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-206 |
2.96e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQ 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGG----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RAR---VRAahvgfvFQSFQLLDSLDALENVML-----------------PLELEGRADARQRARELLERVGLGQRLGHY 140
Cdd:PRK11300 77 IARmgvVRT------FQHVRLFREMTVIENLLVaqhqqlktglfsgllktPAFRRAESEALDRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 141 PRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERL 206
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-209 |
3.18e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.01 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAaHVGFVFQSfqLLDSLDALE 106
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQD--PYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 107 NV----MLPLELEGRAD---ARQRARELLERVGL-GQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:PRK10261 419 TVgdsiMEPLRVHGLLPgkaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190
....*....|....*....|....*....|....*
gi 15598053 179 GERISDLLFELNRERGTTLVLVTHD----ERLAHR 209
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDmavvERISHR 533
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-203 |
4.11e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.07 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 7 NAQNLSKVVGS--AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARV 84
Cdd:PRK11831 3 SVANLVDMRGVsfTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAaHVGFVFQSFQLLDSLDALENVMLPLELEGRADA---RQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAE 161
Cdd:PRK11831 83 RK-RMSMLFQSGALFTDMNVFDNVAYPLREHTQLPApllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 162 PDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-222 |
4.38e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQrarVRAaHVGFVFQS--FQLLdSL 102
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRS-KVGLVFQDpdDQVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVML-PLELE-GRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGE 180
Cdd:PRK13647 96 TVWDDVAFgPVNMGlDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598053 181 RISDLLFELNRErGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEwADQVIVLKEGRVL 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-203 |
5.00e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.63 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 2 SASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKS-TLLGLLAGLDQpSGGEVRLAGH--------- 71
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 72 -ALGDLDEDQRARVRAAHVGFVFQsfQLLDSLDAL----ENVMLPLELE---GRADARQRARELLERVGLGQR---LGHY 140
Cdd:PRK10261 88 iELSEQSAAQMRHVRGADMAMIFQ--EPMTSLNPVftvgEQIAESIRLHqgaSREEAMVEAKRMLDQVRIPEAqtiLSRY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 141 PRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-224 |
7.57e-25 |
|
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: 97.69 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRARVRAaHVGFVFQSFQLLDSlD 103
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ---DIREVTLDSLRR-AIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLpleleGRADARQ-------RARELLERV-----GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:cd03253 91 IGYNIRY-----GRPDATDeevieaaKAAQIHDKImrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 172 GNLDSATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLIDR 224
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-222 |
8.57e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSkvvgSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRAR 83
Cdd:PRK11231 1 MTLRTENLT----VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 vraaHVGFVFQSFQLLDSLDALENVML---P-LELEGR--ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARA 157
Cdd:PRK11231 77 ----RLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 158 FAAEPDVLFADEPTGNLDSATGERISDLLFELNRErGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRyCDHLVVLANGHVM 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-210 |
9.49e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 95.57 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgdldedqrarvr 85
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aahvgfvfqsfqlldsldalenvmlPLELEGRADARQrarellervgLGQRLGHyprQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:cd03216 63 -------------------------EVSFASPRDARR----------AGIAMVY---QLSVGERQMVEIARALARNARLL 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 166 FADEPTGNLDSATGERISDLLFELnRERGTTLVLVTH--DE--RLAHRC 210
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDEvfEIADRV 152
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-222 |
1.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLD---EDQRARVraahvGFVFQ--SFQLL 99
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKV-----GLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLEL-EGRADARQRARELLERVGLGQR--LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK13637 98 EETIEKDIAFGPINLgLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-210 |
3.43e-24 |
|
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: 96.07 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvr 85
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aAHVGFVFQSFQLLDSLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03218 75 -LGIGYLPQEASIFRKLTVEENILAVLEIRGlsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDER----LAHRC 210
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRetlsITDRA 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-221 |
4.17e-24 |
|
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: 99.73 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 14 VVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVF 93
Cdd:TIGR01842 323 TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK----HIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 94 QSFQLLDSLDAlENVMlplELEGRADARQ--------RARELLERV--GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPD 163
Cdd:TIGR01842 399 QDVELFPGTVA-ENIA---RFGENADPEKiieaaklaGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-220 |
4.95e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 92.90 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKvvgsAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlaghalgdldedqrarvr 85
Cdd:cd03221 1 IELENLSK----TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aahvgfvfqsfqlldsldalenvmlplelegradarqrarellerVGLGQRLGHYPrQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:cd03221 59 ---------------------------------------------WGSTVKIGYFE-QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 166 FADEPTGNLDSATGERISDLLFELNRergtTLVLVTHDER-LAHRCRRLIRLESGR 220
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-227 |
5.10e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.40 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLLDSL 102
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVML-------PLELEGRADaRQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:PRK10575 101 TVRELVAIgrypwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 176 SATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLIDRVEP 227
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTP 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-205 |
6.27e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.48 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRAR 83
Cdd:COG1137 2 MTLEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 vraAHVGF------VFQSfqlldsLDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIA 155
Cdd:COG1137 78 ---LGIGYlpqeasIFRK------LTVEDNILAVLELRKlsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 156 RAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTlVLVT-HDER 205
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIG-VLITdHNVR 197
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-224 |
7.47e-24 |
|
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: 99.12 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLdedQRARVRAAhVGFVFQSFQLL-DS 101
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQASLRAA-IGIVPQDTVLFnDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LdaLENVmlpleLEGRADARQ-------RARELLERV-----GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:COG5265 448 I--AYNI-----AYGRPDASEeeveaaaRAAQIHDFIeslpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 170 PTGNLDSATGERISDLLFELNRERgTTLVlvthderLAHR------CRRLIRLESGRLIDR 224
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGR-TTLV-------IAHRlstivdADEILVLEAGRIVER 573
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-221 |
1.07e-23 |
|
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: 93.27 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRarvRAAHVGFV---FQSFQLLDS 101
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVMLPlelegradarqrarellervglgqrlghypRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGER 181
Cdd:cd03215 93 LSVAENIALS------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598053 182 ISDLLFELnRERGTTLVLVTHD-ERLAHRCRRLIRLESGRL 221
Cdd:cd03215 143 IYRLIREL-ADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-203 |
1.69e-23 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 96.02 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQP----SGGEVRLAGHALGDLDEDQ 80
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 81 RARVRAAHVGFVFQSFQllDSLDALENVMLPL-------ELEGRADAR-----QRARELLERVGLGQR---LGHYPRQLS 145
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQ--SCLDPSERVGRQLmqnipgwTYKGRWWQRfgwrkRRAIELLHRVGIKDHkdaMRSFPYELT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 146 GGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-224 |
1.87e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.72 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 7 NAQNLSKVVGSAE---------GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLD 77
Cdd:PRK13657 324 GAIDLGRVKGAVEfddvsfsydNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 78 edqRARVRAAhVGFVFQSFQLLDSLDAlENVMLpleleGRADA----------RQRARELLER--VGLGQRLGHYPRQLS 145
Cdd:PRK13657 404 ---RASLRRN-IAVVFQDAGLFNRSIE-DNIRV-----GRPDAtdeemraaaeRAQAHDFIERkpDGYDTVVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 146 GGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERgTTLVlvthderLAHR------CRRLIRLESG 219
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-TTFI-------IAHRlstvrnADRILVFDNG 545
|
....*
gi 15598053 220 RLIDR 224
Cdd:PRK13657 546 RVVES 550
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-224 |
2.80e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.47 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGSAEG-----KLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAL--GDL 76
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 dedqraRVRAAHVGFVFQS-----------FQLLDsldalenvmLPLELEGRADARQRAREL---LERVGL-GQRLGHYP 141
Cdd:PRK15112 83 ------SYRSQRIRMIFQDpstslnprqriSQILD---------FPLRLNTDLEPEQREKQIietLRQVGLlPDHASYYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 142 RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVT-HDERLAHRCRRLIRLESGR 220
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGE 227
|
....
gi 15598053 221 LIDR 224
Cdd:PRK15112 228 VVER 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-203 |
5.93e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 5.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAegklTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaH 88
Cdd:COG4604 5 KNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLpleleGR---------ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFA 159
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAF-----GRfpyskgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 160 AEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-202 |
7.98e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAlgdlDEDQRARVRAAHVGfvFQSFqLL 99
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACHYLG--HRNA-MK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLELEGRADArqRARELLERVGLgQRLGHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:PRK13539 86 PALTVAENLEFWAAFLGGEEL--DIAAALEAVGL-APLAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....
