|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-227 |
1.12e-134 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 377.46 E-value: 1.12e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLS 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAG 162
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 163 KPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIASYGTRSIRIQDGKLFHEEA 227
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-222 |
1.04e-124 |
|
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: 351.79 E-value: 1.04e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-227 |
7.58e-95 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 276.55 E-value: 7.58e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGEtfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIR 85
Cdd:COG2884 2 IRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:COG2884 79 -RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT-IASYGTRSIRIQDGKLFHEEA 227
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRLVRDEA 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-230 |
1.06e-91 |
|
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: 268.92 E-value: 1.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSvSAREKAAiECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR-DARARAR-ALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPTIASYGTRSIRIQDGKLFHEEATQA 230
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-204 |
2.52e-85 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 256.54 E-value: 2.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIR 85
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE 200
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
7.75e-83 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 246.89 E-value: 7.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlGGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSE 83
Cdd:COG3638 1 PMLELRNLSKRY--PGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRnKKIGFIFQQFNLLPKLSAFENV------ELPLIYAGLS-VSAREKA-AIECLEKVGLLEKRRNLPTQLSGGQQQRVA 155
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSLLGlFPPEDRErALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKLF 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLArRYADRIIGLRDGRVV 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-229 |
3.14e-82 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 257.73 E-value: 3.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSE 83
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGK 163
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 164 PQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGKLFHEEATQ 229
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-203 |
1.08e-79 |
|
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: 238.63 E-value: 1.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITH 203
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITH 199
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
5-222 |
4.34e-79 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 236.54 E-value: 4.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-204 |
4.86e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 237.68 E-value: 4.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnk 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 lseirnkKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:COG1116 81 -------DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHD 198
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-204 |
8.44e-75 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 226.41 E-value: 8.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFkLSDNKLSEI 84
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQFNLLPKLSAFENVELPLIYA-GLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGK 163
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489825110 164 PQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHE 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-204 |
1.47e-73 |
|
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: 222.35 E-value: 1.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdnklsEIR 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV---------TGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489825110 166 ILLADEPTGALDSKTgKEVMG--ILQELNRAGNTIVMITHD 204
Cdd:cd03293 152 VLLLDEPFSALDALT-REQLQeeLLDIWRETGKTVLLVTHD 191
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-221 |
1.58e-73 |
|
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: 222.12 E-value: 1.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGgetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT-IASYGTRSIRIQDGK 221
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-230 |
1.65e-72 |
|
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: 220.52 E-value: 1.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIR 85
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENV------ELPLIYAGLS-VSAREK-AAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIA 157
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVlsgrlgRRSTWRSLFGlFPKEEKqRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 158 RALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKLFHEEATQA 230
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAE 231
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-217 |
4.57e-70 |
|
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: 213.25 E-value: 4.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRNK 87
Cdd:TIGR03608 1 LKNISKKF--GDKV--ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQIL 167
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489825110 168 LADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRI 217
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
4.63e-70 |
|
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: 222.47 E-value: 4.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTL-GGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDN 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 80 KLSEIRnKKIGFIFQ----QFNllPKLSAFENVELPL-IYAGLSVSAREKAAIECLEKVGLLEKRRN-LPTQLSGGQQQR 153
Cdd:COG1123 336 SLRELR-RRVQMVFQdpysSLN--PRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQR 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHD-PTIASYGTRSIRIQDGKL 222
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGlTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-204 |
2.06e-69 |
|
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: 211.62 E-value: 2.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlSDNKLSEIR 85
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYA-GLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-203 |
5.25e-69 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 215.05 E-value: 5.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIR 85
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITH 203
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITH 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-208 |
1.78e-68 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 213.81 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK 80
Cdd:COG3842 1 MAMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 lseiRNkkIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGL--LEKRRnlPTQLSGGQQQRVAIAR 158
Cdd:COG3842 77 ----RN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLegLADRY--PHQLSGGQQQRVALAR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489825110 159 ALAGKPQILLADEPTGALDSK----TGKEVMGILQELnraGNTIVMITHDPTIA 208
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKlreeMREELRRLQREL---GITFIYVTHDQEEA 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-222 |
2.56e-68 |
|
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: 208.80 E-value: 2.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIR 85
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTI-ASYGTRSIRIQDGKL 222
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
3.50e-66 |
|
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: 204.44 E-value: 3.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRnKKIGFIFQQFNLLPKLSAFENVELPLI-YAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARA 159
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD-PTIASYGTRSIRIQDGKL 222
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-222 |
7.65e-66 |
|
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: 203.12 E-value: 7.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnKLSEI 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR-RLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKKIGFIFQ--QFNLLPKLSAFENVELPLIYAGLSV--SAREKAAIECLEKVGLLEKRRN-LPTQLSGGQQQRVAIARA 159
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLPEEVLNrYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIASY-GTRSIRIQDGKL 222
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-230 |
1.05e-62 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 195.59 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGetfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQFNLLPKLSAFENV---------ELPLIYAGLSVSAREKAaIECLEKVGLLEKRRNLPTQLSGGQQQRVA 155
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEEDKERA-LSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKLFHEEATQA 230
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAkKYADRIVGLKAGEIVFDGAPSE 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-205 |
1.08e-62 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 198.83 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVF-KLSdnklseI 84
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLP------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKKIGFIFQQFNLLPKLSAFENVElpliyAGLSVSAREKAAI-----ECLEKVGL--LEKRRnlPTQLSGGQQQRVAIA 157
Cdd:COG1118 73 RERRVGFVFQHYALFPHMTVAENIA-----FGLRVRPPSKAEIrarveELLELVQLegLADRY--PSQLSGGQRQRVALA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 158 RALAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDP 205
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQ 194
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-222 |
1.72e-62 |
|
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: 193.89 E-value: 1.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETFkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklseIR 85
Cdd:cd03259 1 LELKGLSKTY---GSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------PE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKL 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEAlALADRIAVMNEGRI 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-225 |
4.52e-62 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 194.16 E-value: 4.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSE- 83
Cdd:PRK09493 1 MIEFKNVSKHF---GPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV---NDPKVDEr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 -IRnKKIGFIFQQFNLLPKLSAFENVEL-PLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALA 161
Cdd:PRK09493 74 lIR-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA-SYGTRSIRIQDGKLFHE 225
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAED 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-204 |
4.77e-62 |
|
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: 196.43 E-value: 4.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDVP--DEGSYHLDNVDVFKLSDNKL 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIRNKKIGFIFQQ----FNllPKLSAFENVELPL-IYAGLSVSAREKAAIECLEKVGLLEKRRNL---PTQLSGGQQQR 153
Cdd:COG0444 81 RKIRGREIQMIFQDpmtsLN--PVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHD 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-225 |
8.27e-62 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 193.07 E-value: 8.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MP-KPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDN 79
Cdd:PRK10584 1 MPaENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 80 KLSEIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARA 159
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIASYGTRSIRIQDGKLFHE 225
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-225 |
2.24e-61 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 191.95 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIASYGTRSIRIQDGKLFHE 225
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-222 |
4.32e-61 |
|
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: 191.01 E-value: 4.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:COG1122 1 IELENLSFSYP--GGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQ----QFnLLPklSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALA 161
Cdd:COG1122 75 -RKVGLVFQnpddQL-FAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIRIQDGKL 222
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLdLVAELADRVIVLDDGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-204 |
5.59e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 188.35 E-value: 5.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklSEIR 85
Cdd:COG1131 1 IEVRGLTKRY--GD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHY 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-221 |
7.18e-60 |
|
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: 187.29 E-value: 7.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSeirnKK 88
Cdd:cd03225 3 KNLSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 89 IGFIFQQFNL-LPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQIL 167
Cdd:cd03225 77 VGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 168 LADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIRIQDGK 221
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-221 |
7.56e-60 |
|
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: 186.24 E-value: 7.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNklSEIR 85
Cdd:cd03229 1 LELKNVSKRY--GQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE--LPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLiyaglsvsarekaaieclekvgllekrrnlptqlSGGQQQRVAIARALAGKPQ 165
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELN-RAGNTIVMITHDPTIASY-GTRSIRIQDGK 221
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-222 |
8.80e-58 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 182.70 E-value: 8.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIR 85
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAG-LSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD-PTIASYGTRSIRIQDGKL 222
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-204 |
6.42e-57 |
|
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: 180.51 E-value: 6.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseir 85
Cdd:cd03300 1 IELENVSKFY--GG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHD 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-222 |
7.42e-57 |
|
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: 181.69 E-value: 7.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRNKKIGFIFQQFNLLPKLS 103
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKE 183
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489825110 184 VMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKL 222
Cdd:cd03294 199 MQDELLRLQAElQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
8.00e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 180.67 E-value: 8.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlsdnk 80
Cdd:COG1121 2 MMMPAIELENLTVSY--GGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 lseiRNKKIGFIFQQFNL---LPkLSAFENVELPLiYAGLS----VSAREKAAI-ECLEKVGLLEKRRNLPTQLSGGQQQ 152
Cdd:COG1121 73 ----ARRRIGYVPQRAEVdwdFP-ITVRDVVLMGR-YGRRGlfrrPSRADREAVdEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 153 RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIRIQDGKLFH 224
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLgAVREYFDRVLLLNRGLVAH 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-206 |
8.22e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 184.12 E-value: 8.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseiR 85
Cdd:COG3839 4 LELENVSKSY--GG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NkkIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGL--LEKRRnlPTQLSGGQQQRVAIARALAGK 163
Cdd:COG3839 76 N--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLedLLDRK--PKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489825110 164 PQILLADEPTGALDSK----TGKEVMGILQELnraGNTIVMITHDPT 206
Cdd:COG3839 152 PKVFLLDEPLSNLDAKlrveMRAEIKRLHRRL---GTTTIYVTHDQV 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-222 |
9.40e-57 |
|
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: 180.77 E-value: 9.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlsei 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKKIGFIFQQ----FNllPKLSAFENVELPLiyAGLSVSAREKAAIECLEKVGLLEK-RRNLPTQLSGGQQQRVAIARA 159
Cdd:COG1124 77 FRRRVQMVFQDpyasLH--PRHTVDRILAEPL--RIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIASY-GTRSIRIQDGKL 222
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-222 |
2.84e-55 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 176.74 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDvF----KLSDNKL 81
Cdd:COG4161 3 IQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ-FdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIRnKKIGFIFQQFNLLPKLSAFEN-VELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:COG4161 78 RLLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA-SYGTRSIRIQDGKL 222
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRI 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-225 |
3.49e-55 |
|
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: 176.77 E-value: 3.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSei 84
Cdd:COG1120 1 MLEAENLSVGY--GGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 rnKKIGFIFQQFNLLPKLSAFENVEL---PLIYAGLSVSAREKAAI-ECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEDREAVeEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPTIAS-YGTRSIRIQDGKLFHE 225
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAArYADRLVLLKDGRIVAQ 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
1.96e-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: 182.03 E-value: 1.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLdVPD----EGSYHLDNVDVFKLSD 78
Cdd:COG1123 2 TPLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHggriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 nklsEIRNKKIGFIFQ----QFNLLpklSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRV 154
Cdd:COG1123 79 ----ALRGRRIGMVFQdpmtQLNPV---TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDP-TIASYGTRSIRIQDGKL 222
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-208 |
1.08e-53 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 172.51 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNvDVFKLS----DNKL 81
Cdd:PRK11124 3 IQLNGINCFY---GAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG-NHFDFSktpsDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIRnKKIGFIFQQFNLLPKLSAFEN-VELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:PRK11124 78 RELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA 208
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVA 204
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-204 |
2.99e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 173.35 E-value: 2.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLseiR 85
Cdd:COG1125 2 IEFENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVEL-PLIyAGLSVSAREKAAIECLEKVGLLEK--RRNLPTQLSGGQQQRVAIARALAG 162
Cdd:COG1125 76 -RRIGYVIQQIGLFPHMTVAENIATvPRL-LGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489825110 163 KPQILLADEPTGALD----SKTGKEVMGILQELNRagnTIVMITHD 204
Cdd:COG1125 154 DPPILLMDEPFGALDpitrEQLQDELLRLQRELGK---TIVFVTHD 196
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
25-222 |
3.80e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.00 E-value: 3.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDvfkLSDNKLSEIRnKKIGFIFQQFNLLPKlSA 104
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP---LSAMPPPEWR-RQVAYVPQEPALWGG-TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELPLIYAGLSVSarEKAAIECLEKVGL----LEKRrnlPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKT 180
Cdd:COG4619 91 RDNLPFPFQLRERKFD--RERALELLERLGLppdiLDKP---VERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 181 GKEVMGILQEL-NRAGNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:COG4619 166 TRRVEELLREYlAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-204 |
1.04e-52 |
|
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: 169.93 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNklsEIR 85
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVEL------PLIYAGLSVSAREKAAIE----CLEKVGLLEKRRNLPTQLSGGQQQRVA 155
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVaaqartGSGLLLARARREEREAREraeeLLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-204 |
2.20e-52 |
|
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: 169.40 E-value: 2.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLseir 85
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGL--LEKRRNLPTQLSGGQQQRVAIARALAGK 163
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 164 PQILLADEPTGALDSKT----GKEVMGILQELnraGNTIVMITHD 204
Cdd:cd03295 154 PPLLLMDEPFGALDPITrdqlQEEFKRLQQEL---GKTIVFVTHD 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-222 |
5.83e-52 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 167.74 E-value: 5.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtLGGEtfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:PRK10908 1 MIRFEHVSKAY-LGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:PRK10908 78 R-RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHL 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-204 |
9.03e-52 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 168.12 E-value: 9.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlse 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 irnkkiGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGK 163
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489825110 164 PQILLADEPTGALDSKTgKEVMgilQEL-----NRAGNTIVMITHD 204
Cdd:COG4525 153 PRFLLMDEPFGALDALT-REQM---QELlldvwQRTGKGVFLITHS 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-205 |
9.73e-52 |
|
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: 166.97 E-value: 9.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTL---MN-MIGCLD-VPDEGSYHLDNVDVFKLSDNK 80
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKSTLlrlLNrLNDLIPgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LsEIRnKKIGFIFQQFNLLPKlSAFENVELPLIYAGLSVSAREKAAIE-CLEKVGLLE--KRRNLPTQLSGGQQQRVAIA 157
Cdd:cd03260 77 L-ELR-RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWDevKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489825110 158 RALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAgNTIVMITHDP 205
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNM 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-220 |
1.11e-51 |
|
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: 166.84 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTL---GGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGS--YHLDN--VDVFKL 76
Cdd:COG4778 3 TLLEVENLSKTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGgwVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 77 SDNKLSEIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVS-AREKAAiECLEKVGLLEKRRNL-PTQLSGGQQQRV 154
Cdd:COG4778 83 SPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREeARARAR-ELLARLNLPERLWDLpPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIRIQDG 220
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEeVREAVADRVVDVTPF 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-204 |
1.44e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 167.67 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDV-------- 73
Cdd:COG4598 5 APPALEVRDLHKSF---GDL-EVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 74 -FKLSDNK-LSEIRNKkIGFIFQQFNLLPKLSAFENV-ELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQ 150
Cdd:COG4598 81 eLVPADRRqLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHE 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-205 |
2.75e-51 |
|
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: 165.40 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTktYTLGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlsdnklseiRNK 87
Cdd:cd03235 2 VEDLT--VSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGFIFQQFNLLPK--LSAFENVELPL---IYAGLSVSAREKAAI-ECLEKVGLLEKR-RNLpTQLSGGQQQRVAIARAL 160
Cdd:cd03235 69 RIGYVPQRRSIDRDfpISVRDVVLMGLyghKGLFRRLSKADKAKVdEALERVGLSELAdRQI-GELSGGQQQRVLLARAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP 205
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDL 192
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-230 |
2.98e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 166.08 E-value: 2.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTK-TYTLGGETFKAlddvTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseirn 86
Cdd:COG3840 1 MLRLDDlTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 87 KKIGFIFQQFNLLPKLSAFENVELPLiYAGLSVSAREKAAIEC-LEKVGL--LEKRrnLPTQLSGGQQQRVAIARALAGK 163
Cdd:COG3840 71 RPVSMLFQENNLFPHLTVAQNIGLGL-RPGLKLTAEQRAQVEQaLERVGLagLLDR--LPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 164 PQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPT-IASYGTRSIRIQDGKLFHEEATQA 230
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-204 |
3.67e-50 |
|
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: 163.66 E-value: 3.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklseIR 85
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELpliyaGLSVSARE----KAAI-----ECLEKVGL--LEKRrnLPTQLSGGQQQRV 154
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAF-----GLRVKPRSerppEAEIrakvhELLKLVQLdwLADR--YPAQLSGGQRQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHD 204
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHD 196
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-204 |
7.84e-50 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 165.29 E-value: 7.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGETF-------KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDV 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 74 FKLSDNKLSEIRnKKIGFIFQ--QFNLLPKLSAFENVELPLIYAGL-SVSAREKAAIECLEKVGLLEK--RRNlPTQLSG 148
Cdd:COG4608 83 TGLSGRELRPLR-RRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEhaDRY-PHEFSG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 149 GQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHD 204
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISHD 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-222 |
1.03e-49 |
|
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: 161.65 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseiR 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NkkIGFIFQQFNLLPKLSAFENVELPLIYAGLS---VSAREKAAIECLEKVGLLEKRrnlPTQLSGGQQQRVAIARALAG 162
Cdd:cd03301 73 D--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPkdeIDERVREVAELLQIEHLLDRK---PKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 163 KPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKL 222
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-204 |
1.31e-49 |
|
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: 162.52 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNkl 81
Cdd:COG0411 1 SDPLLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 sEIRNKKIGFIFQQFNLLPKLSAFENVELPL-----------IYAGLSVSAREKA----AIECLEKVGLLEKRRNLPTQL 146
Cdd:COG0411 75 -RIARLGIARTFQNPRLFPELTVLENVLVAAharlgrgllaaLLRLPRARREEREarerAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 147 SGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHD 212
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-204 |
1.38e-49 |
|
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: 165.21 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKl 81
Cdd:TIGR03265 1 SSPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 seiRNkkIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALA 161
Cdd:TIGR03265 76 ---RD--YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHD 194
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-223 |
1.98e-49 |
|
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: 162.62 E-value: 1.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGE-TFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQfnllPKLSAFE-NVELPLIYA----GLSVSAREKAAIECLEKVGLLE--KRRNlPTQLSGGQQQRVAIA 157
Cdd:TIGR04521 81 R-KKVGLVFQF----PEHQLFEeTVYKDIAFGpknlGLSEEEAEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 158 RALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD-PTIASYGTRSIRIQDGKLF 223
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-225 |
2.36e-49 |
|
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: 162.21 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfkLSDNKLSEIR 85
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQ----QFnllpkLS-------AF--ENvelpliyagLSVSAREKAAI--ECLEKVGLLEKRRNLPTQLSGGQ 150
Cdd:TIGR04520 77 -KKVGMVFQnpdnQF-----VGatveddvAFglEN---------LGVPREEMRKRvdEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPTIASYGTRSIRIQDGKLFHE 225
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-204 |
2.52e-49 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 168.71 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKS-TLMNMIGCLDVPD---EGSYHLDNVDVFKL 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 77 SDNKLSEIRNKKIGFIFQQfnllPkLSAFeN---------VELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNL---PT 144
Cdd:COG4172 82 SERELRRIRGNRIAMIFQE----P-MTSL-NplhtigkqiAEVLRLHRGLSGAAARARALELLERVGIPDPERRLdayPH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 145 QLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHD 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-222 |
3.88e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 158.76 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlGGETFKALDdvtFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNV--DVFKLSDNKLSE 83
Cdd:PRK11264 4 IEVKNLVKKFH-GQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRN--KKIGFIFQQFNLLPKLSAFENV-ELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:PRK11264 80 IRQlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA-SYGTRSIRIQDGKL 222
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRI 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-222 |
4.55e-48 |
|
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: 156.02 E-value: 4.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnklsEIR 85
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE----EVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELpliyaglsvsarekaaieclekvgllekrrnlptqlSGGQQQRVAIARALAGKPQ 165
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-225 |
2.88e-46 |
|
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: 151.43 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYtlgGETFkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklSEIRNKK 88
Cdd:cd03214 3 ENLSVGY---GGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 89 IGFIFQqfnllpklsafenvelpliyaglsvsarekaaieCLEKVGLLE-KRRNLpTQLSGGQQQRVAIARALAGKPQIL 167
Cdd:cd03214 75 IAYVPQ----------------------------------ALELLGLAHlADRPF-NELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 168 LADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIAS-YGTRSIRIQDGKLFHE 225
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAArYADRVILLKDGRIVAQ 179
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-204 |
3.17e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 157.03 E-value: 3.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnk 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 lSEIRNkkIGFIFQQFNLLPKLSAFENVELpliyaGLSVSAREKAAI-----ECLEKVGLLEKRRNLPTQLSGGQQQRVA 155
Cdd:PRK09452 83 -AENRH--VNTVFQSYALFPHMTVFENVAF-----GLRMQKTPAAEItprvmEALRMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-221 |
3.18e-46 |
|
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: 151.00 E-value: 3.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDvfkLSDNKLSEIR 85
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD---LRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQfnllpklsafenvelPLIYAGlsvSAREkaaieclekvgllekrrNLptqLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03228 76 -KNIAYVPQD---------------PFLFSG---TIRE-----------------NI---LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASYGTRSIRIQDGK 221
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-173 |
1.32e-45 |
|
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: 148.95 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnklsEIRNKKIGFIFQQFNLLPKLSA 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 105 FENVELPLIYAGLSVSAREKAAIECLEKVGLLEKR----RNLPTQLSGGQQQRVAIARALAGKPQILLADEPT 173
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-221 |
2.75e-45 |
|
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: 148.16 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSeirnK 87
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGFIFQqfnllpklsafenvelpliyaglsvsarekaaieclekvgllekrrnlptqLSGGQQQRVAIARALAGKPQIL 167
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 168 LADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIRIQDGK 221
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-204 |
1.02e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 149.85 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseirnkkiGFIFQQFNLLPKLS 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTgKE 183
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT-RE 165
|
170 180
....*....|....*....|...