gi 15598053 179 GERISDLLFElNRERGTTLVLVTH 202
Cdd:PRK13539 163 VALFAELIRA-HLAQGGIVIAATH 185
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
25-224 |
1.07e-22 |
|
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: 95.55 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLdedqRARVRAAHVGFVFQSFQLLDslDA 104
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY----TLASLRRQVALVSQDVVLFN--DT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLPLELEGRADARQR-------ARELLERV--GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:TIGR02203 422 IANNIAYGRTEQADRAEIEralaaayAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 176 SATGERISDLLFELNRERgTTLVlvthderLAHR------CRRLIRLESGRLIDR 224
Cdd:TIGR02203 502 NESERLVQAALERLMQGR-TTLV-------IAHRlstiekADRIVVMDDGRIVER 548
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-205 |
1.08e-22 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 91.95 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGsaegKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARV 84
Cdd:TIGR04406 1 TLVAENLIKSYK----KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 raaHVGFVFQSFQLLDSLDALENVMLPLELEGRADARQRARE---LLERVGLgQRLGHYPRQ-LSGGEQQRVAIARAFAA 160
Cdd:TIGR04406 77 ---GIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERleaLLEEFQI-SHLRDNKAMsLSGGERRRVEIARALAT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 161 EPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDER 205
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVR 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-202 |
1.14e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPS---GGEVRLAGHALGDldEDQRARVraahvGFVFQSF 96
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA--KEMRAIS-----AYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSLDALENVMLPLELEGRADA-----RQRARELLERVGLGQ----RLGHYPRQ--LSGGEQQRVAIARAFAAEPDVL 165
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHLRMPRRVtkkekRERVDEVLQALGLRKcantRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598053 166 FADEPTGNLDSATGERISDLLFELNrERGTTLVLVTH 202
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIH 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-223 |
1.33e-22 |
|
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: 91.78 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSfQLLDSLD 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR----QVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLP---------LELEGRADARQRARELLErvGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:cd03252 92 IRDNIALAdpgmsmervIEAAKLAGAHDFISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 175 DSATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRLID 223
Cdd:cd03252 170 DYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-227 |
1.79e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHA----LGDLDEDQRARvraAHVGFVFQ--SFQL 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVKRLR---KEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 LDSLDALENVMLPLEL-EGRADARQRARELLERVGLGQR-LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK13645 104 FQETIEKDIAFGPVNLgENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-221 |
2.13e-22 |
|
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: 90.99 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVraahVGFVFQSFQLLdSLD 103
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK----VSLVGQEPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPL---ELEGRADARQRAR-----ELLERvGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:cd03248 104 LQDNIAYGLqscSFECVKEAAQKAHahsfiSELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598053 176 SATGERISDLLFELNRERgtTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:cd03248 183 AESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-203 |
2.22e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSkvVGSAEGKLTiLHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDedqRARV 84
Cdd:COG3845 257 VLEVENLS--VRDDRGVPA-LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAAHVGFV---FQSFQLLDSLDALENVML------PLELEG---RADARQRARELLER-----VGLGQRLghypRQLSGG 147
Cdd:COG3845 331 RRLGVAYIpedRLGRGLVPDMSVAENLILgryrrpPFSRGGfldRKAIRAFAEELIEEfdvrtPGPDTPA----RSLSGG 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 148 EQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD 203
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISED 461
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-209 |
4.14e-22 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 90.68 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDedqrARVRAAHVGFVFQSFQLLD-SL 102
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN----LRWLRSQIGLVSQEPVLFDgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 daLENVMLpleleGRADARQrarELLERV---------------GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:cd03249 94 --AENIRY-----GKPDATD---EEVEEAakkanihdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598053 168 DEPTGNLDSATGERISDLLFELNRERgTTLVlvthderLAHR 209
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMKGR-TTIV-------IAHR 197
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-209 |
1.16e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.83 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEGkltiLHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQ--PS---GGEVRLAGHALGD 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 76 LDEDQrARVRAaHVGFVFQS---FqlldSLDALENVMLPLELEGRADaRQRARELLERVGLG--------QRLGHYPRQL 144
Cdd:PRK14239 77 PRTDT-VDLRK-EIGMVFQQpnpF----PMSIYENVVYGLRLKGIKD-KQVLDEAVEKSLKGasiwdevkDRLHDSALGL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 145 SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRErgTTLVLVTHDERLAHR 209
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASR 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-221 |
3.27e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.32 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLLdSLD 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR----QVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEGRADARQRARELLER-------VGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHdfimefpNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 177 atgeRISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:TIGR00958 651 ----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-222 |
3.34e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.36 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 28 LSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdQPSGGEVRLAGHALGDLDEDQRARVRAAHV-----GFVFQSFQLLDsl 102
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSqqqspPFAMPVFQYLA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 dalenvmLPLELEGRADARQRA-RELLERVGLGQRLGHYPRQLSGGEQQRVAIARAF-----AAEPD--VLFADEPTGNL 174
Cdd:COG4138 92 -------LHQPAGASSEAVEQLlAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598053 175 DSATGERISDLLFELnRERGTTLVLVTHDerLAHRCR---RLIRLESGRLI 222
Cdd:COG4138 165 DVAQQAALDRLLREL-CQQGITVVMSSHD--LNHTLRhadRVWLLKQGKLV 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-227 |
3.37e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.89 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQSFQLL 99
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVM------LPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:PRK10253 94 GDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 174 LDSATGERISDLLFELNRERGTTLVLVTHDerLAHRCR---RLIRLESGRLIDRVEP 227
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHD--LNQACRyasHLIALREGKIVAQGAP 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-202 |
3.44e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 15 VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVraaHVGFVFQ 94
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDSLDALENVM---LP------LELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:PRK09700 88 ELSVIDELTVLENLYigrHLtkkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598053 166 FADEPTGNLdsaTGERISDLLFELNRER--GTTLVLVTH 202
Cdd:PRK09700 168 IMDEPTSSL---TNKEVDYLFLIMNQLRkeGTAIVYISH 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-222 |
3.98e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.93 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 26 HDLSLDL---ARGDSlAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDED------QRarvraaHVGFVFQSF 96
Cdd:PRK11144 13 LCLTVNLtlpAQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppeKR------RIGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSLdaleNVMLPLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK11144 86 RLFPHY----KVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598053 177 ATGERISDLLFELNRERGTTLVLVTH--DE--RLAHrcrRLIRLESGRLI 222
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHslDEilRLAD---RVVVLEQGKVK 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-213 |
4.17e-21 |
|
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: 87.03 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSkvvgSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDL-DEDQRARV 84
Cdd:TIGR01189 1 LAARNLA----CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAAHVGFVFQsfqlldSLDALENVMLPLELEGraDARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDV 164
Cdd:TIGR01189 77 YLGHLPGLKP------ELSALENLHFWAAIHG--GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 165 LFADEPTGNLDSAtGERISDLLFELNRERGTTLVLVTHDERLAHRCRRL 213
Cdd:TIGR01189 149 WILDEPTTALDKA-GVALLAGLLRAHLARGGIVLLTTHQDLGLVEAREL 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-224 |
4.37e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 2 SASILNAQNLSKVVGSAEGKL-------TILHDLSLDLARGDSLAIVGSSGSGKST----LLGLLAgldqpSGGEVRLAG 70
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 71 HALGDLDEDQRARVRAaHVGFVFQ--SFQLLDSLDALENVMLPLELEGR----ADARQRARELLERVGLGQRLGH-YPRQ 143
Cdd:PRK15134 347 QPLHNLNRRQLLPVRH-RIQVVFQdpNSSLNPRLNVLQIIEEGLRVHQPtlsaAQREQQVIAVMEEVGLDPETRHrYPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 144 LSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVV 505
|
..
gi 15598053 223 DR 224
Cdd:PRK15134 506 EQ 507
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-203 |
9.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.86 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdlDEDQRARVRAaHVGFVFQS--FQLL-- 99
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRH-KIGMVFQNpdNQFVga 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 ----DSLDALENVMLPLElegraDARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:PRK13650 98 tvedDVAFGLENKGIPHE-----EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180
....*....|....*....|....*...
gi 15598053 176 SATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-224 |
1.59e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.52 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLskVVGSAEGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdQPSGGEVRLAGHALGDLDEDQRARvr 85
Cdd:PRK11174 350 IEAEDL--EILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRK-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 aaHVGFVFQSFQLLD-SLdaLENVMLpleleGRADAR-QRARELLERV-----------GLGQRLGHYPRQLSGGEQQRV 152
Cdd:PRK11174 424 --HLSWVGQNPQLPHgTL--RDNVLL-----GNPDASdEQLQQALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598053 153 AIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNreRGTTLVLVTHdeRLA--HRCRRLIRLESGRLIDR 224
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTH--QLEdlAQWDQIWVMQDGQIVQQ 564
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-212 |
2.04e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.03 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVraahvGFVFQSFQLLDSLDALE 106
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRV-----GYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 107 NvmlpLELEGR------ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGE 180
Cdd:NF033858 359 N----LELHARlfhlpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190
....*....|....*....|....*....|....
gi 15598053 181 RISDLLFELNRERGTTLVLVTH--DErlAHRCRR 212
Cdd:NF033858 435 MFWRLLIELSREDGVTIFISTHfmNE--AERCDR 466
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-202 |
3.15e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.62 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEdqraRVRAAHVGFVFQSFQLL-DSL 102
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH----SVLRQGVAMVQQDPVVLaDTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 daLENVMLpleleGRADARQRARELLERV-----------GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:PRK10790 432 --LANVTL-----GRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190
....*....|....*....|....*....|.
gi 15598053 172 GNLDSATGERISDLLFELnRERgTTLVLVTH 202
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAV-REH-TTLVVIAH 533
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-202 |
3.62e-20 |
|
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: 84.47 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 16 GSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDL-DEDQRARVRAAHVGfvfq 94
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGHAP---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 sfQLLDSLDALENvmlpLELEGRADARQRARELLERVGLGQrLGHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:cd03231 83 --GIKTTLSVLEN----LRFWHADHSDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*....
gi 15598053 174 LDSATGERISDlLFELNRERGTTLVLVTH 202
Cdd:cd03231 156 LDKAGVARFAE-AMAGHCARGGMVVLTTH 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-203 |
8.62e-20 |
|
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: 87.30 E-value: 8.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGsaeGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAghalgdldedqrarvRAAH 88
Cdd:TIGR03719 8 NRVSKVVP---PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------------PGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMLPL--------------------------------ELEGRADArQRAREL---LERVGL 133
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneisakyaepdadfdklaaeqaELQEIIDA-ADAWDLdsqLEIAMD 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598053 134 GQRL--GHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSatgERISDLLFELNRERGtTLVLVTHD 203
Cdd:TIGR03719 149 ALRCppWDADvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-220 |
1.02e-19 |
|
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: 83.29 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgdldedqrarvraahVGFVFQSFQLL-DSL 102
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQEPWIQnGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 daLENVMLPLELEgradaRQRARELLERVGLGQRLGHYPRQ-----------LSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:cd03250 83 --RENILFGKPFD-----EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 172 GNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGR 220
Cdd:cd03250 156 SAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-227 |
1.13e-19 |
|
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: 86.78 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 28 LSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAlgdLDEDQRARVRaAHVGFVFQSFQLLDSLdalen 107
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREAYR-QLFSAVFSDFHLFDRL----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 108 vmlpLELEGRADArQRARELLERVGLGQRLGHY-----PRQLSGGEQQRVAIARAFAAEPDVLFADE------Ptgnlds 176
Cdd:COG4615 422 ----LGLDGEADP-ARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdP------ 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 177 aTGERI--SDLLFELnRERGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:COG4615 491 -EFRRVfyTELLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGP 541
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-203 |
1.20e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.32 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGgEVRLAGHA--LGDLDEDQRA---RVRAaHVGFVFQSFQL 98
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGRVefFNQNIYERRVnlnRLRR-QVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 LdSLDALENVML---------PLELEGRADARQRARELLERVGlgQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:PRK14258 100 F-PMSVYDNVAYgvkivgwrpKLEIDDIVESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....
gi 15598053 170 PTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-227 |
1.28e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDedqrARVRAAHVGFVFQSFQLL 99
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS----ARAASRRVASVPQDTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPL-----ELEGRADARQRA-RELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:PRK09536 90 FEFDVRQVVEMGRtphrsRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 174 LDSATGERISDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGRLIDRVEP 227
Cdd:PRK09536 170 LDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPP 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-202 |
2.40e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 26 HDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvraahvgfvfqsfQLL------ 99
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ--------------DLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 ---DSLDALENVMLPLELEGRADaRQRARELLERVGLGQRLgHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:PRK13538 84 gikTELTALENLRFYQRLHGPGD-DEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|....*..
gi 15598053 176 SATGERISDlLFELNRERGTTLVLVTH 202
Cdd:PRK13538 162 KQGVARLEA-LLAQHAEQGGMVILTTH 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-204 |
3.20e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 15 VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAG--LDQPSGGEVrlaghalgDLDEDQRARVRAahvgfv 92
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCV--------DVPDNQFGREAS------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 93 fqsfqLLDSLDALENVMLplelegradarqrARELLERVGLG--QRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:COG2401 102 -----LIDAIGRKGDFKD-------------AVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|....
gi 15598053 171 TGNLDSATGERISDLLFELNRERGTTLVLVTHDE 204
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-227 |
4.56e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 8 AQNLSKVVGSAEGKLtILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDldedqRARVRAA 87
Cdd:PRK13536 41 AIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-----RARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 88 HVGFVFQsfqlLDSLDALENVMLPLELEGRAdARQRARE-------LLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAA 160
Cdd:PRK13536 115 RIGVVPQ----FDNLDLEFTVRENLLVFGRY-FGMSTREieavipsLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598053 161 EPDVLFADEPTGNLDSATG----ERISDLLfelnrERGTTLVLVTHDERLAHR-CRRLIRLESGRLIDRVEP 227
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARhliwERLRSLL-----ARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRP 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
15-222 |
5.70e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 15 VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRARVRAAHVGFVFQ 94
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK---DITDWQTAKIMREAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDSLDALENvmlpLELEGRADARQRARELLERV-GLGQRLGHYPRQ----LSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:PRK11614 88 GRRVFSRMTVEEN----LAMGGFFAERDQFQERIKWVyELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598053 170 PTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-217 |
7.94e-19 |
|
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: 79.89 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAlgdldedqrarvraahvgfvfqsfqllDSL 102
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------------------DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 dalenvMLPlelegradarQRA-------RELLErvglgqrlghYP--RQLSGGEQQRVAIARAFAAEPDVLFADEPTGN 173
Cdd:cd03223 68 ------FLP----------QRPylplgtlREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 174 LDSATGERISDLLfelnRERGTTLVLVTHDERLAHRCRRLIRLE 217
Cdd:cd03223 122 LDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-206 |
1.07e-18 |
|
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: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 17 SAEGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLD--QPSGGEVRLAGHALGDLDEDQRARvraAHVGFVFQ 94
Cdd:COG0396 9 SVEGK-EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERAR---AGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 S---------FQLLDSldALENVMLplELEGRADARQRARELLERVGLGQRLGHypRQL----SGGEQQRVAIARAFAAE 161
Cdd:COG0396 85 YpveipgvsvSNFLRT--ALNARRG--EELSAREFLKLLKEKMKELGLDEDFLD--RYVnegfSGGEKKRNEILQMLLLE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 162 PDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERL 206
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYQRI 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-209 |
1.69e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgDLDeDQRARVRAahvGFVF-----QSFQLL 99
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIR-SPRDAIRA---GIAYvpedrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLPLeLEG--------RADARQRARELLERV-----GLGQRLGhyprQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:COG1129 343 LDLSIRENITLAS-LDRlsrgglldRRRERALAEEYIKRLriktpSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRErGTTLVLVT--HDE--RLAHR 209
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISseLPEllGLSDR 463
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-207 |
1.95e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.88 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLD--QPSGGEVRLAGHALGDLDEDQRAR 83
Cdd:cd03217 1 LEIKDLHVSVGGKE----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 vraAHVGFVFQSfqlldsldalenvmlPLELEGradarQRARELLERVGLGqrlghyprqLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03217 77 ---LGIFLAFQY---------------PPEIPG-----VKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLA 207
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLL 167
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-203 |
1.98e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.39 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKvvgSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdldedQRARV 84
Cdd:PRK13652 3 LIETRDLCY---SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI------TKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 RAAH--VGFVFQS-----FQLLDSLD-ALENVMLPLELEGRAdarQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIAR 156
Cdd:PRK13652 74 REVRkfVGLVFQNpddqiFSPTVEQDiAFGPINLGLDEETVA---HRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598053 157 AFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHD 203
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQ 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-222 |
3.63e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 28 LSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdQPSGGEVRLAGHALGDLDEDQRARVRA-----AHVGFVFQSFQLLD-S 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAylsqqQTPPFAMPVFQYLTlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVmlplelegrADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAF-----AAEPD--VLFADEPTGNL 174
Cdd:PRK03695 94 QPDKTRT---------EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598053 175 DSATgERISDLLFELNRERGTTLVLVTHD-ERLAHRCRRLIRLESGRLI 222
Cdd:PRK03695 165 DVAQ-QAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-203 |
5.53e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.09 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGsaeGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAghalgdldedqrarvRAAH 88
Cdd:PRK11819 10 NRVSKVVP---PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA---------------PGIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLDSLDALENVMlplelEGRADARQ-RAR----------------ELLERVG-------------LGQRL- 137
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVE-----EGVAEVKAaLDRfneiyaayaepdadfdALAAEQGelqeiidaadawdLDSQLe 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 138 ----------GHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSatgERISDLLFELNRERGtTLVLVTHD 203
Cdd:PRK11819 147 iamdalrcppWDAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPG-TVVAVTHD 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-202 |
6.44e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdQPSG---GEVRLAGhalgdld 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEG------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 78 EDQRAR-VR---AAHVGFVFQSFQLLDSLDALENVMLPLELE--GRAD---ARQRARELLERVGLG----QRLGHYprql 144
Cdd:PRK13549 69 EELQASnIRdteRAGIAIIHQELALVKELSVLENIFLGNEITpgGIMDydaMYLRAQKLLAQLKLDinpaTPVGNL---- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 145 SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTH 202
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-209 |
6.49e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSaegkLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQ--PSG---GEVRLAGHALGDLDED 79
Cdd:PRK14243 10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 80 QrARVRAaHVGFVFQS---FqlldSLDALENVMLPLELEG-RADARQRARELLERVGLGQRLGHYPRQ----LSGGEQQR 151
Cdd:PRK14243 86 P-VEVRR-RIGMVFQKpnpF----PKSIYDNIAYGARINGyKGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 152 VAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRErgTTLVLVTHDERLAHR 209
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-223 |
7.54e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdldedQRARVRAA---HVGFVFQSFQLLDS 101
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM------RFASTTAAlaaGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVML-----PLELEGRADARQRARELLERVGL----GQRLGHyprqLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:PRK11288 94 MTVAENLYLgqlphKGGIVNRRLLNYEAREQLEHLGVdidpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 173 NLDSatgeRISDLLFELNRE---RGTTLVLVTH--DE--RLahrCRRLIRLESGRLID 223
Cdd:PRK11288 170 SLSA----REIEQLFRVIRElraEGRVILYVSHrmEEifAL---CDAITVFKDGRYVA 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-227 |
1.26e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKvvgSAEGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRAR 83
Cdd:PRK10895 2 ATLTAKNLAK---AYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 vraAHVGFVFQSFQLLDSLDALENVMLPLELEGRADARQ---RARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAA 160
Cdd:PRK10895 78 ---RGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQredRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 161 EPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDER-LAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGTP 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-203 |
1.56e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.62 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 34 RGDSLAIVGSSGSGKSTLLGLLAGL---------DQPSGGEV--RLAGHALGDLDEDQRA-RVRAAHvgfvfqSFQLLDs 101
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVlkRFRGTELQNYFKKLYNgEIKVVH------KPQYVD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 ldalenvMLPLELEG-------RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:PRK13409 171 -------LIPKVFKGkvrellkKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 15598053 175 DsaTGERI--SDLLFELNRERgtTLVLVTHD 203
Cdd:PRK13409 244 D--IRQRLnvARLIRELAEGK--YVLVVEHD 270
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-202 |
1.79e-17 |
|
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: 80.83 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 39 AIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRArVRAAhVGFVFQSFQLLDSLDALENVMLPLELEGRA 118
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK---DIETNLDA-VRQS-LGMCPQHNILFHHLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 119 --DARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLfeLNRERGTT 196
Cdd:TIGR01257 1035 weEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRT 1112
|
....*.