gi 489825110 184 VMG--ILQELNRAGNTIVMITHD 204
Cdd:PRK11248 166 QMQtlLLKLWQETGKQVLLITHD 188
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-230 |
2.96e-44 |
|
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: 148.47 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnklsEI 84
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR----EA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQFNLLPKLSAFENVELpliYA---GLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALA 161
Cdd:COG4555 73 R-RQIGVLPDERGLYDRLTVRENIRY---FAelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIRIQDGKLFHEEATQA 230
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMqEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-222 |
3.87e-44 |
|
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: 155.31 E-value: 3.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDvPDEGSYHLDNVDVFKLSDNKLS 82
Cdd:COG4987 332 PSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLD-PQSGSITLGGVDLRDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EirnkKIGFIFQQ---FN--LLpklsafENVELpliyaglsvsAREKA----AIECLEKVGLLEKRRNLP---------- 143
Cdd:COG4987 409 R----RIAVVPQRphlFDttLR------ENLRL----------ARPDAtdeeLWAALERVGLGDWLAALPdgldtwlgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 144 -TQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:COG4987 469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-222 |
4.50e-44 |
|
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: 156.92 E-value: 4.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:COG2274 474 IELENVSFRY--PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKkIGFIFQQFNLLPKlSAFENVelpliyAGLSVSAREKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQQRV 154
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENI------TLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-225 |
7.57e-44 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 147.81 E-value: 7.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDV---------FKLSDNKLSEIRNKKIGFIF 93
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 94 QQFNLLPKLSAFENV-ELPLIYAGLSVSAREKAAIECLEKVGLLEKRR-NLPTQLSGGQQQRVAIARALAGKPQILLADE 171
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 172 PTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASY-GTRSIRIQDGKLFHE 225
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-222 |
1.45e-43 |
|
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: 145.71 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTF-----------TVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdnKLSEIRNKKIGFI 92
Cdd:cd03298 2 RLDKIRFsygeqpmhfdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV------TAAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 93 FQQFNLLPKLSAFENVELPLIyAGLSVSAREKAAIE-CLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADE 171
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLS-PGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 172 PTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAeTKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-221 |
2.21e-43 |
|
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: 144.93 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdNKLSE 83
Cdd:COG4133 1 MMLEAENLSCRR--GERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRNKKIGFIFQQFNLLPKLSAFENVELpliYAGLS-VSAREKAAIECLEKVGLlEKRRNLPT-QLSGGQQQRVAIARALA 161
Cdd:COG4133 72 DYRRRLAYLGHADGLKPELTVRENLRF---WAALYgLRADREAIDEALEAVGL-AGLADLPVrQLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPtIASYGTRSIRIQDGK 221
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP-LELAAARVLDLGDFK 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-204 |
5.53e-43 |
|
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: 144.92 E-value: 5.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLseirnkkigFIFQQFNLLPKLSA 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELPL--IYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKT-- 180
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrg 151
|
170 180
....*....|....*....|....*.
gi 489825110 181 --GKEVMGILQElnrAGNTIVMITHD 204
Cdd:TIGR01184 152 nlQEELMQIWEE---HRVTVLMVTHD 174
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-203 |
1.74e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 144.41 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYtlgGEtFKALDDVTFTVEQGEFLSIVGPSGSGKSTL------MNmigclD-VPD---EGSYHLDNV 71
Cdd:COG1117 8 LEPKIEVRNLNVYY---GD-KQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMN-----DlIPGarvEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 72 DVFKlSDNKLSEIRnKKIGFIFQQFNLLPKlSAFENVELPLIYAGLSvSAREKAAI--ECLEKVGLLE--KRR--NLPTQ 145
Cdd:COG1117 79 DIYD-PDVDVVELR-RRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIK-SKSELDEIveESLRKAALWDevKDRlkKSALG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPTGALDSK-TGK--EVMgilQELnrAGN-TIVMITH 203
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKieELI---LEL--KKDyTIVIVTH 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
5.97e-42 |
|
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: 149.52 E-value: 5.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGEtfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDvfkLSDNKLSE 83
Cdd:COG4988 335 PSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD---LSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRnKKIGFIFQQfNLLPKLSAFENVelpLIYAGlsvSAREKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQQ 152
Cdd:COG4988 409 WR-RQIAWVPQN-PYLFAGTIRENL---RLGRP---DASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 153 RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-204 |
3.08e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 143.69 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklseIR 85
Cdd:PRK10851 3 IEIANIKKSF---GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------AR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELpliyaGLSVSAREK----AAI-----ECLEKVGLLEKRRNLPTQLSGGQQQRVAI 156
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAF-----GLTVLPRRErpnaAAIkakvtQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHD 204
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHD 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-204 |
4.08e-41 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 146.75 E-value: 4.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYTLGG-------ETFKALDDVTFTVEQGEFLSIVGPSGSGKSTL----MNMIgcldvPDEGSYHLDN 70
Cdd:COG4172 272 APPLLEARDLKVWFPIKRglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 71 VDVFKLSDNKLSEIRnKKIGFIFQQ-FNLL-PKLSAFENVELPLI--YAGLSVSAREKAAIECLEKVGLLEKRRN-LPTQ 145
Cdd:COG4172 347 QDLDGLSRRALRPLR-RRMQVVFQDpFGSLsPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHrYPHE 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHD 485
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-228 |
4.12e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 141.31 E-value: 4.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYhldNVDVFKLSDNK 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI---TVGGMVLSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRnKKIGFIFQ----QF---------------NLLPKLSAFENVElpliyaglsvsarekaaiECLEKVGLLEKRRN 141
Cdd:PRK13635 76 VWDVR-RQVGMVFQnpdnQFvgatvqddvafglenIGVPREEMVERVD------------------QALRQVGMEDFLNR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 142 LPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHDPTIASYGTRSIRIQDG 220
Cdd:PRK13635 137 EPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKG 216
|
....*...
gi 489825110 221 KLfHEEAT 228
Cdd:PRK13635 217 EI-LEEGT 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-204 |
4.31e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.82 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDvfklsdnkLSE 83
Cdd:PRK11607 18 PLLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD--------LSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 I--RNKKIGFIFQQFNLLPKLSAFENVELpliyaGLSVSAREKAAI-----ECLEKVGLLEKRRNLPTQLSGGQQQRVAI 156
Cdd:PRK11607 86 VppYQRPINMMFQSYALFPHMTVEQNIAF-----GLKQDKLPKAEIasrvnEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGK----EVMGILQelnRAGNTIVMITHD 204
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILE---RVGVTCVMVTHD 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-222 |
6.32e-41 |
|
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: 142.25 E-value: 6.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 40 IVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNklseirNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSV 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 120 SAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGK----EVMGILQELnraG 195
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDqmqlELKTIQEQL---G 151
|
170 180 190
....*....|....*....|....*....|
gi 489825110 196 NTIVMITHDPTIASygTRSIRI---QDGKL 222
Cdd:TIGR01187 152 ITFVFVTHDQEEAM--TMSDRIaimRKGKI 179
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-203 |
1.29e-40 |
|
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: 139.35 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlgGEtFKALDDVTFTVEQGEFLSIVGPSGSGKSTL---MNMIGCLdVPD---EGSYHLDNVDVFKlSD 78
Cdd:TIGR00972 1 AIEIENLNLFY---GE-KEALKNINLDIPKNQVTALIGPSGCGKSTLlrsLNRMNDL-VPGvriEGKVLFDGQDIYD-KK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 NKLSEIRnKKIGFIFQQFNLLPKlSAFENVELPLIYAGLSVSAR-EKAAIECLEKVGLL-EKRRNL---PTQLSGGQQQR 153
Cdd:TIGR00972 75 IDVVELR-RRVGMVFQKPNPFPM-SIYDNIAYGPRLHGIKDKKElDEIVEESLKKAALWdEVKDRLhdsALGLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITH 203
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTH 201
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-228 |
2.40e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 140.22 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGET-FKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHL-----------DNVDV 73
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 74 FKLSDN----------KLSEIRnKKIGFIFQ--QFNLlpklsaFE-NVELPLIYAGLS--VSARE--KAAIECLEKVGLL 136
Cdd:PRK13651 83 VLEKLViqktrfkkikKIKEIR-RRVGVVFQfaEYQL------FEqTIEKDIIFGPVSmgVSKEEakKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 137 EK--RRNlPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTR 213
Cdd:PRK13651 156 ESylQRS-PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKR 234
|
250
....*....|....*
gi 489825110 214 SIRIQDGKLFHEEAT 228
Cdd:PRK13651 235 TIFFKDGKIIKDGDT 249
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-221 |
4.31e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 138.29 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLG-GETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlsei 84
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKKIGFIFQqfNLL----PKLSAFENveLPLIYA-------GLSVSAREKAAI-ECLEKVGL-LEKRRNLPT-QLSGGQ 150
Cdd:COG1101 78 RAKYIGRVFQ--DPMmgtaPSMTIEEN--LALAYRrgkrrglRRGLTKKRRELFrELLATLGLgLENRLDTKVgLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHDPTIA-SYGTRSIRIQDGK 221
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQAlDYGNRLIMMHEGR 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-204 |
7.67e-40 |
|
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: 136.35 E-value: 7.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnklsEIR 85
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR----EVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHY 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-224 |
1.57e-39 |
|
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: 135.93 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseiRNkkIGFIFQQFNLLPKLSA 104
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK----RD--ISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELPLIYAGLSVSAREKAAIECLEKVG---LLEKRrnlPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTG 181
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGidhLLNRK---PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 182 KEVMGILQELNRAGNTIVM-ITHDPT-IASYGTRSIRIQDGKLFH 224
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLhVTHDFEeAWALADKVAIMLNGKLIQ 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-225 |
1.75e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.14 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGE-TFK-ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnkLS 82
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKKiGFIFQQFN------LLPKLSAF--ENvelpliyagLSVSARE--KAAIECLEKVGLLEKRRNLPTQLSGGQQQ 152
Cdd:PRK13633 82 DIRNKA-GMVFQNPDnqivatIVEEDVAFgpEN---------LGIPPEEirERVDESLKKVGMYEYRRHAPHLLSGGQKQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825110 153 RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPTIASYGTRSIRIQDGKLFHE 225
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-225 |
1.88e-39 |
|
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: 135.01 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGgetfKALDDVTFTVEQGeFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnklsEIR 85
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELnrAGNTIVMI-THD-PTIASYGTRSIRIQDGKLFHE 225
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILsTHIvEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-222 |
2.98e-39 |
|
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: 134.94 E-value: 2.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsDNKLSEIR 85
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVElplIYA---GLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAG 162
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLR---FYArlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 163 KPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASY-GTRSIRIQDGKL 222
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-222 |
4.09e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 135.58 E-value: 4.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIdMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyHLdnvdvfkLSDNK-LS 82
Cdd:PRK11247 12 PLL-LNAVSKRY--GERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--EL-------LAGTApLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKkIGFIFQQFNLLPKLSAFENVELpliyaGLSVSAREkAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAG 162
Cdd:PRK11247 78 EARED-TRLMFQDARLLPWKKVIDNVGL-----GLKGQWRD-AALQALAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 163 KPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDPTIA-SYGTRSIRIQDGKL 222
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-203 |
4.84e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 140.55 E-value: 4.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdnk 80
Cdd:COG3845 1 MMPPALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 lsEIRN------KKIGFIFQQFNLLPKLSAFENVEL---PLIYAGLSVSAREKAAIECLEKVGLlekrrNL-PT----QL 146
Cdd:COG3845 70 --RIRSprdaiaLGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGL-----DVdPDakveDL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 147 SGGQQQRVAIARALAGKPQILLADEPTGALdskTGKEV---MGILQELNRAGNTIVMITH 203
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVL---TPQEAdelFEILRRLAAEGKSIIFITH 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-203 |
5.76e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.54 E-value: 5.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnkl 81
Cdd:COG1129 1 AEPLLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIRNKKIGFIFQQFNLLPKLSAFENV---ELPLIYAGLSVSAREKAAIECLEKVGLlekrrNL-PTQ----LSGGQQQR 153
Cdd:COG1129 74 RDAQAAGIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGL-----DIdPDTpvgdLSVAQQQL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 154 VAIARALAGKPQILLADEPTGALdskTGKEV---MGILQELNRAGNTIVMITH 203
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASL---TEREVerlFRIIRRLKAQGVAIIYISH 198
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-203 |
3.89e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 139.14 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:COG1132 340 IEFENVSFSY--PGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLpKLSAFENvelpLIYAGLSVSarEKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQQRV 154
Cdd:COG1132 414 -RQIGVVPQDTFLF-SGTIREN----IRYGRPDAT--DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITH 203
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAH 533
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-230 |
6.63e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 133.42 E-value: 6.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGG--ETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK-LS 82
Cdd:PRK13641 3 IKFENVDYIYSPGTpmEK-KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRnKKIGFIFQqfnlLPKLSAFENVEL------PLIYAGLSVSAREKAaIECLEKVGLLEKRRN-LPTQLSGGQQQRVA 155
Cdd:PRK13641 82 KLR-KKVSLVFQ----FPEAQLFENTVLkdvefgPKNFGFSEDEAKEKA-LKWLKKVGLSEDLISkSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGKLFHEEATQA 230
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-230 |
7.76e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 132.44 E-value: 7.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGS-YHLDNVDVFKLSDNKLS- 82
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgSHIELLGRTVQREGRLAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKK--IGFIFQQFNLLPKLSAFENVEL------PLIYAGLSVSAREKA--AIECLEKVGLLEKRRNLPTQLSGGQQQ 152
Cdd:PRK09984 80 DIRKSRanTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSWFTREQKqrALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 153 RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKLFHEEATQA 230
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAlRYCERIVALRQGHVFYDGSSQQ 239
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-204 |
1.82e-37 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 133.31 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKS-TLMNMIGCLDVPD--EGSYHLDNVDVFKLSDN 79
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 80 KLSEIRNKKIGFIFQQ--FNLLPKLSAFENV-ELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNL---PTQLSGGQQQR 153
Cdd:PRK09473 90 ELNKLRAEQISMIFQDpmTSLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNT-IVMITHD 204
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHD 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-222 |
2.60e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 131.01 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTktYTLGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDvPDEGSYHLDNVDVFKLSDNKLSE 83
Cdd:COG4559 1 MLEAENLS--VRLGGRT--LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELT-PSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IR-----NKKIGFIFqqfnllpklSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKR-RNLPTqLSGGQQQRVAIA 157
Cdd:COG4559 76 RRavlpqHSSLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAgRSYQT-LSGGEQQRVQLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 158 RALA-------GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIAS-YGTRSIRIQDGKL 222
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAqYADRILLLHQGRL 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-203 |
4.24e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 131.02 E-value: 4.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlGGETF--KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK-LS 82
Cdd:PRK13649 3 INLQNVSYTYQ-AGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRnKKIGFIFQqfnlLPKLSAFENVELPLIYAG-----LSVSAREKAAIECLEKVGLLEKRRNL-PTQLSGGQQQRVAI 156
Cdd:PRK13649 82 QIR-KKVGLVFQ----FPESQLFEETVLKDVAFGpqnfgVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-204 |
9.22e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 131.24 E-value: 9.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTL------GGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVF 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 75 KLSDNKLSEIRnKKIGFIFQqfN----LLPKLSAFENVELPL-IYAGLSVSAREKAAIECLEKVGLL-EKRRNLPTQLSG 148
Cdd:PRK11308 81 KADPEAQKLLR-QKIQIVFQ--NpygsLNPRKKVGQILEEPLlINTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 149 GQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHD 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-203 |
9.88e-37 |
|
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: 128.25 E-value: 9.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlsdNKLSEI 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNkkIGFIFQQFNLLPKLSAFENVELpliYAGL------SVSAREKAAIECLEKVGLLEKRRNlptQLSGGQQQRVAIAR 158
Cdd:cd03266 78 RR--LGFVSDSTGLYDRLTARENLEY---FAGLyglkgdELTARLEELADRLGMEELLDRRVG---GFSTGMRQKVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-221 |
1.92e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.40 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGG--ETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlSDNKLSE 83
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEK-KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRnKKIGFIFQqfnlLPKLSAFE-----NVELPLIYAGLSVSAREKAAIECLEKVGL-LEKRRNL-PTQLSGGQQQRVAI 156
Cdd:PRK13637 81 IR-KKVGLVFQ----YPEYQLFEetiekDIAFGPINLGLSEEEIENRVKRAMNIVGLdYEDYKDKsPFELSGGQKRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD-PTIASYGTRSIRIQDGK 221
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSmEDVAKLADRIIVMNKGK 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-221 |
1.95e-36 |
|
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: 130.99 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 27 DVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlSDNKLS---EIRNkkIGFIFQQFNLLPKLS 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIFlppHRRR--IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENVElpliYaGLSVSAREKAAIECLEKVGLLE-----KRRnlPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDS 178
Cdd:COG4148 94 VRGNLL----Y-GRKRAPRAERRISFDEVVELLGighllDRR--PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 179 KTGKEVMGILQELNRAGNT-IVMITHDPT-IASYGTRSIRIQDGK 221
Cdd:COG4148 167 ARKAEILPYLERLRDELDIpILYVSHSLDeVARLADHVVLLEQGR 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-222 |
3.03e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRNKKIGFIFQQFNLLPKLS 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKE 183
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489825110 184 VMGILQELN-RAGNTIVMITHDPTIA-SYGTRSIRIQDGKL 222
Cdd:PRK10070 203 MQDELVKLQaKHQRTIVFISHDLDEAmRIGDRIAIMQNGEV 243
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-224 |
3.14e-36 |
|
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: 127.03 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 27 DVTFTVEqGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRNKKIGFIFQQFNLLPKLSAFE 106
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 107 NVELpliyaGLSVSAREKAAI---ECLEKVGL--LEKRRnlPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTG 181
Cdd:cd03297 95 NLAF-----GLKRKRNREDRIsvdELLDLLGLdhLLNRY--PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 182 KEVMGILQELNRAGN-TIVMITHDPTIASYGTRSI-RIQDGKLFH 224
Cdd:cd03297 168 LQLLPELKQIKKNLNiPVIFVTHDLSEAEYLADRIvVMEDGRLQY 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-230 |
3.59e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.39 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 29 TFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseirnKKIGFIFQQFNLLPKLSAFENV 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 109 ELPLiYAGLSVSAREKAAIE-CLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGI 187
Cdd:PRK10771 93 GLGL-NPGLKLNAAQREKLHaIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489825110 188 LQELNRAGN-TIVMITHD----PTIAsygTRSIRIQDGKLFHEEATQA 230
Cdd:PRK10771 172 VSQVCQERQlTLLMVSHSledaARIA---PRSLVVADGRIAWDGPTDE 216
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-207 |
7.67e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 127.26 E-value: 7.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYT-----LGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNvDVFKLSD 78
Cdd:COG4167 3 ALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING-HKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 NKLseiRNKKIGFIFQQFN--LLPKLSAFENVELPLIYA-GLSVSAREKAAIECLEKVGLLEKRRNL-PTQLSGGQQQRV 154
Cdd:COG4167 82 YKY---RCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFyPHMLSSGQKQRV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELN-RAGNTIVMITHDPTI 207
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQeKLGISYIYVSQHLGI 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-201 |
1.05e-35 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 125.62 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 22 FKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIRNKKIGFIFQQFNLLPK 101
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP---PHERARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 102 LSAFENVELpliyaGLSVSAREKAAIEcLEKV-----GLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGAL 176
Cdd:cd03224 90 LTVEENLLL-----GAYARRRAKRKAR-LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180
....*....|....*....|....*
gi 489825110 177 DSKTGKEVMGILQELNRAGNTIVMI 201
Cdd:cd03224 164 APKIVEEIFEAIRELRDEGVTILLV 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-208 |
3.85e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 127.53 E-value: 3.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnk 80
Cdd:PRK11432 2 TQKNFVVLKNITKRF--GSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 lseIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGL--LEKRrnLPTQLSGGQQQRVAIAR 158
Cdd:PRK11432 75 ---IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLagFEDR--YVDQISGGQQQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDPTIA 208
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEA 200
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-209 |
4.32e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.03 E-value: 4.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCL-----DVPDEGSYHLDNVDVFKLSdnk 80
Cdd:PRK14247 4 IEIRDLKVSF---GQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRnKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSARE--KAAIECLEKVGLLEK---RRNLPT-QLSGGQQQRV 154
Cdd:PRK14247 77 VIELR-RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLWDEvkdRLDAPAgKLSGGQQQRL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAgNTIVMITHDPTIAS 209
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAA 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-205 |
4.97e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 123.75 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMN-MIGCLDvPD---EGSYHLDNVDVFKLSdnklseIRNKKIGFIFQQFNLLP 100
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLS-PAfsaSGEVLLNGRRLTALP------AEQRRIGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 101 KLSAFENV--ELPliyAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDS 178
Cdd:COG4136 90 HLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180
....*....|....*....|....*...
gi 489825110 179 KTGKEVMG-ILQELNRAGNTIVMITHDP 205
Cdd:COG4136 167 ALRAQFREfVFEQIRQRGIPALLVTHDE 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-204 |
8.31e-35 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 126.88 E-value: 8.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdNKLsEIR 85
Cdd:PRK11650 4 LKLQAVRKSYD-GK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NEL-EPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLIYAGLS---VSAREKAAIECLEKVGLLEKRrnlPTQLSGGQQQRVAIARALAG 162
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPkaeIEERVAEAARILELEPLLDRK---PRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 163 KPQILLADEPTGALDSKTgKEVMGI-LQELNRA-GNTIVMITHD 204
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKL-RVQMRLeIQRLHRRlKTTSLYVTHD 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-222 |
1.22e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.11 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTktYTLGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgCLDV-PDEGSYHLDNVDVFKLSDNKLS 82
Cdd:PRK13548 1 AMLEARNLS--VRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-SGELsPDSGEVRLNGRPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRnkkiGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALA- 161
Cdd:PRK13548 76 RRR----AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 162 -----GKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDPTIAS-YGTRSIRIQDGKL 222
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAArYADRIVLLHQGRL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-222 |
2.61e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.69 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVdvfKLSDNKLSEI 84
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQ-FNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGK 163
Cdd:PRK13650 80 R-HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 164 PQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-207 |
2.93e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 127.90 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKS-TLMNMIGCLDVPD----EGSYHLDNVDVFK 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 76 LSDNKLSEIRNKKIGFIFQQfnLLPKLSAFENVELPLiYAGLSV--SAREKAA----IECLEKVGLLEKRRNL---PTQL 146
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQE--PMVSLNPLHTLEKQL-YEVLSLhrGMRREAArgeiLNCLDRVGIRQAAKRLtdyPHQL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 147 SGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHDPTI 207
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNmGLLFITHNLSI 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-203 |
2.98e-34 |
|
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: 120.23 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNklsEIR 85
Cdd:cd03216 1 LELRGITKRF--GG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR---DAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQqfnllpklsafenvelpliyaglsvsarekaaieclekvgllekrrnlptqLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190
....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-222 |
4.48e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 128.45 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnklSEIR 85
Cdd:TIGR03375 464 IEFRNVSFAYP--GQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDP---ADLR 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQqfnllpklsafenvELPLIYAGL-------SVSAREKAAIECLEKVGLLEKRRNLPT-----------QLS 147
Cdd:TIGR03375 539 -RNIGYVPQ--------------DPRLFYGTLrdnialgAPYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLS 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 148 GGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-203 |
4.50e-34 |
|
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: 121.95 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSEIR 85
Cdd:cd03251 1 VEFKNVTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQ---FNLlpklSAFENVElpliYAGLSVSarEKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQ 151
Cdd:cd03251 76 -RQIGLVSQDvflFND----TVAENIA----YGRPGAT--REEVEEAARAANAHEFIMELPegydtvigergVKLSGGQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 152 QRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVmITH 203
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-203 |
5.13e-34 |
|
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: 121.88 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSEIRNKkIGFIFQQFNLLPKl 102
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLRSQ-IGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 103 SAFENVELPLIYAglSVSAREKAAieclEKVGLLEKRRNLP-----------TQLSGGQQQRVAIARALAGKPQILLADE 171
Cdd:cd03249 92 TIAENIRYGKPDA--TDEEVEEAA----KKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190
....*....|....*....|....*....|..
gi 489825110 172 PTGALDSKTGKEVMGILQELnRAGNTIVMITH 203
Cdd:cd03249 166 ATSALDAESEKLVQEALDRA-MKGRTTIVIAH 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-222 |
9.13e-34 |
|
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: 124.07 E-value: 9.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 27 DVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRNKKIGFIFQQFNLLPKLSAFE 106
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 107 NVELPLIYA-GLSVSAREKAAIECLEKVGLLEKrrnLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVM 185
Cdd:TIGR02142 95 NLRYGMKRArPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 489825110 186 GILQELNRAGNT-IVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:TIGR02142 172 PYLERLHAEFGIpILYVSHSLQeVLRLADRVVVLEDGRV 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
1.04e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.11 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGEtfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfKLSDNKLSEI 84
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQfnllPKLSAF-----ENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARA 159
Cdd:PRK13639 77 R-KTVGIVFQN----PDDQLFaptveEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIAS-YGTRSIRIQDGKLFHE 225
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKE 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-224 |
1.34e-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: 120.96 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhlDNVDVF--KLSDNKL 81
Cdd:COG1119 2 PLLELRNVTVRR---GGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFgeRRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIRnKKIGFI--FQQFNLLPKLSAFENVelpliyagLS-----------VSAREKA-AIECLEKVGLLEKRRNLPTQLS 147
Cdd:COG1119 74 WELR-KRIGLVspALQLRFPRDETVLDVV--------LSgffdsiglyrePTDEQRErARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 148 GGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHD-----PTIasygTRSIRIQDGK 221
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHveeipPGI----THVLLLKDGR 220
|
...
gi 489825110 222 LFH 224
Cdd:COG1119 221 VVA 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-222 |
1.80e-33 |
|
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: 120.00 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLpKLSAFENVELpliyAGLSVSAREkaAIECLEKVGLLEKRRNLPT-----------QLSGGQQQRV 154
Cdd:cd03245 78 -RNIGYVPQDVTLF-YGTLRDNITL----GAPLADDER--ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-225 |
2.02e-33 |
|
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: 125.69 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLD--VPDEGS--YHL------------- 68
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRiiYHValcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 69 ---------------DNVDVFKLSDNKLSEIRnKKIGFIFQQ-FNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEK 132
Cdd:TIGR03269 77 kvgepcpvcggtlepEEVDFWNLSDKLRRRIR-KRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 133 VGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHDP-TIASY 210
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPeVIEDL 235
|
250
....*....|....*
gi 489825110 211 GTRSIRIQDGKLFHE 225
Cdd:TIGR03269 236 SDKAIWLENGEIKEE 250
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-208 |
2.14e-33 |
|
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: 125.86 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYtlGGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDvfkLSDNKL 81
Cdd:TIGR02857 318 PASSLEFSGVSVAY--PGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP---LADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIRnKKIGFIFQQFNLLPKlSAFENVELPLIYAGlsvsarEKAAIECLEKVGLLEKRRNLP-----------TQLSGGQ 150
Cdd:TIGR02857 392 DSWR-DQIAWVPQHPFLFAG-TIAENIRLARPDAS------DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRaGNTIVMITHDPTIA 208
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA 520
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-222 |
2.40e-33 |
|
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: 118.09 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTktYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLsdnKLSEIR 85
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKlSAFENVelpliyaglsvsarekaaieclekvgllekrrnlptqLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03246 76 -DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-222 |
2.93e-33 |
|
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: 119.20 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTF-----------TVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseirnKKIGFI 92
Cdd:TIGR01277 2 ALDKVRYeyehlpmefdlNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 93 FQQFNLLPKLSAFENVELPLiYAGLSVSAREKAAIECL-EKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADE 171
Cdd:TIGR01277 76 FQENNLFAHLTVRQNIGLGL-HPGLKLNAEQQEKVVDAaQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 172 PTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLcSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-222 |
3.86e-33 |
|
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: 118.51 E-value: 3.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdnKLSEiRNKK 88
Cdd:cd03226 3 ENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKE-RRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 89 IGFIFQ--QFNLLpklsaFENVELPLIYaGLSVSAREKAAIEC-LEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03226 73 IGYVMQdvDYQLF-----TDSVREELLL-GLKELDAGNEQAETvLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAI 204
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-208 |
4.25e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 118.29 E-value: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfKLSDNKLSEIRnKKIGFIFQQF-NLLPK 101
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERR-QRVGLVFQDPdDQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 102 LSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTG 181
Cdd:TIGR01166 84 ADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*..
gi 489825110 182 KEVMGILQELNRAGNTIVMITHDPTIA 208
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-203 |
4.57e-33 |
|
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: 118.47 E-value: 4.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNklseir 85
Cdd:cd03268 1 LKTNDLTKTY--GKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLIYAGLsvsaREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-204 |
6.32e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLS 82
Cdd:PRK13632 5 SVMIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRnKKIGFIFQ----QF--NLLPKLSAF--ENVELPliyaglsvSAREKAAIECL-EKVGLLEKRRNLPTQLSGGQQQR 153
Cdd:PRK13632 80 EIR-KKIGIIFQnpdnQFigATVEDDIAFglENKKVP--------PKKMKDIIDDLaKKVGMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHD 204
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHD 202
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-204 |
8.35e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 121.17 E-value: 8.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgcLDVPDEG------SYHLDNVDVFKLS 77
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITKDNwhvtadRFRWNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 78 DNKLSEIRNKKIGFIFQ--QFNLLPKLSAFENVE--LPLIYAGLSV----SAREKAAIECLEKVGLLEKR---RNLPTQL 146
Cdd:COG4170 80 PRERRKIIGREIAMIFQepSSCLDPSAKIGDQLIeaIPSWTFKGKWwqrfKWRKKRAIELLHRVGIKDHKdimNSYPHEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 147 SGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNT-IVMITHD 204
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTsILLISHD 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-204 |
9.31e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 120.62 E-value: 9.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKS-TLMNMIGCLDVPDE---GSYHLDNVDVFKLSDNK 80
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKKIGFIFQQ--FNLLPKLS-AFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNL---PTQLSGGQQQRV 154
Cdd:PRK11022 83 RRNLVGAEVAMIFQDpmTSLNPCYTvGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHD 204
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHD 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-217 |
1.08e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 116.95 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDnvdvfklsdnklseiRNKKIGFIFQQFNL---LP 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---------------GGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 101 kLSAFENVELPLI-YAGLS--VSAREKAAIE-CLEKVGL--LEKRRnLPTqLSGGQQQRVAIARALAGKPQILLADEPTG 174
Cdd:NF040873 72 -LTVRDLVAMGRWaRRGLWrrLTRDDRAAVDdALERVGLadLAGRQ-LGE-LSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489825110 175 ALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRI 217
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-203 |
4.50e-32 |
|
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: 115.84 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNvdvfklsdNKLSEIR 85
Cdd:cd03269 1 LEVENVTKRF---GRV-TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENvelpLIY----AGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALA 161
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQ----LVYlaqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTH 186
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-225 |
5.82e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.96 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGE-TFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVF-KLSDNKLSE 83
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRnKKIGFIFQqfnlLPKLSAFE-NVELPLIYA----GLSVSAREKAAIECLEKVGLlekRRNL----PTQLSGGQQQRV 154
Cdd:PRK13646 83 VR-KRIGMVFQ----FPESQLFEdTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGF---SRDVmsqsPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHDPT-IASYGTRSIRIQDGKLFHE 225
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENkTIILVSHDMNeVARYADEVIVMKEGSIVSQ 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-225 |
5.89e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 116.72 E-value: 5.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSeir 85
Cdd:COG4604 2 IEIKNVSKRY---GGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVEL---PliYAGLSVSAREKAAI-ECLEKVGLLE-KRRNLpTQLSGGQQQRVAIARAL 160
Cdd:COG4604 75 -KRLAILRQENHINSRLTVRELVAFgrfP--YSKGRLTAEDREIIdEAIAYLDLEDlADRYL-DELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQ----ELNRagnTIVMITHDPTIAS-YGTRSIRIQDGKLFHE 225
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRrladELGK---TVVIVLHDINFAScYADHIVAMKDGRVVAQ 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-209 |
6.27e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 117.07 E-value: 6.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCL------DVPDEGSYHLDNVDVFKLSDNKLseirNKKIGFIFQQFNL 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKL----RKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 99 LPKLSAFENVELPLIYAGLSvSAREKAAI--ECLEKVGLLEK---RRNLP-TQLSGGQQQRVAIARALAGKPQILLADEP 172
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIK-EKREIKKIveECLRKVGLWKEvydRLNSPaSQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 489825110 173 TGALDSKTGKEVMGILQELNRAgNTIVMITHDPTIAS 209
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVA 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
1.17e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.39 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTlGGETFkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSE 83
Cdd:PRK13648 6 SIIVFKNVSFQYQ-SDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRnKKIGFIFQ----QF--NLLPKLSAF--ENvelpliyagLSVSAREKAAI--ECLEKVGLLEKRRNLPTQLSGGQQQR 153
Cdd:PRK13648 81 LR-KHIGIVFQnpdnQFvgSIVKYDVAFglEN---------HAVPYDEMHRRvsEALKQVDMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHDPTIASYGTRSIRIQDGKLFHE 225
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-222 |
1.45e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK 80
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKkIGFIFQQ-FNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARA 159
Cdd:PRK13640 79 VWDIREK-VGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-202 |
1.81e-31 |
|
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: 114.95 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP---MHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 489825110 166 ILLADEPTGALDSKTGKEVMGILQELNRAGntI-VMIT 202
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRG--IgVLIT 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-205 |
2.13e-31 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 120.16 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTL-MNMIGCLDvPDEGSYHLDNVDVFKLSDNKLSeirnKKIGFIFQQFNLLPKl 102
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLD-PLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 103 SAFENVelpLIYAGlsvSAREKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQQRVAIARALAGKPQILLADE 171
Cdd:TIGR02868 424 TVRENL---RLARP---DATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....*.