gi 15598053 197 LVLVTH 202
Cdd:TIGR01257 1113 IIMSTH 1118
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-203 |
2.13e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdqpsggeVRLAGHALGDLDEDQRARVRAAHVGFVFQSFQLLDSL 102
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-------VRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DAL-ENVML-----PLELEGRADARQRAR--ELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:PRK15056 94 PVLvEDVVMmgrygHMGWLRRAKKRDRQIvtAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180
....*....|....*....|....*....
gi 15598053 175 DSATGERISDLLFELnRERGTTLVLVTHD 203
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-223 |
2.62e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL-DQPSG----GEVRLAGHALGDLDEDQRARVRaahVGFVFQSFQ 97
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSIFNYRDVLEFRRR---VGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 98 LLdSLDALENVMLPL---ELEGRADARQRARELLERVGL----GQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:PRK14271 112 PF-PMSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598053 171 TGNLDSATGERISDLLFELNRErgTTLVLVTHDERLAHRCR-RLIRLESGRLID 223
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISdRAALFFDGRLVE 242
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-206 |
2.87e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 13 KVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlaghalgdldedqraRVRAAHVGFV 92
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------------RNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 93 FQSFQLldsldaleNVMLPLELEGRADARQRARE-----LLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:PRK09544 73 PQKLYL--------DTTLPLTVNRFLRLRPGTKKedilpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598053 168 DEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERL 206
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-224 |
2.91e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.06 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRARVRAaHVGFVFQSFQLLDSLDA 104
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTLASLRN-QVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 lENVMLPLELE-GRADARQRAR-----ELLERV--GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PRK11176 435 -NNIAYARTEQySREQIEEAARmayamDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598053 177 ATGERISDLLFELNRERgTTLVlvthderLAHR------CRRLIRLESGRLIDR 224
Cdd:PRK11176 514 ESERAIQAALDELQKNR-TSLV-------IAHRlstiekADEILVVEDGEIVER 559
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-227 |
1.60e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.28 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 19 EGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARvraaHVGFVFQS--F 96
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR----KIGMVFQNpdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSlDALENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:PRK13642 93 QFVGA-TVEDDVAFGMENQGipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 175 DSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-221 |
4.54e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.74 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVrLAGHALGDLDedQRARVRAAHVGFVFQSFQLLDSLD 103
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVP--QQAWIMNATVRGNILFFDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 aLENVMLPLELEgrADARQRARellervGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERIS 183
Cdd:PTZ00243 752 -LADAVRVSQLE--ADLAQLGG------GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVV 822
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598053 184 DLLFeLNRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:PTZ00243 823 EECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-198 |
4.82e-16 |
|
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: 73.45 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 3 ASILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdqpSGGEVRLAGHAL-GDLDEDQR 81
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHyNGIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 82 ARVRAAHVGFVFQSfqllDSLDALENVmlplelegradarqraRELLERVGLGQrlGH-YPRQLSGGEQQRVAIARAFAA 160
Cdd:cd03233 78 AEKYPGEIIYVSEE----DVHFPTLTV----------------RETLDFALRCK--GNeFVRGISGGERKRVSIAEALVS 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598053 161 EPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLV 198
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-203 |
5.71e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.98 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 34 RGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEV-----------RLAGHALGDLDEDQRA-RVRAAHvgfvfqSFQLLDs 101
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQDYFKKLANgEIKVAH------KPQYVD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 ldalenvMLPLELEG-------RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:COG1245 171 -------LIPKVFKGtvrelleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 15598053 175 DsaTGERI--SDLLFELNRErGTTLVLVTHD 203
Cdd:COG1245 244 D--IYQRLnvARLIRELAEE-GKYVLVVEHD 271
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-203 |
6.43e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.08 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 41 VGSSGSGKSTLLGLLAGLDQPSGGEVRL-AGHALGDLDEDQrarvraahvgFVFQSFQLLDSL--------------DAL 105
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQ----------FAFEEFTVLDTVimghtelwevkqerDRI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 106 --------ENVMLPLELEGR------ADARQRARELLERVGLGQRLgHYP--RQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:PRK15064 103 yalpemseEDGMKVADLEVKfaemdgYTAEARAGELLLGVGIPEEQ-HYGlmSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190
....*....|....*....|....*....|....
gi 15598053 170 PTGNLDSATgerISDLLFELNrERGTTLVLVTHD 203
Cdd:PRK15064 182 PTNNLDINT---IRWLEDVLN-ERNSTMIIISHD 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-223 |
7.90e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 28 LSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAlgdLDEDQRARVRaAHVGFVFQSFQLLDSLdalen 107
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYR-KLFSAVFTDFHLFDQL----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 108 vmlpLELEGRADARQRARELLERVGLGQRLGHYPR-----QLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:PRK10522 413 ----LGPEGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598053 183 SDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLID 223
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-203 |
2.40e-15 |
|
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: 72.44 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 31 DLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALG----DLDEDQRARVRAahvgFVFQSFQLLDSLDALE 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD----LLSSITKDFYTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 107 N-VMLPLELEGRADarqraRELLErvglgqrlghyprqLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDL 185
Cdd:cd03237 97 TeIAKPLQIEQILD-----REVPE--------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180
....*....|....*....|
gi 15598053 186 L--FELNRERgtTLVLVTHD 203
Cdd:cd03237 158 IrrFAENNEK--TAFVVEHD 175
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-222 |
3.34e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGlDQPSG---------GEVRLAGHALGDLDEDQRARVRA-----AH 88
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRAvlpqaAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 89 VGFVFQSFQLLdSLDALENVMLPLELEGRadARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFA--------- 159
Cdd:PRK13547 94 PAFAFSAREIV-LLGRYPHARRAGALTHR--DGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598053 160 AEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHR-CRRLIRLESGRLI 222
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIV 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-202 |
8.13e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdQPSG---GEVRLAGhalgdldEDQRAR-VRAA-HVGFVF--QSFQ 97
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDG-------EVCRFKdIRDSeALGIVIihQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 98 LLDSLDALENVMLPLELEGR-----ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:NF040905 89 LIPYLSIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190
....*....|....*....|....*....|
gi 15598053 173 NLDSATGERISDLLFELnRERGTTLVLVTH 202
Cdd:NF040905 169 ALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-217 |
1.88e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDedqrarvRAAHVGFVFQSFQLLDSLD 103
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEGRaDARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERIS 183
Cdd:PRK13543 99 TLENLHFLCGLHGR-RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVN 177
|
170 180 190
....*....|....*....|....*....|....*
gi 15598053 184 DLLFELNRERGTTLVlVTHDERLAHRCR-RLIRLE 217
Cdd:PRK13543 178 RMISAHLRGGGAALV-TTHGAYAAPPVRtRMLTLE 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-222 |
4.07e-14 |
|
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: 68.67 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLD-EDQRARvraahVGFVFQSFQL---- 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSR-----ISIIPQDPVLfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 ----LDSLDALENVMLplelegradarqraRELLERVGLGQRLGHYP-----------RQLSGGEQQRVAIARAFAAEPD 163
Cdd:cd03244 94 irsnLDPFGEYSDEEL--------------WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 164 VLFADEPTGNLDSATGERISDLLFElnRERGTTLVLVTHdeRLAH--RCRRLIRLESGRLI 222
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAH--RLDTiiDSDRILVLDKGRVV 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-210 |
8.71e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.66 E-value: 8.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGlDQPSG--------GEVRLAGHALGDLDEdqrarvraaHVGFVFQS 95
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGETIWDIKK---------HIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 96 FQLLDSLDA-LENVMlpleLEGRADA-----------RQRARELLERVGLGQRLGHYP-RQLSGGEQQRVAIARAFAAEP 162
Cdd:PRK10938 345 LHLDYRVSTsVRNVI----LSGFFDSigiyqavsdrqQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598053 163 DVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRC 210
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAC 468
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-203 |
9.79e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 9.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAlgdLDEDQRARVR-AAHVGFVFQS-FQLLDS 101
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP---LDYSKRGLLAlRQQVATVFQDpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVMLPLELEGRADAR--QRARELLERVGlGQRLGHYPRQ-LSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEitRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180
....*....|....*....|....*
gi 15598053 179 GERISDLLFELnRERGTTLVLVTHD 203
Cdd:PRK13638 172 RTQMIAIIRRI-VAQGNHVIISSHD 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-203 |
1.27e-13 |
|
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: 67.78 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 35 GDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVR-----------LAGHALGD-----LDEDQRARVRAAHVGFVFQSFQl 98
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNyftklLEGDVKVIVKPQYVDLIPKAVK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 ldsldalENVmlpLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDsaT 178
Cdd:cd03236 105 -------GKV---GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--I 172
|
170 180
....*....|....*....|....*..