gi 489825110 172 PTGALDSKTGKEvmgILQELNRA--GNTIVMITHDP 205
Cdd:TIGR02868 498 PTEHLDAETADE---LLEDLLAAlsGRTVVLITHHL 530
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-204 |
2.17e-31 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 117.21 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgCLDVPDE-----GSYHLDNVDVFKLSD 78
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAI-CGVTKDNwrvtaDRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 NKLSEIRNKKIGFIFQQfnllPK--LSAFENVELPLI-------YAG---LSVSAREKAAIECLEKVGLLEKR---RNLP 143
Cdd:PRK15093 81 RERRKLVGHNVSMIFQE----PQscLDPSERVGRQLMqnipgwtYKGrwwQRFGWRKRRAIELLHRVGIKDHKdamRSFP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 144 TQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHD 204
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHD 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-201 |
3.03e-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: 114.69 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlgGEtFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklSE 83
Cdd:COG0410 2 PMLEVENLHAGY---GG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP----PH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRNKK-IGFIFQQFNLLPKLSAFENVELPLiYAGLSVSAREKAaiecLEKVG-----LLEKRRNLPTQLSGGQQQRVAIA 157
Cdd:COG0410 74 RIARLgIGYVPEGRRIFPSLTVEENLLLGA-YARRDRAEVRAD----LERVYelfprLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 158 RALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMI 201
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-203 |
3.09e-31 |
|
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: 114.63 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGgetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSEIR 85
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQ---FNllpklsafENVELPLIYAGLSVSarEKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQ 151
Cdd:cd03253 75 -RAIGVVPQDtvlFN--------DTIGYNIRYGRPDAT--DEEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 152 QRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITH 203
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-203 |
3.13e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.89 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK-LSEIRnKKIGFIFQqfnlLPK 101
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKkLKPLR-KKVGIVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 102 LSAFE-NVELPLIYA----GLSVSAREKAAIECLEKVGLLEK-RRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGA 175
Cdd:PRK13634 96 HQLFEeTVEKDICFGpmnfGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180
....*....|....*....|....*....
gi 489825110 176 LDSKTGKEVMGILQELNRAGN-TIVMITH 203
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGlTTVLVTH 204
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-222 |
3.63e-31 |
|
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: 114.93 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYTLGgetfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDN-----VDVFKLS 77
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 78 DNKLSEIRNKKIGFIFQQF--NLLPKLSAFENVELPLIYAGLSVSAREKA-AIECLEKVGLLEKR-RNLPTQLSGGQQQR 153
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRAtAQDWLEEVEIDPTRiDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPTIAS-YGTRSIRIQDGKL 222
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRdLGLAVIIVTHDLGVARlLAQRLLVMQQGRV 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
4.27e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.22 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGetfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSyhldnVDVFKLSDNKLSE-- 83
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR-----VKVMGREVNAENEkw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRNKkIGFIFQQ-FNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAG 162
Cdd:PRK13647 77 VRSK-VGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 163 KPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA-SYGTRSIRIQDGK 221
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAaEWADQVIVLKEGR 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-230 |
5.49e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.86 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTktYTLGGEtfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:PRK11831 7 LVDMRGVS--FTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQFNLLPKLSAFENVELPLI-YAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGK 163
Cdd:PRK11831 83 R-KRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 164 PQILLADEPTGALDSKTgkevMGIL----QELNRA-GNTIVMITHD-PTIASYGTRSIRIQDGKLFHEEATQA 230
Cdd:PRK11831 162 PDLIMFDEPFVGQDPIT----MGVLvkliSELNSAlGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-208 |
6.69e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 114.25 E-value: 6.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGEtfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDN-----VDVFK 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLY--GPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 76 LSDNKLSEIRNKKIGFIFQ--QFNLLPKLSAFENVELPLiyagLSVSAR-----EKAAIECLEKVGLLEKR-RNLPTQLS 147
Cdd:PRK11701 78 LSEAERRRLLRTEWGFVHQhpRDGLRMQVSAGGNIGERL----MAVGARhygdiRATAGDWLERVEIDAARiDDLPTTFS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 148 GGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDPTIA 208
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVA 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-226 |
9.91e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 113.09 E-value: 9.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSEIR 85
Cdd:cd03254 3 IEFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKkIGFIFQQFNLLPKlSAFENvelpLIYAGLSvsAREKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQQRV 154
Cdd:cd03254 77 SM-IGVVLQDTFLFSG-TIMEN----IRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRaGNTIVMITHDPTIASYGTRSIRIQDGKLF----HEE 226
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKIIeegtHDE 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-206 |
1.15e-30 |
|
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: 111.87 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYT--LGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDVP-DEGSYHLDNVDVfklsdnKL 81
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPL------DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIRnKKIGFIFQQFNLLPKLSAFENvelpliyagLSVSAREKaaieclekvgllekrrnlptQLSGGQQQRVAIARALA 161
Cdd:cd03213 78 RSFR-KIIGYVPQDDILHPTLTVRET---------LMFAAKLR--------------------GLSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT 206
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPS 172
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-203 |
5.12e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.90 E-value: 5.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRNKKIGFIFQqfnlLPKL 102
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 103 SAFENVELPLIYAG-----LSVSAREKAAIECLEKVGLL-EKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGAL 176
Cdd:PRK13643 96 QLFEETVLKDVAFGpqnfgIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 489825110 177 DSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-226 |
5.20e-30 |
|
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: 116.74 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDvfkLSDNKLSEI 84
Cdd:TIGR02203 330 DVEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD---LADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKkIGFIFQQFNLLPKlSAFENVElpliYAGLS--VSAREKAAiecLEKVGLLEKRRNLP-----------TQLSGGQQ 151
Cdd:TIGR02203 405 RRQ-VALVSQDVVLFND-TIANNIA----YGRTEqaDRAEIERA---LAAAYAQDFVDKLPlgldtpigengVLLSGGQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 152 QRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVmITHDPTIASYGTRSIRIQDGKLF----HEE 226
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLV-IAHRLSTIEKADRIVVMDDGRIVergtHNE 553
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-204 |
7.26e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.51 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgcLDV--PDEGSYHLDNvdvfklsdNKLSE 83
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII--LGIlaPDSGEVLWDG--------EPLDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRNKKIGFIFQQFNLLPKLSAFENvelpLIY----AGLSVSAREKAAIECLEKVGLLEkRRNLPTQ-LSGGQQQRVAIAR 158
Cdd:COG4152 68 EDRRRIGYLPEERGLYPKMKVGEQ----LVYlarlKGLSKAEAKRRADEWLERLGLGD-RANKKVEeLSKGNQQKVQLIA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-204 |
9.62e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 112.88 E-value: 9.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 21 TFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRnKKIGFIFQQ--FNL 98
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 99 LPKLSAFENVELPLI--YAGLSVSAREKAAIECLEKVGLLEKRRN-LPTQLSGGQQQRVAIARALAGKPQILLADEPTGA 175
Cdd:PRK15079 112 NPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190
....*....|....*....|....*....|
gi 489825110 176 LDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-204 |
1.42e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.19 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETFK-------ALDDVTFTVEQGEFLSIVGPSGSGKST----LMNMIgcldvPDEGSYHLDNVD 72
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 73 VFKLSDNKLSEIRnKKIGFIFQQFN--LLPKLSAFENVE--LPLIYAGLSVSAREKAAIECLEKVGL-LEKRRNLPTQLS 147
Cdd:PRK15134 349 LHNLNRRQLLPVR-HRIQVVFQDPNssLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFS 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 148 GGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHD 204
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHD 485
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-204 |
1.87e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.82 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYtlgGETFKAlDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhldnvDVFkLSDNKLSEIRNK 87
Cdd:PRK11000 6 LRNVTKAY---GDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-------DLF-IGEKRMNDVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 K--IGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREK---AAIECLEKVGLLEKRrnlPTQLSGGQQQRVAIARALAG 162
Cdd:PRK11000 74 ErgVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQrvnQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489825110 163 KPQILLADEPTGALDS----KTGKEVMGILQELNRagnTIVMITHD 204
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalrvQMRIEISRLHKRLGR---TMIYVTHD 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-204 |
6.33e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 113.36 E-value: 6.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTY-TLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHL----DNVDVFKLS 77
Cdd:TIGR03269 277 EPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 78 dnKLSEIRNKK-IGFIFQQFNLLPKLSAFEN------VELP-------LIYAGLSVSAREKAAIECLEKvgllekrrnLP 143
Cdd:TIGR03269 357 --PDGRGRAKRyIGILHQEYDLYPHRTVLDNlteaigLELPdelarmkAVITLKMVGFDEEKAEEILDK---------YP 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 144 TQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVM-GILQELNRAGNTIVMITHD 204
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHD 487
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-226 |
1.37e-28 |
|
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: 107.23 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGG------------------ETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSyh 67
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 68 ldnVDVfklsDNKLSEIRNKKIGFifqqfnlLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGlLEKRRNLPT-QL 146
Cdd:cd03220 79 ---VTV----RGRVSSLLGLGGGF-------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSE-LGDFIDLPVkTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 147 SGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIRIQDGKLFHE 225
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPsSIKRLCDRALVLEKGKIRFD 223
|
.
gi 489825110 226 E 226
Cdd:cd03220 224 G 224
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-204 |
1.97e-28 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 106.86 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 30 FTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNvdvfklsdnKLSEIRNKKIGFIFQQFNLlpklsafeNVE 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---------ASPGKGWRHIGYVPQRHEF--------AWD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 110 LPLIYAGLSVSARE--------------KAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGA 175
Cdd:TIGR03771 64 FPISVAHTVMSGRTghigwlrrpcvadfAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180
....*....|....*....|....*....
gi 489825110 176 LDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGAGTAILMTTHD 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-209 |
2.29e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.62 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCL-----DVPDEGSYHLDNVDVFKLSDNKLsEIRnKKIGFIFQQFNLL 99
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI-EVR-REVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 100 PKLSAFENVELPLIYAGLSVSARE--KAAIECLEKVGLLEKRRN----LPTQLSGGQQQRVAIARALAGKPQILLADEPT 173
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 489825110 174 GALDSKTGKEVMGILQELnRAGNTIVMITHDPTIAS 209
Cdd:PRK14267 178 ANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAA 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-222 |
5.19e-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: 104.70 E-value: 5.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDvPDEGSYHLDNVDVFKLSDNklsei 84
Cdd:cd03247 1 LSINNVSFSY--PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLK-PQQGEITLDGVPVSDLEKA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKKIGFIFQQfnllpklsafenvelPLIYAGlsvsarekaaieclekvgllEKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:cd03247 73 LSSLISVLNQR---------------PYLFDT--------------------TLRNNLGRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRaGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-202 |
7.92e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.88 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYtlGGETfkALDDVTFTVEQGEflsIV---GPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKlseiR 85
Cdd:COG1137 7 ENLVKSY--GKRT--VVKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKK-IGF------IFQqfnllpKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIAR 158
Cdd:COG1137 76 ARLgIGYlpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGntI-VMIT 202
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG--IgVLIT 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-204 |
1.29e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.92 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETFKA-----LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSD 78
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 NKLSEIRnKKIGFIFQQ----FNllPKLSAFENVELPLIY-AGLSVSAREKAAIECLEKVGL-LEKRRNLPTQLSGGQQQ 152
Cdd:PRK10419 82 AQRKAFR-RDIQMVFQDsisaVN--PRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 153 RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHD 204
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHD 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
1.48e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.16 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKpLIDMKNLTKTYTLG------------------GETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPD 62
Cdd:COG1134 1 MSS-MIEVENVSKSYRLYhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 63 EGSYhldnvdvfklsdnklseIRNKKIGFI------FQqfnllPKLSAFENVELP-LIYaGLS---VSAREKAAIECLEk 132
Cdd:COG1134 80 SGRV-----------------EVNGRVSALlelgagFH-----PELTGRENIYLNgRLL-GLSrkeIDEKFDEIVEFAE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 133 vglLEKRRNLPTQ-LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASY 210
Cdd:COG1134 136 ---LGDFIDQPVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMgAVRRL 212
|
250
....*....|..
gi 489825110 211 GTRSIRIQDGKL 222
Cdd:COG1134 213 CDRAIWLEKGRL 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-225 |
1.97e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSeirnKK 88
Cdd:PRK11231 6 ENLTVGY---GTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 89 IGFIFQQfNLLPK-LSAFENVE------LPLiYAGLSVSAREKA--AIECLEKVGLLEKRRnlpTQLSGGQQQRVAIARA 159
Cdd:PRK11231 78 LALLPQH-HLTPEgITVRELVAygrspwLSL-WGRLSAEDNARVnqAMEQTRINHLADRRL---TDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIAS-YGTRSIRIQDGKLFHE 225
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQ 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-203 |
2.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 20 ETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGS------YHLDNVDVFKLSDNKLS-EIRN-----K 87
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgdiYIGDKKNNHELITNPYSkKIKNfkelrR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGFIFQqfnlLPKLSAFEN-VELPLIYA--GLSVS---AREKAAIEcLEKVGLLEK--RRNlPTQLSGGQQQRVAIARA 159
Cdd:PRK13631 117 RVSMVFQ----FPEYQLFKDtIEKDIMFGpvALGVKkseAKKLAKFY-LNKMGLDDSylERS-PFGLSGGQKRRVAIAGI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITH 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-219 |
3.76e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.47 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLM---NMIGCL--DVPDEGSYHLDNVDVFK 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYN----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 76 LSDNKLsEIRnKKIGFIFQQFNLLPkLSAFENVELPLIYAGLSVSAREKAAIE-CLEKVGLLEKRRNL----PTQLSGGQ 150
Cdd:PRK14239 77 PRTDTV-DLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIWDEVKDRlhdsALGLSGGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIASygtrsiRIQD 219
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQAS------RISD 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-204 |
4.14e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYtlGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDnvdvfklsdnklseiRNK 87
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGFIFQQFNLLPKLSAFENV------------ELPLIYAGLSVSAREKAAIECLE--------------------KVGL 135
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaELEELEAKLAEPDEDLERLAELQeefealggweaearaeeilsGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 136 LEKRRNLP-TQLSGGQQQRVAIARALAGKPQILLADEPTGALDsktgkeVMGI--LQE-LNRAGNTIVMITHD 204
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIewLEEfLKNYPGTVLVVSHD 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-207 |
4.55e-27 |
|
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: 108.30 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTktYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLdVPDEGSYHLDNVDVFKLSDNK 80
Cdd:COG4618 327 PKGRLSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIrnkkIGFifqqfnlLPklsafENVELpliYAGlSVS---AR------EKAaIECLEKVGLLEKRRNLP-------- 143
Cdd:COG4618 404 LGRH----IGY-------LP-----QDVEL---FDG-TIAeniARfgdadpEKV-VAAAKLAGVHEMILRLPdgydtrig 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 144 ---TQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTI 207
Cdd:COG4618 463 eggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSL 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-226 |
9.95e-27 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 102.95 E-value: 9.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 14 TYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLseirNKKIGFIF 93
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 94 QQfNLLPKLSAFENVELpliyaglsvsAREKAAIECLEKVGLL----EKRRNLP-----------TQLSGGQQQRVAIAR 158
Cdd:cd03252 83 QE-NVLFNRSIRDNIAL----------ADPGMSMERVIEAAKLagahDFISELPegydtivgeqgAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQELNrAGNTIVMITHDPTIASYGTRSIRIQDGKLF----HEE 226
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNADRIIVMEKGRIVeqgsHDE 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-191 |
1.15e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.33 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKT--YTLG---GETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDnvdvfklsDN 79
Cdd:PRK15112 4 LLEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID--------DH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 80 KLS----EIRNKKIGFIFQ--QFNLLPKLSAFENVELPLIY-AGLSVSAREKAAIECLEKVGLLEKRRNL-PTQLSGGQQ 151
Cdd:PRK15112 76 PLHfgdySYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 152 QRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL 191
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-216 |
1.28e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 101.80 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 26 DDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDnklseirnkkigfIFQQfNLL------ 99
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-------------EYHQ-DLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 100 ---PKLSAFENVelpLIYAGLSVSAREKAAIECLEKVGLlEKRRNLPT-QLSGGQQQRVAIARALAGKPQILLADEPTGA 175
Cdd:PRK13538 84 gikTELTALENL---RFYQRLHGPGDDEALWEALAQVGL-AGFEDVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489825110 176 LDSKTGKEVMGILQELNRAGNTIVMITHDP-TIASYGTRSIR 216
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQGGMVILTTHQDlPVASDKVRKLR 201
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-203 |
1.36e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 106.41 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GcldVPDEGSY----HLDNvDVFKLSDN 79
Cdd:NF040905 1 ILEMRGITKTF--PG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsG---VYPHGSYegeiLFDG-EVCRFKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 80 KLSEirNKKIGFIFQQFNLLPKLSAFENvelplIYAGLSVSAR--------EKAAIECLEKVGLLEKRRNLPTQLSGGQQ 151
Cdd:NF040905 73 RDSE--ALGIVIIHQELALIPYLSIAEN-----IFLGNERAKRgvidwnetNRRARELLAKVGLDESPDTLVTDIGVGKQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 152 QRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-204 |
1.66e-26 |
|
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: 100.58 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTktytlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLS 82
Cdd:cd03215 2 EPVLEVRGLS--------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---PR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKKIGFI---FQQFNLLPKLSAFENVelpliyaglsvsarekaaieclekvgllekrrNLPTQLSGGQQQRVAIARA 159
Cdd:cd03215 71 DAIRAGIAYVpedRKREGLVLDLSVAENI--------------------------------ALSSLLSGGNQQKVVLARW 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE 163
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-225 |
1.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGetfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnKLSEI 84
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQ----QF--NLLPKLSAF--ENVELPLIyaglSVSAREKAAiecLEKVGLLEKRRNLPTQLSGGQQQRVAI 156
Cdd:PRK13644 76 R-KLVGIVFQnpetQFvgRTVEEDLAFgpENLCLPPI----EIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGKLFHE 225
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-203 |
2.26e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.14 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhldNVDVFKLSDNK 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSY--GDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-----KITVLGVPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSvsARE-KAAIECLEKVGLLEKRRNLP-TQLSGGQQQRVAIAR 158
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMS--TREiEAVIPSLLEFARLESKADARvSDLSGGMKRRLTLAR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-204 |
2.67e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.89 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIRNKK 88
Cdd:PRK10895 7 KNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 89 IGFIFQQFNLLPKLSAFENVELPL-IYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQIL 167
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489825110 168 LADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-209 |
2.99e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTktYTLGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSE 83
Cdd:PRK09536 2 PMIDVSDLS--VEFGDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 I-----RNKKIGFIFQ-----QFNLLPKLSAFenvelpliyaGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQR 153
Cdd:PRK09536 78 RvasvpQDTSLSFEFDvrqvvEMGRTPHRSRF----------DTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIAS 209
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAA 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-203 |
4.19e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.57 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLseirNKKIGfIFQQFNLLPKLSA 104
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVA-LVGQEPVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELPLIYAGLS-VSAREKAAiECLEKVGLLEKRRNLP-----TQLSGGQQQRVAIARALAGKPQILLADEPTGALDS 178
Cdd:TIGR00958 572 RENIAYGLTDTPDEeIMAAAKAA-NAHDFIMEFPNGYDTEvgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180
....*....|....*....|....*.
gi 489825110 179 ktgkEVMGILQEL-NRAGNTIVMITH 203
Cdd:TIGR00958 651 ----ECEQLLQESrSRASRTVLLIAH 672
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-203 |
5.18e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.29 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKL 81
Cdd:PRK11160 335 DQVSLTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 seiRNKkIGFIFQQFNLLpklSAF--ENvelpLIYAglSVSAREKAAIECLEKVGL---LEKRRNLPT-------QLSGG 149
Cdd:PRK11160 413 ---RQA-ISVVSQRVHLF---SATlrDN----LLLA--APNASDEALIEVLQQVGLeklLEDDKGLNAwlgeggrQLSGG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489825110 150 QQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRaGNTIVMITH 203
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-222 |
7.17e-26 |
|
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: 104.74 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSeirnKKIGFIFQQFNLLPKLSA 104
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELFPGTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 fENVelpliyAGLSVSAREKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQQRVAIARALAGKPQILLADEPT 173
Cdd:TIGR01842 410 -ENI------ARFGENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 174 GALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-204 |
1.18e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.79 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTktYTLGGEtfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklS 82
Cdd:PRK10247 5 SPLLQLQNVG--YLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKKIGFIFQQfnllPKL---SAFENVELPliYAGLSVSAREKAAIECLEKVGL----LEKRRNlptQLSGGQQQRVA 155
Cdd:PRK10247 77 EIYRQQVSYCAQT----PTLfgdTVYDNLIFP--WQIRNQQPDPAIFLDDLERFALpdtiLTKNIA---ELSGGEKQRIS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVM-ITHD 204
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHD 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-222 |
1.23e-25 |
|
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: 99.49 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQ---------QFNLLPkLSAFENVELpliyaglsvsarekaaIECLEKVGLLEKRRNLPTQL---------- 146
Cdd:cd03244 78 -SRISIIPQdpvlfsgtiRSNLDP-FGEYSDEEL----------------WQALERVGLKEFVESLPGGLdtvveeggen 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 147 -SGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQElNRAGNTIVMITHD-PTIASYGtRSIRIQDGKL 222
Cdd:cd03244 140 lSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRlDTIIDSD-RILVLDKGRV 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-206 |
1.72e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 99.27 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDvpdEGSYHLDNVDVFKLSDNKLSEIRnKKIGFIFQQFNLLPKL 102
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGQILFNGQPRKPDQFQ-KCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 103 SAFENVELPLIYAG---LSVSAREK-AAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDS 178
Cdd:cd03234 97 TVRETLTYTAILRLprkSSDAIRKKrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180
....*....|....*....|....*...
gi 489825110 179 KTGKEVMGILQELNRAGNTIVMITHDPT 206
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPR 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-222 |
2.66e-25 |
|
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: 98.94 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYT-------LGG----------ETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHL 68
Cdd:cd03267 1 IEVSNLSKSYRvyskepgLIGslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 69 DNVDVFKLSDNKLseirnKKIGFIFQQFN-LLPKLSAFENVEL-PLIYaGLSvSAREKAAIECLEKVGLLEKRRNLPT-Q 145
Cdd:cd03267 81 AGLVPWKRRKKFL-----RRIGVVFGQKTqLWWDLPVIDSFYLlAAIY-DLP-PARFKKRLDELSELLDLEELLDTPVrQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD-PTIASYGTRSIRIQDGKL 222
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-230 |
2.68e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.35 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTkTYTLGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI--------GCLDVPDEGsyhldnvDVFkls 77
Cdd:COG4178 363 LALEDLT-LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsGRIARPAGA-------RVL--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 78 dnklseirnkkigFIFQQfnllPKLsafenvelP-------LIYAGLSVSAREKAAIECLEKVGL------LEKRRNLPT 144
Cdd:COG4178 430 -------------FLPQR----PYL--------PlgtlreaLLYPATAEAFSDAELREALEAVGLghlaerLDEEADWDQ 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 145 QLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQElNRAGNTIVMITHDPTIASYGTRSIRIQDGKLFH 224
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQ 563
|
....*.
gi 489825110 225 EEATQA 230
Cdd:COG4178 564 LLPAEA 569
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-203 |
4.72e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgCLDVPdEGSYhlDNVDVFKLSDNK 80
Cdd:PRK13549 1 MMEYLLEMKNITKTF--GG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYP-HGTY--EGEIIFEGEELQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRN---KKIGFIFQQFNLLPKLSAFENVEL--PLIYAGL----SVSARekaAIECLEKVGLlEKRRNLPT-QLSGGQ 150
Cdd:PRK13549 73 ASNIRDterAGIAIIHQELALVKELSVLENIFLgnEITPGGImdydAMYLR---AQKLLAQLKL-DINPATPVgNLGLGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-203 |
1.36e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLdvPDEGSYHLDNVDvfkLSDNKLSEIRnKKIGFIFQqfN-LLPKL 102
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALlGFL--PYQGSLKINGIE---LRELDPESWR-KHLSWVGQ--NpQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 103 SAFENVELPliyaglSVSAREKAAIECLEKVGLLEKRRNLP----TQ-------LSGGQQQRVAIARALAGKPQILLADE 171
Cdd:PRK11174 438 TLRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPqgldTPigdqaagLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 489825110 172 PTGALDSKTGKEVMGILQElNRAGNTIVMITH 203
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNA-ASRRQTTLMVTH 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-203 |
2.56e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.24 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLsDNK 80
Cdd:PRK09700 1 MATPYISMAGIGKSF--GPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEirNKKIGFIFQQFNLLPKLSAFENV---ELPL-IYAGLSV----SAREKAAIeCLEKVGLLEKRRNLPTQLSGGQQQ 152
Cdd:PRK09700 76 LAA--QLGIGIIYQELSVIDELTVLENLyigRHLTkKVCGVNIidwrEMRVRAAM-MLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489825110 153 RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-204 |
3.92e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.64 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCL-----DVPDEGSYHLDNVDVFKLSD 78
Cdd:PRK14258 6 PAIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 NkLSEIRnKKIGFIFQQFNLLPkLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLL-----EKRRNLPTQLSGGQQQR 153
Cdd:PRK14258 82 N-LNRLR-RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwdeikHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELN-RAGNTIVMITHD 204
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-203 |
4.16e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.02 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 40 IVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlSDNKLS---EIRnkKIGFIFQQFNLLPKLSafenVELPLIYaG 116
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD-AEKGIClppEKR--RIGYVFQDARLFPHYK----VRGNLRY-G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 117 LSVSAREK-AAIECLEKVGLLEKRrnLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAG 195
Cdd:PRK11144 101 MAKSMVAQfDKIVALLGIEPLLDR--YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
....*....
gi 489825110 196 NT-IVMITH 203
Cdd:PRK11144 179 NIpILYVSH 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-204 |
5.30e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYTLGGETFK-------ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFK 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 76 LSDNKLSEIRnKKIGFIFQQ--FNLLPKLSAFENVELPLIYAGL--SVSAREKAAiECLEKVGLL-EKRRNLPTQLSGGQ 150
Cdd:PRK10261 391 LSPGKLQALR-RDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLlpGKAAAARVA-WLLERVGLLpEHAWRYPHEFSGGQ 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHD 523
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-203 |
7.30e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.80 E-value: 7.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlgGETFkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdNK 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY---GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSvSAREKAAIECLEKVGLLEKRRNLPT-QLSGGQQQRVAIARA 159
Cdd:PRK13537 74 RARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLS-AAAARALVPPLLEFAKLENKADAKVgELSGGMKRRLTLARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-204 |
8.46e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.44 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF--GG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 lseIRNKKIGFIFQQFNLLPKLSAFEN--------VELPLIyAGL----SVSAREKAAIE----CLEKVGLLEKRRNLPT 144
Cdd:PRK11300 77 ---IARMGVVRTFQHVRLFREMTVIENllvaqhqqLKTGLF-SGLlktpAFRRAESEALDraatWLERVGLLEHANRQAG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 145 QLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHD 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-204 |
1.16e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.91 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLdVPDEGSYHLDNVDVFKLSDNKLSEIRnkkiGFIFQQFNLLPKLSA 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELPLiYAGLSVSAREKAAIECLEKVGLLEK-RRNLpTQLSGGQQQRVAIARAL-----AGKP--QILLADEPTGAL 176
Cdd:COG4138 87 FQYLALHQ-PAGASSEAVEQLLAQLAEALGLEDKlSRPL-TQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*...
gi 489825110 177 DSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHD 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-204 |
1.45e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.31 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYT-------LGG----------ETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLdVPDEGSYH 67
Cdd:COG4586 2 IEVENLSKTYRvyekepgLKGalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 68 LDNVDVFKLsdnklsEIRN-KKIGFIFQQFN-LLPKLSAFENVEL-PLIYaglSVSARE-----KAAIECLEKVGLLEKr 139
Cdd:COG4586 81 VLGYVPFKR------RKEFaRRIGVVFGQRSqLWWDLPAIDSFRLlKAIY---RIPDAEykkrlDELVELLDLGELLDT- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 140 rnlPT-QLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMIT-HD 204
Cdd:COG4586 151 ---PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTsHD 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-210 |
1.45e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 94.25 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 16 TLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI--GCLDVPDEGSyhldnvdvFKLSDNKLSEirnkkigfif 93
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGC--------VDVPDNQFGR---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 94 qqfnllpklsafenvELPLIYAgLSVSAREKAAIECLEKVGL----LEKRRnlPTQLSGGQQQRVAIARALAGKPQILLA 169
Cdd:COG2401 99 ---------------EASLIDA-IGRKGDFKDAVELLNAVGLsdavLWLRR--FKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489825110 170 DEPTGALDSKTGKEVMGILQELNR-AGNTIVMITHDPTIASY 210
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARrAGITLVVATHHYDVIDD 202
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
1.55e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTLGGEtfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfKLSDNK 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRnKKIGFIFQQ-FNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLlEKRRNLPTQ-LSGGQQQRVAIAR 158
Cdd:PRK13636 77 LMKLR-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD-PTIASYGTRSIRIQDGK 221
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-203 |
1.76e-23 |
|
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: 97.97 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTlmnmIGCL-----DVpDEGSYHLDNVDvfkLSDNKLSEIRnKKIGFIFQQ---F 96
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKST----LARLlfrfyDV-TSGRILIDGQD---IRDVTQASLR-AAIGIVPQDtvlF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 97 NLlpklSAFENVelplIYAGLSVSARE-----KAA-----IECLEK-----VGllEkrRNLptQLSGGQQQRVAIARALA 161
Cdd:COG5265 445 ND----TIAYNI----AYGRPDASEEEveaaaRAAqihdfIESLPDgydtrVG--E--RGL--KLSGGEKQRVAIARTLL 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 162 GKPQILLADEPTGALDSKTGKEvmgILQELNRA--GNTIVMITH 203
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERA---IQAALREVarGRTTLVIAH 551
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-203 |
2.36e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.78 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlGGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCL-DVpDEGSYHLDNVDvfkLSDNKLSEI 84
Cdd:PRK11176 342 IEFRNVTFTYP-GKEV-PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFyDI-DEGEILLDGHD---LRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNkKIGFIFQQFNLLPKLSAfENVElpliYAGLSVSAREK--AAIECLEKVGLLEKRRN-LPT-------QLSGGQQQRV 154
Cdd:PRK11176 416 RN-QVALVSQNVHLFNDTIA-NNIA----YARTEQYSREQieEAARMAYAMDFINKMDNgLDTvigengvLLSGGQRQRI 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL--NRagnTIVMITH 203
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAH 537
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-227 |
2.52e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.77 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTLGGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVdvfKLSDNKLSEI 84
Cdd:PRK13642 4 ILEVENLVFKYEKESDV-NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQ-FNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGK 163
Cdd:PRK13642 80 R-RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 164 PQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHDPTIASYGTRSIRIQDGKLFHEEA 227
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-205 |
2.62e-23 |
|
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: 92.81 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 28 VTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdNKLSEIRNKKIGFIFQQFNLLPKLSAFEN 107
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 108 VELpliYAGLSVSAReKAAIECLEKVGLLEkRRNLPT-QLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMG 186
Cdd:TIGR01189 94 LHF---WAAIHGGAQ-RTIEDALAAVGLTG-FEDLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*....
gi 489825110 187 ILQELNRAGNTIVMITHDP 205
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTHQD 187
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
24-173 |
4.60e-23 |
|
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: 92.97 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTLMN-MIGCLDVPDeGSYHLDNVDVFKLSdnklSEIRNKK-IGFIFQQFNLLPK 101
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLPVKS-GSIRLDGEDITKLP----PHERARAgIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 102 LSAFENVELpliyaGLSVSAREKAAI--ECLEKVGLLEKRRNLPT-QLSGGQQQRVAIARALAGKPQILLADEPT 173
Cdd:TIGR03410 90 LTVEENLLT-----GLAALPRRSRKIpdEIYELFPVLKEMLGRRGgDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-203 |
5.73e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIRnKKIGFIFQQFNLLPKlS 103
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENVEL---PLIYAGLSVSAREKAAIECLEK--------VGllEKRRnlptQLSGGQQQRVAIARALAGKPQILLADEP 172
Cdd:PRK13657 425 IEDNIRVgrpDATDEEMRAAAERAQAHDFIERkpdgydtvVG--ERGR----QLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190
....*....|....*....|....*....|.
gi 489825110 173 TGALDSKTGKEVMGILQELnRAGNTIVMITH 203
Cdd:PRK13657 499 TSALDVETEAKVKAALDEL-MKGRTTFIIAH 528
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-210 |
1.68e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKlsdNKLSEI 84
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RnKKIGFIFQQfnllPKLSAF-----ENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARA 159
Cdd:PRK13652 77 R-KFVGLVFQN----PDDQIFsptveQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQEL-NRAGNTIVMITHD----PTIASY 210
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQldlvPEMADY 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-222 |
3.51e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDvPDEGSYHL-DNVdvfklsd 78
Cdd:COG0488 311 LGKKVLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELE-PDSGTVKLgETV------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 nklseirnkKIGFIFQQFNLL-PKLSAFENVelpliyAGLSVSAREKAAIECLEKVGLLEKRRNLPT-QLSGGQQQRVAI 156
Cdd:COG0488 379 ---------KIGYFDQHQEELdPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVgVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTgkevmgiLQELNRA-----GnTIVMITHDP----TIAsygTRSIRIQDGKL 222
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIET-------LEALEEAlddfpG-TVLLVSHDRyfldRVA---TRILEFEDGGV 507
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-221 |
3.67e-22 |
|
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: 89.84 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGG-ETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMN-MIGCLDVPdEGSYHLdnvdvfklsdnklse 83
Cdd:cd03250 1 ISVEDASFTWDSGEqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSV--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 irNKKIGFIFQQfnllpklsAF-------ENvelplIYAGLSV-SAREKAAIE--CLEK------------VGllEKRRN 141
Cdd:cd03250 65 --PGSIAYVSQE--------PWiqngtirEN-----ILFGKPFdEERYEKVIKacALEPdleilpdgdlteIG--EKGIN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 142 LptqlSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVM--GILQELnRAGNTIVMITHDPTIASYGTRSIRIQD 219
Cdd:cd03250 128 L----SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLL-LNNKTRILVTHQLQLLPHADQIVVLDN 202
|
..