gi 15598053 179 GERIS--DLLFELNRERGTTLVlVTHD 203
Cdd:cd03236 173 KQRLNaaRLIRELAEDDNYVLV-VEHD 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-202 |
2.45e-13 |
|
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: 68.31 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdQPSG---GEVRLAGHAL--GDLDEDQRARVRAAHvgfvfQ 94
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLkaSNIRDTERAGIVIIH-----Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDSLDALENVMLPLELE---GRADARQ---RARELLERVGLGQRLGHYP-RQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITlpgGRMAYNAmylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190
....*....|....*....|....*....|....*
gi 15598053 168 DEPTGNLDSATGERISDLLFELNReRGTTLVLVTH 202
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKA-HGVACVYISH 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-202 |
2.54e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQrarv 84
Cdd:PRK15439 11 LLCARSISKQYSGVE----VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 raAH---VGFVFQSFQLLDSLDALENVMlpLELEGRADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAE 161
Cdd:PRK15439 83 --AHqlgIYLVPQEPLLFPNLSVKENIL--FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598053 162 PDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTH 202
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISH 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-202 |
2.63e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAL---GDLDEDQrarvraAHVGFVFQSFQLLDS 101
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfnGPKSSQE------AGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 LDALENVMLPLELE---GRADAR---QRARELLERVGLGqrlgHYPRQLSG----GEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:PRK10762 94 LTIAENIFLGREFVnrfGRIDWKkmyAEADKLLARLNLR----FSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190
....*....|....*....|....*....|.
gi 15598053 172 GNLDSATGERISDLLFELnRERGTTLVLVTH 202
Cdd:PRK10762 170 DALTDTETESLFRVIREL-KSQGRGIVYISH 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-178 |
2.92e-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: 68.04 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 5 ILNAQNLSKVVGsaeGKLTIlHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlaghaLGDldedqrarv 84
Cdd:TIGR03719 322 VIEAENLTKAFG---DKLLI-DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-----IGE--------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 85 rAAHVGFVFQSfqlLDSLDALENVMlpLELEGRADARQRA-RELLERVGLG----------QRLGhyprQLSGGEQQRVA 153
Cdd:TIGR03719 384 -TVKLAYVDQS---RDALDPNKTVW--EEISGGLDIIKLGkREIPSRAYVGrfnfkgsdqqKKVG----QLSGGERNRVH 453
|
170 180
....*....|....*....|....*
gi 15598053 154 IARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-206 |
4.43e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 1 MSASILNAQNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGldQPS----GGEVRLAGHALGDL 76
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 DEDQRarvraAHVGfVFQSFQlldsldalenvmLPLELEG--RAD-------ARQRAREL---------------LERVG 132
Cdd:CHL00131 77 EPEER-----AHLG-IFLAFQ------------YPIEIPGvsNADflrlaynSKRKFQGLpeldplefleiinekLKLVG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 133 LGQRLGHypRQL----SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERL 206
Cdd:CHL00131 139 MDPSFLS--RNVnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRL 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-206 |
6.56e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.12 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 15 VGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLA-GHALGDLDEDQRARVRAAHvgfvf 93
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRADE----- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 94 QSFQLLDSLdalenvmLPLELEgradarQRARELLERVGL-GQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:PRK10636 393 SPLQHLARL-------APQELE------QKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190
....*....|....*....|....*....|....
gi 15598053 173 NLDSATGERISDLLFELNrergTTLVLVTHDERL 206
Cdd:PRK10636 460 HLDLDMRQALTEALIDFE----GALVVVSHDRHL 489
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-202 |
7.42e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGgevrLAGHALGDLDEDQRARVRaaHVGFVFQSFQLLDSL 102
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILK--RTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVM------LPLELEgRADARQRARELLERVGLGQ----RLGH-YPRQLSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:PLN03211 156 TVRETLVfcsllrLPKSLT-KQEKILVAESVISELGLTKcentIIGNsFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|.
gi 15598053 172 GNLDSATGERISDLLFELnRERGTTLVLVTH 202
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-202 |
8.83e-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: 64.57 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 4 SILNAQNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPS--GGEVRLAGHALGdlDEDQR 81
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD--KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 82 ArvraahVGFVFQsfqlLDSLDALENVmlplelegradarqraRELLervglgqRLGHYPRQLSGGEQQRVAIARAFAAE 161
Cdd:cd03232 80 S------TGYVEQ----QDVHSPNLTV----------------REAL-------RFSALLRGLSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598053 162 PDVLFADEPTGNLDSATGERISDLLFELNRErGTTLVLVTH 202
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIH 166
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-223 |
1.40e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 6 LNAQNLSKvvgsAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAghalgdldedqrarvR 85
Cdd:PRK15064 320 LEVENLTK----GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS---------------E 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 AAHVGFVFQsfqllDSLDALENVMLPLELEGR----ADARQRARELLERVGLGQ-RLGHYPRQLSGGEQQRVAIARAFAA 160
Cdd:PRK15064 381 NANIGYYAQ-----DHAYDFENDLTLFDWMSQwrqeGDDEQAVRGTLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598053 161 EPDVLFADEPTGNLDSatgERISDLLFELNRERGtTLVLVTHD-ERLAHRCRRLIRLESGRLID 223
Cdd:PRK15064 456 KPNVLVMDEPTNHMDM---ESIESLNMALEKYEG-TLIFVSHDrEFVSSLATRIIEITPDGVVD 515
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-222 |
2.28e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.14 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 117 RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTT 196
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197
|
90 100
....*....|....*....|....*.
gi 15598053 197 LVLVTHDERLAHRCRRLIRLESGRLI 222
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-203 |
2.77e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 34 RGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLA-------GHALGDLDEDQRARVRAAHVGFVFQSFqlldsldALE 106
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpQYISPDYDGTVEEFLRSANTDDFGSSY-------YKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 107 NVMLPLELEgradarqrarELLERvglgqrlghYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAtgERIS--D 184
Cdd:COG1245 438 EIIKPLGLE----------KLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAvaK 496
|
170
....*....|....*....
gi 15598053 185 LLFELNRERGTTLVLVTHD 203
Cdd:COG1245 497 AIRRFAENRGKTAMVVDHD 515
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-203 |
3.64e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.97 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 19 EGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlAGHALGDLDEDQRarvRAAhvgfvfqsfql 98
Cdd:PRK11147 330 DGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLEVAYFDQH---RAE----------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 ldsLDALENVMlplelEGRADARQ------RARELLervGLGQRLGHYP-------RQLSGGEQQRVAIARAFAAEPDVL 165
Cdd:PRK11147 394 ---LDPEKTVM-----DNLAEGKQevmvngRPRHVL---GYLQDFLFHPkramtpvKALSGGERNRLLLARLFLKPSNLL 462
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598053 166 FADEPTGNLDSATGErisdLLFELNRERGTTLVLVTHD 203
Cdd:PRK11147 463 ILDEPTNDLDVETLE----LLEELLDSYQGTVLLVSHD 496
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-209 |
6.61e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRArvraaHVGFVF------QSFQLLD 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRL-----ARGLVYlpedrqSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 101 SLDALENVMLPLELEGRADARQRARELLERV--GLGQRLGHYP---RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:PRK15439 356 APLAWNVCALTHNRRGFWIKPARENAVLERYrrALNIKFNHAEqaaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598053 176 SATGERISDLLFELNrERGTTLVLVTHD----ERLAHR 209
Cdd:PRK15439 436 VSARNDIYQLIRSIA-AQNVAVLFISSDleeiEQMADR 472
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-202 |
1.08e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQrARVRAAHVG---FVFQsfqll 99
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS-WRSRLAVVSqtpFLFS----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDAleNVMLpleleGRADARQRARELLERV------------GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:PRK10789 403 DTVAN--NIAL-----GRPDATQQEIEHVARLasvhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190
....*....|....*....|....*....|....*
gi 15598053 168 DEPTGNLDSATGERISDLLFELNRERgtTLVLVTH 202
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGR--TVIISAH 508
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-202 |
1.26e-11 |
|
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: 61.96 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 22 LTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAG-HALGDLDEDQRARVRAAhVGFVFQSFQLLD 100
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNkNESEPSFEATRSRNRYS-VAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 101 SlDALENVMLpleleGRADARQRARELLERVGLG-----------QRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:cd03290 93 A-TVEENITF-----GSPFNKQRYKAVTDACSLQpdidllpfgdqTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....
gi 15598053 170 PTGNLDSATGERI-SDLLFELNRERGTTLVLVTH 202
Cdd:cd03290 167 PFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTH 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-203 |
1.83e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 32 LARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVrlaghaLGDLD---------EDQRARVRAahvgFVFQSFQLLDSL 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELKisykpqyikPDYDGTVED----LLRSITDDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVMLPLELEgradarqrarELLERvglgqrlghYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAtgERI 182
Cdd:PRK13409 432 YYKSEIIKPLQLE----------RLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRL 490
|
170 180
....*....|....*....|...