gi 489825110 220 GK 221
Cdd:cd03250 203 GR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-222 |
3.85e-22 |
|
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: 90.16 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLsdnKLSEIR 85
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NkKIGFIFQQFNLL-----PKLSAFENVELPLIYAGLSVSarekaaieclekvgllEKRRNlptqLSGGQQQRVAIARAL 160
Cdd:cd03369 82 S-SLTIIPQDPTLFsgtirSNLDPFDEYSDEEIYGALRVS----------------EGGLN----LSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHD-PTIASYgTRSIRIQDGKL 222
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRlRTIIDY-DKILVMDAGEV 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-203 |
4.18e-22 |
|
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: 93.74 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYtlGGetFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgCLDVPdEGSYhlDNVDVFKLSDNKLSEI 84
Cdd:TIGR02633 1 LLEMKGIVKTF--GG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYP-HGTW--DGEIYWSGSPLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RN---KKIGFIFQQFNLLPKLSAFENV----ELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPT-QLSGGQQQRVAI 156
Cdd:TIGR02633 73 RDterAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-204 |
5.12e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 14 TYTLGGET---FKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNvdvFKLSDN--KLSEIRN-- 86
Cdd:PRK13645 13 SYTYAKKTpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD---YAIPANlkKIKEVKRlr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 87 KKIGFIFQqfnlLPKLSAF-ENVELPLIYAGLSVSAREKAAI----ECLEKVGLLEKR-RNLPTQLSGGQQQRVAIARAL 160
Cdd:PRK13645 90 KEIGLVFQ----FPEYQLFqETIEKDIAFGPVNLGENKQEAYkkvpELLKLVQLPEDYvKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHN 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-227 |
1.13e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.05 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 16 TLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSeirnKKIGFIFQQ 95
Cdd:PRK10253 14 TLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 96 FNLLPKLSAFENVELPLiYAGLSVSAR-----EKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLAD 170
Cdd:PRK10253 90 ATTPGDITVQELVARGR-YPHQPLFTRwrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 171 EPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIA-SYGTRSIRIQDGKLFHEEA 227
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQAcRYASHLIALREGKIVAQGA 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-206 |
1.88e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.03 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPD---EGSYHLDNVDVfklsdnKLSEIRnKKIGFIFQQFNLLPK 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI------DAKEMR-AISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 102 LSAFENvelpLIYA-----GLSVSAREKAAI--ECLEKVGLLeKRRNLPTQ-------LSGGQQQRVAIARALAGKPQIL 167
Cdd:TIGR00955 114 LTVREH----LMFQahlrmPRRVTKKEKRERvdEVLQALGLR-KCANTRIGvpgrvkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 489825110 168 LADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT 206
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPS 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-204 |
2.09e-21 |
|
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: 86.35 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDnvdvfklsdnklseiR 85
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIfqqfnllpklsafenvelpliyaglsvsarekaaieclekvgllekrrnlpTQLSGGQQQRVAIARALAGKPQ 165
Cdd:cd03221 62 TVKIGYF---------------------------------------------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*....
gi 489825110 166 ILLADEPTGALDSKTgkeVMGILQELNRAGNTIVMITHD 204
Cdd:cd03221 91 LLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHD 126
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-204 |
2.39e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 28 VTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLdVPDEGSYHLDNVDVFKLSDNKLSEIRnkkiGFIFQQFNLLPKLSAFEN 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 108 VELPLiYAGLSVSAREKAAIECLEKVGLLEK-RRNLpTQLSGGQQQRVAIARAL-----AGKP--QILLADEPTGALDSK 179
Cdd:PRK03695 90 LTLHQ-PDKTRTEAVASALNEVAEALGLDDKlGRSV-NQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*
gi 489825110 180 TGKEVMGILQELNRAGNTIVMITHD 204
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-204 |
4.92e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.07 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKS----TLMNMI---GCLDVPDEGSYHLDNVDVFKL---S 77
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRQVIELseqS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 78 DNKLSEIRNKKIGFIFQQ--FNLLPKLSAFENV-ELPLIYAGLSvsaREKAAIEC---LEKVGLLEKRRNL---PTQLSG 148
Cdd:PRK10261 95 AAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIaESIRLHQGAS---REEAMVEAkrmLDQVRIPEAQTILsryPHQLSG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 149 GQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNT-IVMITHD 204
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHD 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-217 |
1.20e-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: 86.01 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 28 VTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRnkkigFIFQQFNLLPKLSAFEN 107
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL-----YLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 108 veLPLIYAGLSVSAREKAaiecLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGI 187
Cdd:cd03231 94 --LRFWHADHSDEQVEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180 190
....*....|....*....|....*....|.
gi 489825110 188 LQELNRAGNTIVMITHDP-TIASYGTRSIRI 217
Cdd:cd03231 168 MAGHCARGGMVVLTTHQDlGLSEAGARELDL 198
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-209 |
1.34e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 22 FKALDDVTFTVEQGEFLSIVGPSGSGKSTLM-------NMIGCLDVPDEGSYHLDNVDVfklSDNKLSEIRnKKIGFIFQ 94
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVEGKVTFHGKNLYA---PDVDPVEVR-RRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 95 QFNLLPKlSAFENVEL-PLI--YAGLSVSAREKAaiecLEKVGLLE----KRRNLPTQLSGGQQQRVAIARALAGKPQIL 167
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYgARIngYKGDMDELVERS----LRQAALWDevkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489825110 168 LADEPTGALDSKTGKEVMGILQELNRAgNTIVMITHDPTIAS 209
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAA 214
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-204 |
3.94e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.52 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKpLIDMKNLTKtytlggETFKAL-DDVTFTVEQGEFLSIVGPSGSGKStlMNMIGCLDV-P-----DEGSYHLDNVDV 73
Cdd:PRK10418 1 MPQ-QIELRNIAL------QAAQPLvHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGIlPagvrqTAGRVLLDGKPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 74 fklsdnKLSEIRNKKIGFIFQQfnllPKlSAFENVELPLIYA-----GLSVSAREKAAIECLEKVGLLEKRRNL---PTQ 145
Cdd:PRK10418 72 ------APCALRGRKIATIMQN----PR-SAFNPLHTMHTHAretclALGKPADDATLTAALEAVGLENAARVLklyPFE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHD 204
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHD 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-203 |
5.59e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.85 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLseiR 85
Cdd:PRK10790 341 IDIDNVSFAY---RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIgfIFQQFNLLPKLSAFENVELpliyaGLSVSarEKAAIECLEKVGLLEKRRNLP-----------TQLSGGQQQRV 154
Cdd:PRK10790 415 QGVA--MVQQDPVVLADTFLANVTL-----GRDIS--EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITH 203
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-REHTTLVVIAH 533
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-203 |
9.58e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 19 GETF---KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDV-FKLSDNKLseirNKKIGFIFQ 94
Cdd:PRK11288 11 GKTFpgvKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrFASTTAAL----AAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 95 QFNLLPKLSAFENV---ELPLIYAGLSVSAREKAAIECLEKVGL-LEKRRNLpTQLSGGQQQRVAIARALAGKPQILLAD 170
Cdd:PRK11288 87 ELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVdIDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190
....*....|....*....|....*....|...
gi 489825110 171 EPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-217 |
1.27e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSEirnkKIGFIFQQFNLLPKLSA 104
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAE----ACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELpliYAGLsVSAREKAAIECLEKVGL--LEkrrNLPTQ-LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTG 181
Cdd:PRK13539 91 AENLEF---WAAF-LGGEELDIAAALEAVGLapLA---HLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 489825110 182 KEVMGILQELNRAGNTIVMITHDPtIASYGTRSIRI 217
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAATHIP-LGLPGARELDL 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-222 |
2.05e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 83.29 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYTLGGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfKLSDNKLs 82
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 eiRNKKIGFIFQQFNLLPKlSAFENVE--LPLIYAGLSVSAREKAA----IECLEKvGLLEKRRNLPTQLSGGQQQRVAI 156
Cdd:cd03248 86 --LHSKVSLVGQEPVLFAR-SLQDNIAygLQSCSFECVKEAAQKAHahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAgNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-223 |
2.69e-19 |
|
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: 86.22 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGEtfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsDNKLSE 83
Cdd:TIGR01257 927 PGVCVKNLVKIFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDA 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRnKKIGFIFQQFNLLPKLSAFENVelpLIYAGLSVSAREKAAIEC---LEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:TIGR01257 1001 VR-QSLGMCPQHNILFHHLTVAEHI---LFYAQLKGRSWEEAQLEMeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELnRAGNTIVMITHDPTIAS-YGTRSIRIQDGKLF 223
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-202 |
2.95e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTytlggetfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfKLSDNK-- 80
Cdd:COG1129 254 EVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPRda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 -------LSEIRnKKIGfifqqfnLLPKLSAFENVELPLI--YAGLSV--SAREKAAIEclEKVGLLEKRRNLPTQ---- 145
Cdd:COG1129 325 iragiayVPEDR-KGEG-------LVLDLSIRENITLASLdrLSRGGLldRRRERALAE--EYIKRLRIKTPSPEQpvgn 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPT-----GAldsKTgkEVMGILQELNRAGNTIVMIT 202
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTrgidvGA---KA--EIYRLIRELAAEGKAVIVIS 451
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-229 |
3.82e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 16 TLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNV-----DVFKLSDnkLSEIRnKKIG 90
Cdd:PRK14271 28 TLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrSIFNYRD--VLEFR-RRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 91 FIFQQFNLLPkLSAFENVeLPLIYAGLSVSARE--KAAIECLEKVGLLE----KRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNV-LAGVRAHKLVPRKEfrGVAQARLTEVGLWDavkdRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQEL-NRAgnTIVMITHD-PTIASYGTRSIRIQDGKLFHEEATQ 229
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLaDRL--TVIIVTHNlAQAARISDRAALFFDGRLVEEGPTE 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-204 |
3.89e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.39 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTlGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgcldvpdEGSYHLDNVDVFKLSDNK 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWR-NGHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKAL-------MGFVRLASGKISILGQPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKKIGFIFQQFNL---LPKLsaFENVELPLIYAGLSVSAREKA-----AIECLEKVGLLEKRRNLPTQLSGGQQQ 152
Cdd:PRK15056 72 RQALQKNLVAYVPQSEEVdwsFPVL--VEDVVMMGRYGHMGWLRRAKKrdrqiVTAALARVDMVEFRHRQIGELSGGQKK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 153 RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-203 |
1.14e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfKLSDNKLS 82
Cdd:PRK10762 2 QALLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EirNKKIGFIFQQFNLLPKLSAFENV----ELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIAR 158
Cdd:PRK10762 77 Q--EAGIGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489825110 159 ALAGKPQILLADEPTGAL-DSKTgKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTET-ESLFRVIRELKSQGRGIVYISH 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-204 |
2.94e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTktyTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLS 82
Cdd:COG3845 255 EVVLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKKIGFI---FQQFNLLPKLSAFENVELPLIYAG-------LSVSAREKAAIECLEKVGLLEKRRNLPT-QLSGGQQ 151
Cdd:COG3845 329 ERRRLGVAYIpedRLGRGLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQ 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 152 QRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED 461
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-206 |
3.06e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 83.01 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGcldvpdeGSYHLDNVDVFKLSDN-KLSEIRNKKIGFIFQQFNLLPKLS 103
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQGNNFTGTILANNrKPTKQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENvelpLIYAGL-----SVSAREK--AAIECLEKVGLLEKRRNLPTQ-----LSGGQQQRVAIARALAGKPQILLADE 171
Cdd:PLN03211 157 VRET----LVFCSLlrlpkSLTKQEKilVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|....*
gi 489825110 172 PTGALDSKTGKEVMGILQELNRAGNTIVMITHDPT 206
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPS 267
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-203 |
1.02e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.25 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 2 PKPLIDMKNLTKTYTlGGETFKALDdvtFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKL 81
Cdd:PRK15439 8 APPLLCARSISKQYS-GVEVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 SEIrnkKIGFIFQQFNLLPKLSAFENvelplIYAGLSVSAREKAAIEclEKVGLLEKRRNLPTQ---LSGGQQQRVAIAR 158
Cdd:PRK15439 84 HQL---GIYLVPQEPLLFPNLSVKEN-----ILFGLPKRQASMQKMK--QLLAALGCQLDLDSSagsLEVADRQIVEILR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 159 ALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-219 |
1.44e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.81 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI--------GCLDVPDEGsyhldnvDVFklsdnklseirnkkigFIFQQf 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMPEGE-------DLL----------------FLPQR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 97 nllpklsafenvelPLIYAGlsvSAREkAAIECLEKVgllekrrnlptqLSGGQQQRVAIARALAGKPQILLADEPTGAL 176
Cdd:cd03223 73 --------------PYLPLG---TLRE-QLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489825110 177 DSKTGKEVMGILQELnraGNTIVMITHDPTIASYGTRSIRIQD 219
Cdd:cd03223 123 DEESEDRLYQLLKEL---GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-204 |
1.79e-17 |
|
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: 80.75 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYTLGGETFKaldDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhldnvdvfklsdnklsEIR-- 85
Cdd:TIGR03719 7 MNRVSKVVPPKKEILK---DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------------------EARpq 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 -NKKIGFIFQQFNLLPKLSAFENVELPL------------IYAGLS-------VSAREKAAI-ECLEKVGLLEKRRNL-- 142
Cdd:TIGR03719 66 pGIKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneISAKYAepdadfdKLAAEQAELqEIIDAADAWDLDSQLei 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 143 -------P------TQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTgkeVMGILQELNRAGNTIVMITHD 204
Cdd:TIGR03719 146 amdalrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHD 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-204 |
3.06e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhldnvdvfklsdnKLSE 83
Cdd:PRK09544 3 SLVSLENVSVSF---GQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG---------------VIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRNKKIGFIFQQFNLLPKLsafenvelPLI---YAGLSVSAREKAAIECLEKVG---LLEKrrnlPTQ-LSGGQQQRVAI 156
Cdd:PRK09544 64 NGKLRIGYVPQKLYLDTTL--------PLTvnrFLRLRPGTKKEDILPALKRVQaghLIDA----PMQkLSGGETQRVLL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 157 ARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGN-TIVMITHD 204
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHD 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-209 |
4.40e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 14 TYTLGGETFKA-----LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnklSEIRNKK 88
Cdd:PRK10575 11 TFALRNVSFRVpgrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS----SKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 89 IGFIFQQfnlLPKLSAFENVELPLI----YAG----LSVSAREKAAiECLEKVGLLEKRRNLPTQLSGGQQQRVAIARAL 160
Cdd:PRK10575 87 VAYLPQQ---LPAAEGMTVRELVAIgrypWHGalgrFGAADREKVE-EAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEVMGILQELNRA-GNTIVMITHDPTIAS 209
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAA 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-217 |
1.77e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCL-----------------DVPDEGSYH- 67
Cdd:PTZ00265 1166 IEIMDVNFRY-ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtnDMTNEQDYQg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 68 -------LDNVDVFKLS--------------------------DNKLSEIRNkkIGFIFQQFNLLPKLSAFENVELpliy 114
Cdd:PTZ00265 1245 deeqnvgMKNVNEFSLTkeggsgedstvfknsgkilldgvdicDYNLKDLRN--LFSIVSQEPMLFNMSIYENIKF---- 1318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 115 aglsvsAREKAAIECLEKV----GLLEKRRNLPTQ-----------LSGGQQQRVAIARALAGKPQILLADEPTGALDSK 179
Cdd:PTZ00265 1319 ------GKEDATREDVKRAckfaAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270
....*....|....*....|....*....|....*....
gi 489825110 180 TGKEVMGILQEL-NRAGNTIVMITHdpTIASYgTRSIRI 217
Cdd:PTZ00265 1393 SEKLIEKTIVDIkDKADKTIITIAH--RIASI-KRSDKI 1428
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-230 |
2.37e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNK 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 LSEIRNKKIGFIFQQFNLLPKLSAFENVELPLIYAglsvsaREKAAIECLEKV-----GLLEKRRNLPTQLSGGQQQRVA 155
Cdd:PRK11614 74 TAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFA------ERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA-SYGTRSIRIQDGKLFHEEATQA 230
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQAlKLADRGYVLENGHVVLEDTGDA 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-208 |
3.29e-16 |
|
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: 73.82 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNmigCLDVPDEGSYHLDNVdvfKLSDNKLSEIRNKK 88
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLD---VLAGRKTAGVITGEI---LINGRPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 89 IGFIFQQFNLLPKLSAFENVELPLIYAGLSVSarekaaieclekvgllekrrnlptqlsggQQQRVAIARALAGKPQILL 168
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALLRGLSVE-----------------------------QRKRLTIGVELAAKPSILF 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 169 ADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA 208
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSAS 171
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-203 |
1.67e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDV-PDEGSYHLDNVDVFKLSdnklSEIRNKK-IGFIFQQ------ 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHPKYeVTSGSILLDGEDILELS----PDERARAgIFLAFQYpveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 96 ---FNLL---------PKLSAFENVELpliyaglsvsAREKAaieclEKVGLLEK--RRNLPTQLSGGQQQRVAIARALA 161
Cdd:COG0396 92 vsvSNFLrtalnarrgEELSAREFLKL----------LKEKM-----KELGLDEDflDRYVNEGFSGGEKKRNEILQMLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-221 |
1.82e-15 |
|
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: 73.17 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 31 TVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYH-----LDNVDVFKLSD--NKLSEIRNKKIGFIF--QQFNLLPK 101
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwDEILDEFRGSElqNYFTKLLEGDVKVIVkpQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 102 lsAFENVELPLIYAGLSVSAREKAaIECLEKVGLLEkrRNLpTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTG 181
Cdd:cd03236 102 --AVKGKVGELLKKKDERGKLDEL-VDQLELRHVLD--RNI-DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489825110 182 KEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGK 221
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-204 |
2.31e-15 |
|
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: 74.59 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSY------HLDNVDVFK--LS 77
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeigetvKLAYVDQSRdaLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 78 DNK---------LSEIRNKKIgfifqQFNLLPKLSAFenvelpliyaGLSVSAREKaaiecleKVGllekrrnlptQLSG 148
Cdd:TIGR03719 399 PNKtvweeisggLDIIKLGKR-----EIPSRAYVGRF----------NFKGSDQQK-------KVG----------QLSG 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 149 GQQQRVAIARALAGKPQILLADEPTGALDSKTgkevMGILQE--LNRAGNTIVmITHD 204
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVET----LRALEEalLNFAGCAVV-ISHD 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-222 |
6.42e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTktytlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnKLS 82
Cdd:PRK09700 263 ETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRnKKIGFIFQ---QFNLLPKLSAFENVEL-----------------PLIYAGLSVSAREKAAIECLEKvgllekRRNL 142
Cdd:PRK09700 335 AVK-KGMAYITEsrrDNGFFPNFSIAQNMAIsrslkdggykgamglfhEVDEQRTAENQRELLALKCHSV------NQNI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 143 pTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGK 221
Cdd:PRK09700 408 -TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGR 486
|
.
gi 489825110 222 L 222
Cdd:PRK09700 487 L 487
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-229 |
8.47e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDVpDEGSYHLDNVDVFKLS-----DNKL---SEIRnKKIGfifqq 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSpqdglANGIvyiSEDR-KRDG----- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 96 fnLLPKLSAFENVELP----LIYAGLSVS-AREKAAieclekVGLLEKRRNLPT--------QLSGGQQQRVAIARALAG 162
Cdd:PRK10762 341 --LVLGMSVKENMSLTalryFSRAGGSLKhADEQQA------VSDFIRLFNIKTpsmeqaigLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 163 KPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGKL----FHEEATQ 229
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRIsgefTREQATQ 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-222 |
9.03e-15 |
|
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: 72.55 E-value: 9.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDVPDEGSYHLDN--VDVfklsDNKLSEIRnKKIGFI---FQQF 96
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGkpVDI----RNPAQAIR-AGIAMVpedRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 97 NLLPKLSAFENVELPLI--YAGLSV---SAREKAAIECLEKVGLLEKRRNLP-TQLSGGQQQRVAIARALAGKPQILLAD 170
Cdd:TIGR02633 349 GIVPILGVGKNITLSVLksFCFKMRidaAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 171 EPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGKL 222
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-210 |
1.15e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 69.86 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDV-PDEGSYHLDNVDVFKLSDNklsEIRNKKIGFIFQqfnllpkl 102
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKYeVTEGEILFKGEDITDLPPE---ERARLGIFLAFQ-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 103 safENVELPliyaGLSVSArekaaieclekvgLLekrRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGK 182
Cdd:cd03217 85 ---YPPEIP----GVKNAD-------------FL---RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180
....*....|....*....|....*...
gi 489825110 183 EVMGILQELNRAGNTIVMITHDPTIASY 210
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-229 |
3.50e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GCLDVPDEGSYHLDNVDVfKLSdNKLSEIRN---------KKIGfi 92
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPV-KIR-NPQQAIAQgiamvpedrKRDG-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 93 fqqfnLLPKLSAFENVELPLI--YAGLSV--SAREKAAIEclEKVGLLEKRRNLP----TQLSGGQQQRVAIARALAGKP 164
Cdd:PRK13549 352 -----IVPVMGVGKNITLAALdrFTGGSRidDAAELKTIL--ESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGKL----FHEEATQ 229
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLkgdlINHNLTQ 494
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-207 |
4.50e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNmigCL-DVPDEGSYHLDNVDVfklSDNKLSEIRN 86
Cdd:TIGR00956 762 WRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLN---VLaERVTTGVITGGDRLV---NGRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 87 KKIGFIFQQFNLLPKLSAFENvelpLIYAGL-----SVSAREK-----AAIECLEKVGLLEKRRNLPTQ-LSGGQQQRVA 155
Cdd:TIGR00956 836 RSIGYVQQQDLHLPTSTVRES----LRFSAYlrqpkSVSKSEKmeyveEVIKLLEMESYADAVVGVPGEgLNVEQRKRLT 911
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489825110 156 IARALAGKPQILL-ADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTI 207
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSA 964
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
6-222 |
5.54e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.07 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTL----------------GGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhld 69
Cdd:PRK13546 5 VNIKNVTKEYRIyrtnkermkdalipkhKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 70 NVDvfklsdnklseiRNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGG 149
Cdd:PRK13546 80 KVD------------RNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825110 150 QQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGKL 222
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKL 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-201 |
6.38e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 27 DVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDnvDVFKLSDNKLSEIRNKkIGFIFQ------------ 94
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSK-IGVVSQdpllfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 95 -QFNL-----LPKLSAFENVELPLIYAGLSV--SAREKAA------IECLEKVGLLEKRRN------------------- 141
Cdd:PTZ00265 480 iKYSLyslkdLEALSNYYNEDGNDSQENKNKrnSCRAKCAgdlndmSNTTDSNELIEMRKNyqtikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 142 -----LP-----------TQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMI 201
Cdd:PTZ00265 560 dfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-222 |
7.83e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSEIR 85
Cdd:PRK10522 323 LELRNVTFAY--QDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPKLSAFENVElpliyaglsvsAREKAAIECLEKVGLLEK-----RRNLPTQLSGGQQQRVAIARAL 160
Cdd:PRK10522 397 -KLFSAVFTDFHLFDQLLGPEGKP-----------ANPALVEKWLERLKMAHKleledGRISNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 161 AGKPQILLADEPTGALDSKTGKEV-MGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGKL 222
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-204 |
9.84e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYtlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhldnvdvfklsDNKLSEirNK 87
Cdd:PRK11819 9 MNRVSKVV---PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAP--GI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGFIFQQFNLLPKLSAFENVELPL------------IYAGLsvsAREKAAIECL-EKVGLLEK-----------RR--- 140
Cdd:PRK11819 71 KVGYLPQEPQLDPEKTVRENVEEGVaevkaaldrfneIYAAY---AEPDADFDALaAEQGELQEiidaadawdldSQlei 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 141 -----NLP------TQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTgkeVMGILQELNRAGNTIVMITHD 204
Cdd:PRK11819 148 amdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPGTVVAVTHD 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-173 |
1.15e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlgGEtFKALDDVTFTVEQGE---FLsivGPSGSGKSTLMNMI-GCLDvPDEGSYHL-----DNVDVf 74
Cdd:NF033858 265 PAIEARGLTMRF---GD-FTAVDHVSFRIRRGEifgFL---GSNGCGKSTTMKMLtGLLP-ASEGEAWLfgqpvDAGDI- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 75 klsdnklsEIRnKKIGFIFQQFNLLPKLSAFENVELpliYAGL-SVSARE-KAAI-ECLEKVGLLEKRRNLPTQLSGGQQ 151
Cdd:NF033858 336 --------ATR-RRVGYMSQAFSLYGELTVRQNLEL---HARLfHLPAAEiAARVaEMLERFDLADVADALPDSLPLGIR 403
|
170 180
....*....|....*....|..
gi 489825110 152 QRVAIARALAGKPQILLADEPT 173
Cdd:NF033858 404 QRLSLAVAVIHKPELLILDEPT 425
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-177 |
1.51e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.89 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI-GclDVPDEGSYHLDNVDVFKLSDNKLS 82
Cdd:PRK10938 259 PRIVLNNGVVSY---NDR-PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItG--DHPQGYSNDLTLFGRRRGSGETIW 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRnKKIGFIFQQFNLLPKLSA-FENVELP------LIYAGLSvSAREKAAIECLEKVGLLEKRRNLPTQ-LSGGQQQRV 154
Cdd:PRK10938 333 DIK-KHIGYVSSSLHLDYRVSTsVRNVILSgffdsiGIYQAVS-DRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLA 410
|
170 180
....*....|....*....|...
gi 489825110 155 AIARALAGKPQILLADEPTGALD 177
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-203 |
1.52e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 13 KTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIG-CLDVPD-EGSYHldnvdVFKLSDNKLSEIRNK--- 87
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDVSEgDIRFH-----DIPLTKLQLDSWRSRlav 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 --KIGFIFQQfnllpklSAFENVELpliyaglsvsAREKAAIECLEKVGLL----EKRRNLP----TQ-------LSGGQ 150
Cdd:PRK10789 394 vsQTPFLFSD-------TVANNIAL----------GRPDATQQEIEHVARLasvhDDILRLPqgydTEvgergvmLSGGQ 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 151 QQRVAIARALAGKPQILLADEPTGALDSKTGKEvmgILQELN--RAGNTIVMITH 203
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQ---ILHNLRqwGEGRTVIISAH 508
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-204 |
1.00e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHL-DNVdvfklsdnklsei 84
Cdd:PRK11819 325 IEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETV------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 rnkKIGFIFQQF-NLLPKLSAFENV--ELPLIYAG-LSVSAR-------------EKaaiecleKVGllekrrnlptQLS 147
Cdd:PRK11819 388 ---KLAYVDQSRdALDPNKTVWEEIsgGLDIIKVGnREIPSRayvgrfnfkggdqQK-------KVG----------VLS 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 148 GGQQQRVAIARALAGKPQILLADEPTGALDSKTgkevMGILQE--LNRAGNTIVmITHD 204
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET----LRALEEalLEFPGCAVV-ISHD 501
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-222 |
2.09e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.68 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTyTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSyhldnVDVfklsdnkls 82
Cdd:PRK13545 19 KPFDKLKDLFFR-SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-----VDI--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 eirNKKIGFIFQQFNLLPKLSAFENVELPLIYAGLSVSAREKAAIECLEkVGLLEKRRNLPTQ-LSGGQQQRVAIARALA 161
Cdd:PRK13545 84 ---KGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIE-FADIGKFIYQPVKtYSSGMKSRLGFAISVH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 162 GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGKL 222
Cdd:PRK13545 160 INPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSlSQVKSFCTKALWLHYGQV 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-222 |
2.20e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGClDVP-DEGSYHLD-NVDVFKLSDNKLSEIRN----------KKIGFI 92
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYEqDLIVARLQQDPPRNVEGtvydfvaegiEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 93 FQQFNLLPKLSAFENVELPLiyaglsvsaREKAAI-ECLEKVGL--LEKRRN-------LP-----TQLSGGQQQRVAIA 157
Cdd:PRK11147 98 LKRYHDISHLVETDPSEKNL---------NELAKLqEQLDHHNLwqLENRINevlaqlgLDpdaalSSLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 158 RALAGKPQILLADEPTGALDSKTGKEVMGILQELNragNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---GSIIFISHDRSfIRNMATRIVDLDRGKL 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-204 |
3.15e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 40 IVGPSGSGKSTL-MNMIGCLDvPDEGSYhLDNVDVFKLSDNKLSEIRnKKIGFIFQQfnllPKLSAF-----ENVELPLI 113
Cdd:PRK13638 32 LVGANGCGKSTLfMNLSGLLR-PQKGAV-LWQGKPLDYSKRGLLALR-QQVATVFQD----PEQQIFytdidSDIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 114 YAGLsvsAREKAAIECLEKVGLLEKR--RNLPTQ-LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQE 190
Cdd:PRK13638 105 NLGV---PEAEITRRVDEALTLVDAQhfRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR 181
|
170
....*....|....
gi 489825110 191 LNRAGNTIVMITHD 204
Cdd:PRK13638 182 IVAQGNHVIISSHD 195
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-202 |
4.11e-12 |
|
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: 63.05 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNmIGCLDVPD----EGSYHLDNVDVfklsdNKLSEI 84
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLK-ALANRTEGnvsvEGDIHYNGIPY-----KEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNKKIGFIFQQFNLLPKLSAFENVElpliyaglsvsarekAAIEClekvglleKRRNLPTQLSGGQQQRVAIARALAGKP 164
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLD---------------FALRC--------KGNEFVRGISGGERKRVSIAEALVSRA 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 489825110 165 QILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMIT 202
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-178 |
4.53e-12 |
|
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: 63.58 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEF-----LSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsDNKLSEIRNKKIGFIfQQFn 97
Cdd:cd03237 8 KTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV----SYKPQYIKADYEGTV-RDL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 98 LLPKLSAFenvelpliyagLSVSAREKAAIECLEKVGLLEkrRNLPTqLSGGQQQRVAIARALAGKPQILLADEPTGALD 177
Cdd:cd03237 82 LSSITKDF-----------YTHPYFKTEIAKPLQIEQILD--REVPE-LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
.
gi 489825110 178 S 178
Cdd:cd03237 148 V 148
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-220 |
4.55e-12 |
|
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: 63.12 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 9 KNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKST-LMNMIGCLDVPdEGSYHLDNVDVFKLSDNKLSEIRNK 87
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMQTL-EGKVHWSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGFIFQQFNLLPKlsafeNVELPLIYAGLSVSAREKAAIECLE---KVGLL---------EKRRNlptqLSGGQQQRVA 155
Cdd:cd03290 80 SVAYAAQKPWLLNA-----TVEENITFGSPFNKQRYKAVTDACSlqpDIDLLpfgdqteigERGIN----LSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVM--GILQELNRAGNTIVMITHDPTIASYGTRSIRIQDG 220
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-230 |
1.19e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.28 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTY--TLGGETFkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklSDNKLSE 83
Cdd:COG4615 328 LELRGVTYRYpgEDGDEGF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRNKkigF--IFQQFNLLPKLSAFENVELPliyaglsvsarEKAAiECLEKVGL-----LEKRRNLPTQLSGGQQQRVAI 156
Cdd:COG4615 404 YRQL---FsaVFSDFHLFDRLLGLDGEADP-----------ARAR-ELLERLELdhkvsVEDGRFSTTDLSQGQRKRLAL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 157 ARALAGKPQILLADE------PtgaldskTGKEV--MGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGKLFHEEAT 228
Cdd:COG4615 469 LVALLEDRPILVFDEwaadqdP-------EFRRVfyTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGP 541
|
..
gi 489825110 229 QA 230
Cdd:COG4615 542 AA 543
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-203 |
1.34e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSyhldnVDVFKLSDNKLSEIRNKKIGFIFQQFNLLPKLSA 104
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE-----ILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELPLIYAGLSVSAREKAAIECLEKvgLLEKRRNLptqLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEV 184
Cdd:PRK13540 92 RENCLYDIHFSPGAVGITELCRLFSLEH--LIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170
....*....|....*....
gi 489825110 185 MGILQELNRAGNTIVMITH 203
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-203 |
1.34e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.88 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLTKTYTlgGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgcldvpdEGSYHLDNVDVFKLSDNKLSEI 84
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGDATVAGKSILTNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 RNkkigfIFQQFNLLPKLSAFENV----ELPLIYA---GLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIA 157
Cdd:TIGR01257 2008 SD-----VHQNMGYCPQFDAIDDLltgrEHLYLYArlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489825110 158 RALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-203 |
1.56e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 8 MKNLTKTYTlggeTFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDV-FKLSDNKLseirN 86
Cdd:PRK10982 1 MSNISKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEAL----E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 87 KKIGFIFQQFNLLPKLSAFENVEL---PLiyAGLSVSA----REKAAIecLEKVGLLEKRRNLPTQLSGGQQQRVAIARA 159
Cdd:PRK10982 73 NGISMVHQELNLVLQRSVMDNMWLgryPT--KGMFVDQdkmyRDTKAI--FDELDIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825110 160 LAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-203 |
2.00e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 14 TYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMN-MIGCLDvPDEGSYHLDNvdvfklsdnklseirnkKIGFI 92
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMD-KVEGHVHMKG-----------------SVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 93 FQQfNLLPKLSAFENVelpLIYAGLSvsarEKAAIECLEKVGLLEKRRNLPT-----------QLSGGQQQRVAIARALA 161
Cdd:TIGR00957 705 PQQ-AWIQNDSLRENI---LFGKALN----EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVY 776
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489825110 162 GKPQILLADEPTGALDSKTGKEV-------MGILqelnrAGNTIVMITH 203
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIfehvigpEGVL-----KNKTRILVTH 820
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-203 |
2.13e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 30 FTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNvdvfklSDNKLSEiRNKKIGFIFQQFNLLPKLSAFENVE 109
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG------KTATRGD-RSRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 110 LpliYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQ 189
Cdd:PRK13543 105 F---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
170
....*....|....
gi 489825110 190 ELNRAGNTIVMITH 203
Cdd:PRK13543 182 AHLRGGGAALVTTH 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-178 |
2.30e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVE-----QGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLD----------NVDVFKLSDNKLSEIRNK 87
Cdd:COG1245 349 KSYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 88 KIGfifqqfnllpklSAFENVEL--PLiyaglsvsarekaaieCLEKvgLLEKrrNLPTqLSGGQQQRVAIARALAGKPQ 165
Cdd:COG1245 429 DFG------------SSYYKTEIikPL----------------GLEK--LLDK--NVKD-LSGGELQRVAIAACLSRDAD 475
|
170
....*....|...
gi 489825110 166 ILLADEPTGALDS 178
Cdd:COG1245 476 LYLLDEPSAHLDV 488
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-184 |
3.35e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhldnvdvfklsdnklsEIRNK-KIGFIFQQFNLLPKlS 103
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG------------------KIKHSgRISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENVELPLIYAGLSVSAREKAAiECLEKVGLLEKRRNLP-----TQLSGGQQQRVAIARALAGKPQILLADEPTGALDS 178
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYTSVIKAC-QLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*.
gi 489825110 179 KTGKEV 184
Cdd:TIGR01271 582 VTEKEI 587
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-180 |
4.01e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLdVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRA--VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT---LQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIGFIFQQFNLLPklSAFENVELPliYAGLSVSAREKAAieclEKVGLLEKRRNLPTQ-----------LSGGQQQRV 154
Cdd:TIGR01271 1292 -KAFGVIPQKVFIFS--GTFRKNLDP--YEQWSDEEIWKVA----EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLM 1362
|
170 180
....*....|....*....|....*.