gi 15598053 183 --SDLLFELNRERGTTLVLVTHD 203
Cdd:PRK13409 491 avAKAIRRIAEEREATALVVDHD 513
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-202 |
3.91e-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: 62.27 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 18 AEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLL-GLLAGLDQPSGgEVRLAGHalgdldedqrarvraahVGFVFQSF 96
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLsALLAEMDKVEG-HVHMKGS-----------------VAYVPQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLL-DSLDalENVMLpleleGRADARQRARELLERVGL---------GQR--LGHYPRQLSGGEQQRVAIARAFAAEPDV 164
Cdd:TIGR00957 709 WIQnDSLR--ENILF-----GKALNEKYYQQVLEACALlpdleilpsGDRteIGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598053 165 LFADEPTGNLDSATGERISD-LLFELNRERGTTLVLVTH 202
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTH 820
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-227 |
5.06e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 59.73 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLD-EDQRARvraahVGFVFQSFQLLDSl 102
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSS-----LTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 daleNVMLPLELEGRADARQrARELLERVGLGQrlghyprQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:cd03369 97 ----TIRSNLDPFDEYSDEE-IYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 183 SDLLFELNreRGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:cd03369 165 QKTIREEF--TNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-184 |
7.37e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldedqrarvraaHVGFVFQsFQLLDSLD 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQ-FSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEgradaRQRARELLERVGLGQRLGHYPRQ-----------LSGGEQQRVAIARAFAAEPDVLFADEPTG 172
Cdd:cd03291 114 IKENIIFGVSYD-----EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170
....*....|..
gi 15598053 173 NLDSATGERISD 184
Cdd:cd03291 189 YLDVFTEKEIFE 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-221 |
8.60e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHV-------GFvFQSFQLL 99
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYItesrrdnGF-FPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENV----------MLPLELEGRADARQRARELLERVGLGQRLGhyprQLSGGEQQRVAIARAFAAEPDVLFADE 169
Cdd:PRK09700 360 QNMAISRSLkdggykgamgLFHEVDEQRTAENQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598053 170 PTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-202 |
1.29e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL-DQPSGGEVRLAGHALGDL--------DEDQRARVR--------- 85
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMtneqdyqgDEEQNVGMKnvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 86 ---AAHVGFVFQSFQ--LLDSLDA--------------------------LENVMLPLELEGRADARQRAR-----ELLE 129
Cdd:PTZ00265 1263 eggSGEDSTVFKNSGkiLLDGVDIcdynlkdlrnlfsivsqepmlfnmsiYENIKFGKEDATREDVKRACKfaaidEFIE 1342
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598053 130 RV--GLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVLVTH 202
Cdd:PTZ00265 1343 SLpnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-200 |
1.61e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAG-LDQPSGgevrlaghalgdldEDQRARVRAAHVgfvfqSFQLLDSLD 103
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSG--------------ERQSQFSHITRL-----SFEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALE-----NVMLPLELE--GRADA---------RQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFA 167
Cdd:PRK10938 80 SDEwqrnnTDMLSPGEDdtGRTTAeiiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190
....*....|....*....|....*....|...
gi 15598053 168 DEPTGNLDSATGERISDLLFELNRErGTTLVLV 200
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-206 |
2.57e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 17 SAEGKlTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLD--QPSGGEVRLAGHALGDLDEDQRARVRaahvgfVFQ 94
Cdd:PRK09580 10 SVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEG------IFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 95 SFQLLDSLDALENVMLpLELEGRADARQRARELLERVGLGQ------RLGHYPRQL---------SGGEQQRVAIARAFA 159
Cdd:PRK09580 83 AFQYPVEIPGVSNQFF-LQTALNAVRSYRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598053 160 AEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERL 206
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRI 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
38-206 |
2.79e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 38 LAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlaghalgdldedQRARVRAAhvgfVFqSFQLLDSLDALENVMLPLELEGR 117
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF------------RSAKVRMA----VF-SQHHVDGLDLSSNPLLYMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 118 ADARQRARELLERVGLGQRLGHYPR-QLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD-SATGERISDL-LFElnrerg 194
Cdd:PLN03073 601 GVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQGLvLFQ------ 674
|
170
....*....|..
gi 15598053 195 TTLVLVTHDERL 206
Cdd:PLN03073 675 GGVLMVSHDEHL 686
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-204 |
2.87e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHalgDLDEDQRARVRaaHVGFVFQSFQLLDSLD 103
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---SIKKDLCTYQK--QLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEGRAdarQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERIS 183
Cdd:PRK13540 91 LRENCLYDIHFSPGA---VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170 180
....*....|....*....|.
gi 15598053 184 DLLfELNRERGTTLVLVTHDE 204
Cdd:PRK13540 168 TKI-QEHRAKGGAVLLTSHQD 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-182 |
3.01e-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: 59.54 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalgdldedqrarvraaHVGFVFQSFQLLDSlD 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLEL-EGRADARQRARELLERVGLGQR-----LGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:TIGR01271 503 IKDNIIFGLSYdEYRYTSVIKACQLEEDIALFPEkdktvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*
gi 15598053 178 TGERI 182
Cdd:TIGR01271 583 TEKEI 587
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-221 |
4.66e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGgevrlaghalGDLDEDQRARVRAAHVGFVFQsfqlldsLDA 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV----------GKVDRNGEVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLPLELEG--RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:PRK13546 103 IENIEFKMLCMGfkRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598053 183 SDLLFELnRERGTTLVLVTHDERLAHR-CRRLIRLESGRL 221
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKL 221
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-217 |
4.79e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 57.23 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 39 AIVGSSGSGKSTLL-GLLAGLDqpsgGEVRLAGHALGDLDEDQRARVRAAHVGFVFQSFQ-----LLDSLDALENV-MLP 111
Cdd:cd03240 26 LIVGQNGAGKTTIIeALKYALT----GELPPNSKGGAHDPKLIREGEVRAQVKLAFENANgkkytITRSLAILENViFCH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 112 LElegradarQRARELLERVGlgqrlghyprQLSGGEQQ------RVAIARAFAAEPDVLFADEPTGNLDSATGE-RISD 184
Cdd:cd03240 102 QG--------ESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAE 163
|
170 180 190
....*....|....*....|....*....|...
gi 15598053 185 LLFELNRERGTTLVLVTHDERLAHRCRRLIRLE 217
Cdd:cd03240 164 IIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-203 |
1.01e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdldeDQRARVRAAHVGFVFQSFQ-----LL 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV-----VTRSPQDGLANGIVYISEDrkrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 100 DSLDALENVMLP-LELEGRADARQRARELLERVG------------LGQRLGhyprQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:PRK10762 343 LGMSVKENMSLTaLRYFSRAGGSLKHADEQQAVSdfirlfniktpsMEQAIG----LLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRErGTTLVLVTHD 203
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSE 454
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-219 |
1.03e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSggevrlaghalgdldEDQRARVRAAhVGFVFQSFQLLDSlDA 104
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA---------------ETSSVVIRGS-VAYVPQVSWIFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLPLELE----GRA---DARQRARELL---ERVGLGQRlghyPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNL 174
Cdd:PLN03232 696 RENILFGSDFEseryWRAidvTALQHDLDLLpgrDLTEIGER----GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598053 175 DSATGERISDLLFElNRERGTTLVLVTHDERLAHRCRRLIRLESG 219
Cdd:PLN03232 772 DAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-171 |
1.20e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 20 GKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGhalGDLdEDQRARVRAAH-VGFVFQSF-- 96
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDM-ADARHRRAVCPrIAYMPQGLgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSLDALENvmlpLELEGR------ADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEP 170
Cdd:NF033858 88 NLYPTLSVFEN----LDFFGRlfgqdaAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
.
gi 15598053 171 T 171
Cdd:NF033858 164 T 164
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-175 |
1.28e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 8 AQNLSKVVGsaeGKLTIlHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRlaghaLGDldedqrarvrAA 87
Cdd:PRK11819 327 AENLSKSFG---DRLLI-DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-----IGE----------TV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 88 HVGFVFQSfqlLDSLDALENV---------MLPL---ELEGRA----------DARQrarelleRVGlgqrlghyprQLS 145
Cdd:PRK11819 388 KLAYVDQS---RDALDPNKTVweeisggldIIKVgnrEIPSRAyvgrfnfkggDQQK-------KVG----------VLS 447
|
170 180 190
....*....|....*....|....*....|
gi 15598053 146 GGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-223 |
1.88e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 30 LDLARGDSLAIVGSSGSGKSTLLGLLAGlDQP-SGGEVRLAGH-ALGDLDEDQRARVRA----------AHVGFVFQSF- 96
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYEQDlIVARLQQDPPRNVEGtvydfvaegiEEQAEYLKRYh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLD---------SLDALENVMLPLELEGRADARQRARELLERVGLGqrlGHYP-RQLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:PRK11147 103 DISHlvetdpsekNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLD---PDAAlSSLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598053 167 ADEPTGNLDSATGERISDLLFELnreRGtTLVLVTHDerlahrcRRLIRLESGRLID 223
Cdd:PRK11147 180 LDEPTNHLDIETIEWLEGFLKTF---QG-SIIFISHD-------RSFIRNMATRIVD 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-201 |
4.12e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAG-LDQPSGGEVRLAGhalgdldedqrarvRAAHVGFVFQSFqlldSLD 103
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG--------------TVAYVPQVSWIF----NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEG-------RADARQRARELLERVGLGQrLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PLN03130 695 VRDNILFGSPFDPeryeraiDVTALQHDLDLLPGGDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180
....*....|....*....|....*..
gi 15598053 177 ATGERISD--LLFELnreRGTTLVLVT 201
Cdd:PLN03130 774 HVGRQVFDkcIKDEL---RGKTRVLVT 797
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-178 |
4.58e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 21 KLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAG-LDQ---PSGGEVRLAGHALGDLDEDQRARV-----RAAHVGf 91
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDGITPEEIKKHYRGDVvynaeTDVHFP- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 92 VFQSFQLLDSLDALENVMLPLELEGRADARQRARELLERVgLGqrLGH---------YPRQLSGGEQQRVAIARAFAAEP 162
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAT-YG--LSHtrntkvgndFVRGVSGGERKRVSIAEASLGGA 228
|
170
....*....|....*.
gi 15598053 163 DVLFADEPTGNLDSAT 178
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-208 |
1.59e-08 |
|
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: 54.37 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGevRLAGHALG-----------------------DLDEDQRAR 83
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG--RLTKPAKGklfyvpqrpymtlgtlrdqiiypDSSEDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 84 vraahvGFVFQSF-QLLDSLDaLENVmlpLELEGRADARQRARELLervglgqrlghyprqlSGGEQQRVAIARAFAAEP 162
Cdd:TIGR00954 548 ------GLSDKDLeQILDNVQ-LTHI---LEREGGWSAVQDWMDVL----------------SGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598053 163 DVLFADEPTgnldSATGERISDLLFELNRERGTTLVLVTHDERLAH 208
Cdd:TIGR00954 602 QFAILDECT----SAVSVDVEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-202 |
1.96e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLA-GHALGDLDedqrARVRAAHVGFVFQSFQL---- 98
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDIN----LKWWRSKIGVVSQDPLLfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 99 --------LDSLDALENVMLPLELEGRA-----DARQRAR-----------------ELL------------ERVGLGQR 136
Cdd:PTZ00265 476 iknnikysLYSLKDLEALSNYYNEDGNDsqenkNKRNSCRakcagdlndmsnttdsnELIemrknyqtikdsEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 137 L-----------------GHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRERGTTLVL 199
Cdd:PTZ00265 556 VlihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
...
gi 15598053 200 VTH 202
Cdd:PTZ00265 636 IAH 638
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-202 |
2.85e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHAlgdldedqrarvraahvGFVFQSFQLLDSLDA 104
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------------ALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVmlplELEG------RADARQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSAT 178
Cdd:PRK13545 103 IENI----ELKGlmmgltKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180
....*....|....*....|....
gi 15598053 179 GERISDLLFELnRERGTTLVLVTH 202
Cdd:PRK13545 179 TKKCLDKMNEF-KEQGKTIFFISH 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-223 |
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 15598053 34 RGDSLAIVGSSGSGKSTLLGLLAG-LDQPSGGEVRLAGhalgdldedqrarvraahvgfvfqsfqlldsldalenvmlpl 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 113 elegradarQRARELLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI-----SDLLF 187
Cdd:smart00382 39 ---------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLL 109
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598053 188 ELNRERGTTLVLVTHDERLAHrcRRLIRLESGRLID 223
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIV 143
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-216 |
5.33e-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: 50.82 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 29 SLDLARGDSLAIVGSSGSGKSTLL---GLLAGLDQPsggevrlagHALGDLDEDQRARVRAAHVGFVFQSFQLldsldal 105
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILdaiGLALGGAQS---------ATRRRSGVKAGCIVAAVSAELIFTRLQL------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 106 envmlplelegradarqrarellervglgqrlghyprqlSGGEQQRVAIARAFA---AEPDVLFA-DEPTGNLDSATGER 181
Cdd:cd03227 79 ---------------------------------------SGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....*
gi 15598053 182 ISDLLFELnRERGTTLVLVTHDERLAHRCRRLIRL 216
Cdd:cd03227 120 LAEAILEH-LVKGAQVIVITHLPELAELADKLIHI 153
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-214 |
5.38e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLglLAGLDQPsgGEVRLAGhalgdldedqrARVRAAHVGFVFqsfqlLDSLDA 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYAS--GKARLIS-----------FLPKFSRNKLIF-----IDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 105 LENVMLplelegradarqrarellERVGLGQRLGhyprQLSGGEQQRVAIARAFAAEP-DVLFA-DEPTGNLDSATGERI 182
Cdd:cd03238 71 LIDVGL------------------GYLTLGQKLS----TLSGGELQRVKLASELFSEPpGTLFIlDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|..
gi 15598053 183 SDLLFELnRERGTTLVLVTHDERLAHRCRRLI 214
Cdd:cd03238 129 LEVIKGL-IDLGNTVILIEHNLDVLSSADWII 159
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-227 |
5.92e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEDQRARVraahVGFVFQSFQLLDSld 103
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLFSG-- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 104 ALENVMLPLELEGRAD---ARQRA--RELLER--VGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDS 176
Cdd:PLN03232 1325 TVRFNIDPFSEHNDADlweALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598053 177 atgeRISDLLFELNRE--RGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVEP 227
Cdd:PLN03232 1405 ----RTDSLIQRTIREefKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSP 1453
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-203 |
1.96e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 26 HDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgDLDEDQRArVRAAHV---------GFV---- 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDA-IRAGIMlcpedrkaeGIIpvhs 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 93 ------------FQSFQLLdsldalenvmlpleLEGRADARQrARELLERVGLGQRLGHYP-RQLSGGEQQRVAIARAFA 159
Cdd:PRK11288 348 vadninisarrhHLRAGCL--------------INNRWEAEN-ADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLS 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 160 AEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHD 203
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSD 455
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-214 |
3.96e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 144 LSGGEQQRVAIARAFAAEpdvLFA-----DEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHRCRRLI 214
Cdd:PRK00635 477 LSGGEQERTALAKHLGAE---LIGityilDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISLADRII 548
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
114-204 |
4.30e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 114 LEGRADARQRARELLErVGLGQ-RLGHYPRQLSGGEQQRVAIARAFAAE-PDVLFA-DEPTGNLDSATGERISDLLFELn 190
Cdd:cd03270 108 LFARVGIRERLGFLVD-VGLGYlTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRL- 185
|
90
....*....|....
gi 15598053 191 RERGTTLVLVTHDE 204
Cdd:cd03270 186 RDLGNTVLVVEHDE 199
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
23-205 |
4.56e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 23 TILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLDEdqrarvraAHVGFVFQSFQLLDSL 102
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK--------PYCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DALENVMLPLELEGRADARQRArelLERVGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERI 182
Cdd:PRK13541 86 TVFENLKFWSEIYNSAETLYAA---IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|...
gi 15598053 183 SDLLFeLNRERGTTLVLVTHDER 205
Cdd:PRK13541 163 NNLIV-MKANSGGIVLLSSHLES 184
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-203 |
7.18e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 35 GDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGH-ALGDLDEDQRARVRAAhVGFVF-------QSFQLLDSLDALE 106
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPA-LEYVIdgdreyrQLEAQLHDANERN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 107 NVMLPLELEGRADA------RQRARELLERVGLGQ-RLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDsatg 179
Cdd:PRK10636 106 DGHAIATIHGKLDAidawtiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---- 181
|
170 180
....*....|....*....|....*..
gi 15598053 180 eriSDLLFELNR---ERGTTLVLVTHD 203
Cdd:PRK10636 182 ---LDAVIWLEKwlkSYQGTLILISHD 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-226 |
7.62e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 25 LHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLD-------------EDQRARVRAAHVGF 91
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalvtEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 92 VFQSF-----QLLDSLDALENVMLPLELEGRADArQRARELLERVGLGQrlghyprqLSGGEQQRVAIARAFAAEPDVLF 166
Cdd:PRK10982 344 GFNSLisnirNYKNKVGLLDNSRMKSDTQWVIDS-MRVKTPGHRTQIGS--------LSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 167 ADEPTGNLDSATGERISDLLFELNRERGTTLVLVTHDERLAHRCRRLIRLESGRLIDRVE 226
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVD 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-219 |
1.28e-06 |
|
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: 48.86 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 35 GDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALgdldedqrarvrAAHVGFVFQSFQLLDSLDALENVMLPLE- 113
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------------LTNISDVHQNMGYCPQFDAIDDLLTGREh 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 114 LEGRADARQRARELLERV------GLGqrLGHYPRQL----SGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERIS 183
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEKVanwsiqSLG--LSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598053 184 DLLFELNRErGTTLVLVTHD-ERLAHRCRRLIRLESG 219
Cdd:TIGR01257 2111 NTIVSIIRE-GRAVVLTSHSmEECEALCTRLAIMVKG 2146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-178 |
1.46e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.37 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 19 EGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLdQPSGGEVRLAGHALGD--LDEDQRARVRAAHVGFVFQ-S 95
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSvtLQTWRKAFGVIPQKVFIFSgT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 96 FQLldSLDALENVmlplelegradARQRARELLERVGLGQRLGHYPRQ-----------LSGGEQQRVAIARAFAAEPDV 164
Cdd:TIGR01271 1308 FRK--NLDPYEQW-----------SDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|....
gi 15598053 165 LFADEPTGNLDSAT 178
Cdd:TIGR01271 1375 LLLDEPSAHLDPVT 1388
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-189 |
2.65e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAEGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQP---SGGEVRLAGHALgdlDED-QR--- 81
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL---DSSfQRsig 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 82 -----------ARVRAA--HVGFVFQSFQLLDS--LDALENVMLPLELEGRADArqrareLLERVGLGqrlghyprqLSG 146
Cdd:TIGR00956 840 yvqqqdlhlptSTVRESlrFSAYLRQPKSVSKSekMEYVEEVIKLLEMESYADA------VVGVPGEG---------LNV 904
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598053 147 GEQQRVAIARAFAAEPDVL-FADEPTGNLDSATGERISDLLFEL 189
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-219 |
3.04e-06 |
|
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: 47.63 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 24 ILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALGDLD-EDQRARVRAAHVGFVFQSFQLLDSL 102
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 103 DAL-----ENVMLPLELEGRADARQRAREllervGLGQRLGHYPRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:TIGR00957 1381 DPFsqysdEEVWWALELAHLKTFVSALPD-----KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598053 178 TgeriSDLLFELNRERGTTLVLVThderLAHRCR------RLIRLESG 219
Cdd:TIGR00957 1456 T----DNLIQSTIRTQFEDCTVLT----IAHRLNtimdytRVIVLDKG 1495
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
151-217 |
5.71e-06 |
|
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: 46.58 E-value: 5.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598053 151 RVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFEL----NRERGTTLVLVTHDERLAHRCRRLIRLE 217
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrSQQRNFQLLVITHDEDFVELLGRSEYVE 1283
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
93-204 |
8.06e-06 |
|
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: 46.16 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 93 FQSFQLLDSLDALENvmLPLELEGRADARQRARELLER------VGLGQ-RLGHYPRQLSGGEQQRVAIARAFAAE-PDV 164
Cdd:TIGR00630 433 VSELSIREAHEFFNQ--LTLTPEEKKIAEEVLKEIRERlgflidVGLDYlSLSRAAGTLSGGEAQRIRLATQIGSGlTGV 510
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15598053 165 LFA-DEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDE 204
Cdd:TIGR00630 511 LYVlDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE 550
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-175 |
1.05e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 9 QNLSKVVGSAEgkltILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLA--GLDQ-PSGGEV-RLAGHALGD--------L 76
Cdd:PLN03073 181 ENFSISVGGRD----LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDGiPKNCQIlHVEQEVVGDdttalqcvL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 77 DED--------QRARVRAAHVGFVFQSFQLLDSLDA------------LENVMLPLELEGRADARQRARELLERVGLGQR 136
Cdd:PLN03073 257 NTDiertqlleEEAQLVAQQRELEFETETGKGKGANkdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLSFTPE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598053 137 LGHY-PRQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLD 175
Cdd:PLN03073 337 MQVKaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-203 |
2.13e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 39 AIVGSSGSGKSTLL-GLLAGLDQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFV---------FQSFQLLDS------- 101
Cdd:COG0419 27 LIVGPNGAGKSTILeAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRyrierrqgeFAEFLEAKPserkeal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 102 -----LDALENVM-----LPLELEGRADARQRARELLERvgLGQRLGHY--PRQLSGGEQQRVAIARAFAaepdvLFADe 169
Cdd:COG0419 107 krllgLEIYEELKerlkeLEEALESALEELAELQKLKQE--ILAQLSGLdpIETLSGGERLRLALADLLS-----LILD- 178
|
170 180 190
....*....|....*....|....*....|....
gi 15598053 170 pTGNLDSATGERISDLLFElnrergttLVLVTHD 203
Cdd:COG0419 179 -FGSLDEERLERLLDALEE--------LAIITHV 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-203 |
2.25e-05 |
|
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: 43.33 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 31 DLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEvrlaghalgdldedqrarvraahvgfvfqsfqllDSLDALENVML 110
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN----------------------------------DEWDGITPVYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 111 PLELEgradarqrarellervglgqrlghyprqLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELN 190
Cdd:cd03222 67 PQYID----------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170
....*....|...
gi 15598053 191 RERGTTLVLVTHD 203
Cdd:cd03222 119 EEGKKTALVVEHD 131
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
143-200 |
5.43e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 5.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598053 143 QLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSATGERISDLLFELNRErGTTLVLV 200
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-201 |
5.81e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.27 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 27 DLSLDLARGDSLAIVGSSGSGKSTLLGLLAGL-DQPSGGEVRLAGHALGDLDEDQRARVRAAHVGFVFQSFQLLDSLDAL 105
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 106 ENVMLP----LELEGRADA---RQRARELLERVGLGQRLGHYP-RQLSGGEQQRVAIARAFAAEPDVLFADEPTGNLDSA 177
Cdd:TIGR02633 358 KNITLSvlksFCFKMRIDAaaeLQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180
....*....|....*....|....
gi 15598053 178 TGERISDLLFELNRErGTTLVLVT 201
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVS 460
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-221 |
1.22e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.15 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 19 EGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQpSGGEVRLAGHALGD--LDEDQRARVRAAHVGFVFqSF 96
Cdd:cd03289 14 EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvpLQKWRKAFGVIPQKVFIF-SG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 97 QLLDSLDALENVmlplelegradARQRARELLERVGLGQRLGHYPRQL-----------SGGEQQRVAIARAFAAEPDVL 165
Cdd:cd03289 92 TFRKNLDPYGKW-----------SDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 166 FADEPTGNLDSATGERISDLLFElnRERGTTLVLVTHDERLAHRCRRLIRLESGRL 221
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
144-171 |
2.89e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 2.89e-04
10 20
....*....|....*....|....*...
gi 15598053 144 LSGGEQQRVAIARAFAAEPDVLFADEPT 171
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
142-217 |
5.47e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 142 RQLSGGEQQRVAIARAFA----------AEPDVLFADEPTGNLDSATGERISDLLFELnRERGTTLVLVTHDERLAHRCR 211
Cdd:TIGR00618 949 ATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAI-REGSKMIGIISHVPEFRERIP 1027
|
....*.
gi 15598053 212 RLIRLE 217
Cdd:TIGR00618 1028 HRILVK 1033
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
126-203 |
6.49e-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: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 126 ELLERVGLGQ-RLGHYPRQLSGGEQQRVAIAR--AFAAEPDVLFA-DEPTgnldsaTG---ERISDLLFELNR--ERGTT 196
Cdd:cd03271 151 QTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKelSKRSTGKTLYIlDEPT------TGlhfHDVKKLLEVLQRlvDKGNT 224
|
....*..
gi 15598053 197 LVLVTHD 203
Cdd:cd03271 225 VVVIEHN 231
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
126-202 |
8.08e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 126 ELLERVGLGQ-RLGhyprQ----LSGGEQQRVAIARAFA--AEPDVLFA-DEPTgnldsaTG---ERISDLLFELNR--E 192
Cdd:COG0178 808 QTLQDVGLGYiKLG----QpattLSGGEAQRVKLASELSkrSTGKTLYIlDEPT------TGlhfHDIRKLLEVLHRlvD 877
|
90
....*....|
gi 15598053 193 RGTTLVLVTH 202
Cdd:COG0178 878 KGNTVVVIEH 887
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
123-202 |
9.36e-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: 40.00 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 123 RARELLERVGLGQ-RLGHYPRQLSGGEQQRVAIARAFAAE---PDVLFADEPTgnldsaTG---ERISDLLFELNR--ER 193
Cdd:TIGR00630 808 RKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT------TGlhfDDIKKLLEVLQRlvDK 881
|
....*....
gi 15598053 194 GTTLVLVTH 202
Cdd:TIGR00630 882 GNTVVVIEH 890
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-74 |
1.19e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598053 19 EGKLTILHDLSLDLARGDSLAIVGSSGSGKSTLLGLLAGLDQPSGGEVRLAGHALG 74
Cdd:PTZ00243 1320 EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG 1375
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
126-202 |
6.96e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 126 ELLERVGLGQ-RLGHYPRQLSGGEQQRVAIARAFAAEPD-----VLfaDEPTgnldsaTG---ERISDLLFELNR--ERG 194
Cdd:PRK00349 812 QTLVDVGLGYiKLGQPATTLSGGEAQRVKLAKELSKRSTgktlyIL--DEPT------TGlhfEDIRKLLEVLHRlvDKG 883
|
....*...
gi 15598053 195 TTLVLVTH 202
Cdd:PRK00349 884 NTVVVIEH 891
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-226 |
9.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 36.97 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598053 144 LSGGEqqRVAIARAF--------AAEPDVLFADEPTGNLDSatgERISDLLFELNR--ERGTTLVLVTHDERLAHRCRRL 213
Cdd:PRK03918 789 LSGGE--RIALGLAFrlalslylAGNIPLLILDEPTPFLDE---ERRRKLVDIMERylRKIPQVIIVSHDEELKDAADYV 863
|
90
....*....|...
gi 15598053 214 IRLESGRLIDRVE 226
Cdd:PRK03918 864 IRVSLEGGVSKVE 876
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-52 |
9.76e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 9.76e-03
10 20
....*....|....*....|....*..
gi 15598053 26 HDLSLDLARGDSLAIVGSSGSGKSTLL 52
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| |