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKT 180
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVT 1388
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-217 |
1.22e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.49 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 15 YTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLmnmigCLDVPDEGSYHLDNVDVFKLSDNKLseirnkkigfIFq 94
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL-----VNEGLYASGKARLISFLPKFSRNKL----------IF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 95 qfnlLPKLSAfenvelpLIYAGLsvsarekaaieclekvGLLEKRRNLPTqLSGGQQQRVAIARALAG--KPQILLADEP 172
Cdd:cd03238 65 ----IDQLQF-------LIDVGL----------------GYLTLGQKLST-LSGGELQRVKLASELFSepPGTLFILDEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489825110 173 TGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRI 217
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
6-207 |
1.23e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMigcLDVPDEGSYHLDNVDVFKLSdnKLSEIR 85
Cdd:PLN03140 877 VDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFP--KKQETF 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 NKKIGFIFQQFNLLPKLSAFENvelpLIYAGL-----SVSAREK-----AAIECLEKVGLLEKRRNLP--TQLSGGQQQR 153
Cdd:PLN03140 952 ARISGYCEQNDIHSPQVTVRES----LIYSAFlrlpkEVSKEEKmmfvdEVMELVELDNLKDAIVGLPgvTGLSTEQRKR 1027
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489825110 154 VAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTI 207
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-222 |
3.10e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGClDVPDEGSYH---------LDNVDVFKLSDNKLSEIRnkkiGFIFQQ 95
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAPRgarvtgdvtLNGEPLAAIDAPRLARLR----AVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 96 FNLLPKLSAFENVEL---PLIYAGLSVSAREKAAIEC-LEKVGLLEKRRNLPTQLSGGQQQRVAIARALA---------G 162
Cdd:PRK13547 92 AQPAFAFSAREIVLLgryPHARRAGALTHRDGEIAWQaLALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 163 KPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVM-ITHDPTIAS-YGTRSIRIQDGKL 222
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAArHADRIAMLADGAI 233
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-230 |
3.26e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 58.71 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTLGGETfkALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLdVPDEGSYHLDNVDVFKLSdnkLSEIR 85
Cdd:cd03289 3 MTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP---LQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 nKKIG------FIFQ---QFNLLPklsafenvelpliYAGLSVSAREKAAieclEKVGLLEKRRNLPTQ----------- 145
Cdd:cd03289 77 -KAFGvipqkvFIFSgtfRKNLDP-------------YGKWSDEEIWKVA----EEVGLKSVIEQFPGQldfvlvdggcv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQElNRAGNTIVMITHDPTIASYGTRSIRIQDGKLFHE 225
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLECQRFLVIEENKVRQY 217
|
....*
gi 489825110 226 EATQA 230
Cdd:cd03289 218 DSIQK 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-210 |
3.88e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 31 TVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYH----LDNV-DVFKLSD--NKLSEIRNKKIGFIF--QQFNLLPK 101
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepsWDEVlKRFRGTElqDYFKKLANGEIKVAHkpQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 102 lsAFE-NV-ELpliyagLSVSAREKAAIECLEKVGL---LEkrRNLpTQLSGGQQQRVAIARALAGKPQILLADEPTGAL 176
Cdd:COG1245 175 --VFKgTVrEL------LEKVDERGKLDELAEKLGLeniLD--RDI-SELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|....
gi 489825110 177 DSKTGKEVMGILQELNRAGNTIVMITHDPTIASY 210
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEHDLAILDY 277
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-230 |
4.53e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIRNKkIGFIFQ---------Q 95
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFK-ITIIPQdpvlfsgslR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 96 FNLLPkLSAF--ENVELPLIYAGLS--VSAR-EKAAIECLEKvgllekrrnlPTQLSGGQQQRVAIARALAGKPQILLAD 170
Cdd:TIGR00957 1378 MNLDP-FSQYsdEEVWWALELAHLKtfVSALpDKLDHECAEG----------GENLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825110 171 EPTGALDSKTGK-------------EVMGILQELNRAGN-TIVMITHDPTIASYGTRSIRIQDGKLFHEEATQA 230
Cdd:TIGR00957 1447 EATAAVDLETDNliqstirtqfedcTVLTIAHRLNTIMDyTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDA 1520
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-230 |
7.02e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTktytlgGETFKaldDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNK-- 80
Cdd:PRK15439 266 APVLTVEDLT------GEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrl 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 81 ------LSEIRnkkigfifQQFNLLPKLSAFENVeLPLIYAGLSV---SAREKAAIECLEKVglLEKRRNLPTQ----LS 147
Cdd:PRK15439 337 arglvyLPEDR--------QSSGLYLDAPLAWNV-CALTHNRRGFwikPARENAVLERYRRA--LNIKFNHAEQaartLS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 148 GGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGKLFHEE 226
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEISGAL 485
|
....
gi 489825110 227 ATQA 230
Cdd:PRK15439 486 TGAA 489
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-205 |
1.08e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 56.50 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLM---------------------NMIGCLDVPDegsyhLDNVDvfKLS-----D 78
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPD-----VDSIE--GLSpaiaiD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 NKLSEiRNKK--IGFIFQQFNLLPklsafenvelpLIYAGLSVSARekaaIECLEKVGL--LEKRRNLPTqLSGGQQQRV 154
Cdd:cd03270 84 QKTTS-RNPRstVGTVTEIYDYLR-----------LLFARVGIRER----LGFLVDVGLgyLTLSRSAPT-LSGGEAQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 155 AIAR----ALAGKPQILlaDEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP 205
Cdd:cd03270 147 RLATqigsGLTGVLYVL--DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-204 |
1.29e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTKTYtlggetfkalDDVTFTVE-----QGEFLSIVGPSGSGKSTLMNMI-GCLDvPDEGSyhldnVDvfkl 76
Cdd:PRK13409 338 ETLVEYPDLTKKL----------GDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLaGVLK-PDEGE-----VD---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 77 SDNKLS----EIRNKK-------IGFIFQQFNllpklSAFENVEL--PLiyaglsvsarekaaieCLEKvgLLEKRRNlp 143
Cdd:PRK13409 398 PELKISykpqYIKPDYdgtvedlLRSITDDLG-----SSYYKSEIikPL----------------QLER--LLDKNVK-- 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 144 tQLSGGQQQRVAIARALAGKPQILLADEPTGALD-------SKTGKEVMgilqELNRAgnTIVMITHD 204
Cdd:PRK13409 453 -DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIA----EEREA--TALVVDHD 513
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-207 |
1.52e-09 |
|
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: 54.69 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 34 QGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFklsdnklseirnkkigfifqqfnllpklsafenvelpli 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 114 yaglsvsarekaaIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGI------ 187
Cdd:smart00382 42 -------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrll 108
|
170 180
....*....|....*....|
gi 489825110 188 LQELNRAGNTIVMITHDPTI 207
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKD 128
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-217 |
3.53e-09 |
|
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: 53.90 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 27 DVTFTveQGEFLSIVGPSGSGKSTLMNMIGcldvpdegsyhldnvdvfklsdnklseirnkkIGFIFQQFNLLPKLSAFE 106
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRRSGVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 107 NVELPLIYAGLSVSArekaaieclekvgllekrrnlpTQLSGGQQQRVAIARALA-----GKPQILLaDEPTGALDSKTG 181
Cdd:cd03227 61 GCIVAAVSAELIFTR----------------------LQLSGGEKELSALALILAlaslkPRPLYIL-DEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....*.
gi 489825110 182 KEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRI 217
Cdd:cd03227 118 QALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-203 |
3.89e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYtlgGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTlmnmiGCLDV----PDEGSYH------LDNVDVFK 75
Cdd:NF000106 14 VEVRGLVKHF---GEV-KAVDGVDLDVREGTVLGVLGP*GAA**R-----GALPAhv*gPDAGRRPwrf*twCANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 76 LSDNKLSEIRNKKigfifqqfnlLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVA 155
Cdd:NF000106 85 RTIG*HRPVR*GR----------RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-230 |
3.96e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 28 VTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdnklsEIRNKKIGfIFQQFNLLPKLSAFEN 107
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---------DIRSPRDA-IRAGIMLCPEDRKAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 108 velplIYAGLSVsaREKAAIEC---LEKVGLLEKRR-------------NLPT--------QLSGGQQQRVAIARALAGK 163
Cdd:PRK11288 342 -----IIPVHSV--ADNINISArrhHLRAGCLINNRweaenadrfirslNIKTpsreqlimNLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 164 PQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD-PTIASYGTRSIRIQDGK----LFHEEATQA 230
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRiageLAREQATER 486
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-204 |
4.71e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.93 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI----------GCLDVPD-----EGSYHLDnvdvfklsdnKLSEIRNKKI 89
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlypalarrlhLKKEQPGnhdriEGLEHID----------KVIVIDQSPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 90 G---------------FIFQQFNLLPKLSAFENVELPLIYAGLSVS---------ARE--------KAAIECLEKVGL-- 135
Cdd:cd03271 81 GrtprsnpatytgvfdEIRELFCEVCKGKRYNRETLEVRYKGKSIAdvldmtveeALEffenipkiARKLQTLCDVGLgy 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 136 LEKRRNLPTqLSGGQQQRVAIARALAGK---PQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:cd03271 161 IKLGQPATT-LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-184 |
5.79e-09 |
|
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: 54.86 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGsyhldnvdvfklsdnklsEIRNK-KIGFIFQQFNLLPKlS 103
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG------------------KIKHSgRISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 104 AFENvelplIYAGLSVSA-REKAAIECL---EKVGLLEKRRNLP-----TQLSGGQQQRVAIARALAGKPQILLADEPTG 174
Cdd:cd03291 114 IKEN-----IIFGVSYDEyRYKSVVKACqleEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170
....*....|
gi 489825110 175 ALDSKTGKEV 184
Cdd:cd03291 189 YLDVFTEKEI 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-180 |
6.42e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIRnKKIGFIFQ---------Q 95
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQapvlfsgtvR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 96 FNLLPkLSAFENVELpliyaglsvsarekaaIECLEKVGLLEKRRNLPTQL-----------SGGQQQRVAIARALAGKP 164
Cdd:PLN03130 1331 FNLDP-FNEHNDADL----------------WESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRS 1393
|
170
....*....|....*.
gi 489825110 165 QILLADEPTGALDSKT 180
Cdd:PLN03130 1394 KILVLDEATAAVDVRT 1409
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-203 |
7.40e-09 |
|
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: 55.40 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMI--GCLD--------VPD-----EGSYHLD---NVD-------------- 72
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTlyPALAnrlngaktVPGrytsiEGLEHLDkviHIDqspigrtprsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 73 ---VFklsdnklSEIRN--------KKIGF----------------------IFQQFNLLPKLSA---------FENVEL 110
Cdd:TIGR00630 704 ytgVF-------DEIRElfaetpeaKVRGYtpgrfsfnvkggrceacqgdgvIKIEMHFLPDVYVpcevckgkrYNRETL 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 111 PLIYAGLSVS---------ARE--------KAAIECLEKVGL--LEKRRNLPTqLSGGQQQRVAIARALAGK---PQILL 168
Cdd:TIGR00630 777 EVKYKGKNIAdvldmtveeAYEffeavpsiSRKLQTLCDVGLgyIRLGQPATT-LSGGEAQRIKLAKELSKRstgRTLYI 855
|
250 260 270
....*....|....*....|....*....|....*
gi 489825110 169 ADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-221 |
8.42e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.14 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 27 DVTFTVEQGEFLSIVGPSGSGKSTLMNMIG--------CLDVPDEGSY-------------------HLDNVDVFK---L 76
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLfyvpqrpymtlgtlrdqiiYPDSSEDMKrrgL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 77 SDNKLSEIrnkkigfifqqfnllpklsaFENVELPLIyaglsvsarekaaiecLEKVGLLEKRRNLPTQLSGGQQQRVAI 156
Cdd:TIGR00954 550 SDKDLEQI--------------------LDNVQLTHI----------------LEREGGWSAVQDWMDVLSGGEKQRIAM 593
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 157 ARALAGKPQILLADEPTGALDSktgkEVMG-ILQELNRAGNTIVMITHDPTIASYGTRSIRIqDGK 221
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSV----DVEGyMYRLCREFGITLFSVSHRKSLWKYHEYLLYM-DGR 654
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-202 |
1.19e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 21 TFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGC----LDVPDEGSYHLDNVDvfklsdnkLSEIRNKKIG---FIF 93
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGIT--------PEEIKKHYRGdvvYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 94 QQFNLLPKLSAFENVELP-------LIYAGLSVSAREK------AAIECLE-----KVGllekrRNLPTQLSGGQQQRVA 155
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFAarcktpqNRPDGVSREEYAKhiadvyMATYGLShtrntKVG-----NDFVRGVSGGERKRVS 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489825110 156 IARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMIT 202
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-210 |
1.26e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 1 MPKPLIDMKNLTKTYtlggETFKALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIG------------------CLDVPD 62
Cdd:CHL00131 3 KNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpaykilegdilfkgesILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 63 EGSYHL---------------DNVDVFKLSDNKLseirnkkigfifQQFNLLPKLSAFENVELpliyaglsvsAREKaai 127
Cdd:CHL00131 79 EERAHLgiflafqypieipgvSNADFLRLAYNSK------------RKFQGLPELDPLEFLEI----------INEK--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 128 ecLEKVGLLEK--RRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP 205
Cdd:CHL00131 134 --LKLVGMDPSflSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ 211
|
....*
gi 489825110 206 TIASY 210
Cdd:CHL00131 212 RLLDY 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-222 |
1.38e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 12 TKTYTLGGETF------KALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIgcldvpdegsyhldnvdvfkLSDNKLSEIR 85
Cdd:PTZ00243 657 AKTPKMKTDDFfelepkVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL--------------------LSQFEISEGR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 ---NKKIGFIFQQF---------NLLpklsaFENVELPliyaglsvsAREKAAIEC--LE-KVGLL---------EKRRN 141
Cdd:PTZ00243 717 vwaERSIAYVPQQAwimnatvrgNIL-----FFDEEDA---------ARLADAVRVsqLEaDLAQLgggleteigEKGVN 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 142 LptqlSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMG--ILQELnrAGNTIVMITHDPTIASYGTRSIRIQD 219
Cdd:PTZ00243 783 L----SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGAL--AGKTRVLATHQVHVVPRADYVVALGD 856
|
...
gi 489825110 220 GKL 222
Cdd:PTZ00243 857 GRV 859
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-210 |
1.60e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 31 TVEQGEFLSIVGPSGSGKSTLMNMI-GCL-----DVPDEGSYhlDNV-DVFKLSD--NKLSEIRNKKIGFIF--QQFNLL 99
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsGELipnlgDYEEEPSW--DEVlKRFRGTElqNYFKKLYNGEIKVVHkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 100 PKlsAFE-NV-ELpliyagLSVSAREKAAIECLEKVGL---LEKRRNlptQLSGGQQQRVAIARALAGKPQILLADEPTG 174
Cdd:PRK13409 173 PK--VFKgKVrEL------LKKVDERGKLDEVVERLGLeniLDRDIS---ELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|....*.
gi 489825110 175 ALDSKTGKEVMGILQELNRaGNTIVMITHDPTIASY 210
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDY 276
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-220 |
2.42e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.06 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 133 VGLLEKRRNLPTqLSGGQQQRVAIAR----ALAGKPQILlaDEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIA 208
Cdd:PRK00635 465 LPYLTPERALAT-LSGGEQERTALAKhlgaELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI 541
|
90
....*....|..
gi 489825110 209 SYGTRSIRIQDG 220
Cdd:PRK00635 542 SLADRIIDIGPG 553
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-222 |
3.05e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 6 IDMKNLTKTYTlGGETFKaldDVTFTVEQGEFLSIVGPSGSGKSTLMN-MIGCLDvPDEGSYhldnvdvfklsdnKLSEi 84
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFK---NLNLLLEAGERLAIIGENGVGKTTLLRtLVGELE-PDSGTV-------------KWSE- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 85 rNKKIGFIFQQFNllpklSAFENvELPLiYAGLSVSAREKAAIECLEkvGLLEkrRNLPTQ---------LSGGQQQRVA 155
Cdd:PRK15064 381 -NANIGYYAQDHA-----YDFEN-DLTL-FDWMSQWRQEGDDEQAVR--GTLG--RLLFSQddikksvkvLSGGEKGRML 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 156 IARALAGKPQILLADEPTGALDsktgkevMGILQELNRA----GNTIVMITHDPT-IASYGTRSIRIQDGKL 222
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMAlekyEGTLIFVSHDREfVSSLATRIIEITPDGV 513
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-204 |
3.75e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 41 VGPSGSGKSTLMNMIGCLDVPDEGSYHLD-NVDVFKLSDNKlseirnkkigFIFQQFNLL-------PKLSAFeNVELPL 112
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQ----------FAFEEFTVLdtvimghTELWEV-KQERDR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 113 IYA-----------------------GLSVSARekaAIECLEKVGLLEKRRNLP-TQLSGGQQQRVAIARALAGKPQILL 168
Cdd:PRK15064 102 IYAlpemseedgmkvadlevkfaemdGYTAEAR---AGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILL 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 489825110 169 ADEPTGALDSKTGKEVMGILQELNragNTIVMITHD 204
Cdd:PRK15064 179 LDEPTNNLDINTIRWLEDVLNERN---STMIIISHD 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-173 |
3.89e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 24 ALDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSyhldnVDVF--KLSDNKLSEIRNKKIGFIFQQF--NLL 99
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGR-----VEVLggDMADARHRRAVCPRIAYMPQGLgkNLY 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 100 PKLSAFENVELpliYA---GLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPT 173
Cdd:NF033858 91 PTLSVFENLDF---FGrlfGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-209 |
4.04e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETFKALDdvtFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSyhldnvdVFKLSDNKLSe 83
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLFKNLN---FGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT-------VFRSAKVRMA- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 irnkkigfIFQQFNLlpklSAFENVELPLIYAGLSVSAREKAAIECleKVGLLEKRRNLPTQ----LSGGQQQRVAIARA 159
Cdd:PLN03073 576 --------VFSQHHV----DGLDLSSNPLLYMMRCFPGVPEQKLRA--HLGSFGVTGNLALQpmytLSGGQKSRVAFAKI 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489825110 160 LAGKPQILLADEPTGALDSKTgkeVMGILQELNRAGNTIVMITHDPTIAS 209
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-204 |
4.29e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 3 KPLIDMKNLTktYTLGGETFkaLDDVTFTVEQGEFLSIVGPSGSGKSTLMN-MIGCLDvPDEGSYHldnvdvfklSDNKL 81
Cdd:PRK11147 317 KIVFEMENVN--YQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIH---------CGTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 82 sEIRnkkigfIFQQF--NLLPKLSAFENVElpliyAG---LSVSAREKAAIECLEKVGLLEKRRNLPTQ-LSGGQQQRVA 155
Cdd:PRK11147 383 -EVA------YFDQHraELDPEKTVMDNLA-----EGkqeVMVNGRPRHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLL 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 156 IARALAgKPQILLA-DEPTGALDSKTgkevMGILQEL--NRAGnTIVMITHD 204
Cdd:PRK11147 451 LARLFL-KPSNLLIlDEPTNDLDVET----LELLEELldSYQG-TVLLVSHD 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-203 |
8.06e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSdnkLSEIRnkkigfifQQFNLLPklsa 104
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLR--------RVLSIIP---- 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 fenvELPLIYAGL------SVSAREKAAI-ECLEKVGLLEKRRNLPTQL-----------SGGQQQRVAIARALAGKPQI 166
Cdd:PLN03232 1317 ----QSPVLFSGTvrfnidPFSEHNDADLwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKI 1392
|
170 180 190
....*....|....*....|....*....|....*..
gi 489825110 167 LLADEPTGALDSKTGKEVMGILQELNRAGnTIVMITH 203
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIREEFKSC-TMLVIAH 1428
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-202 |
1.54e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMIT 202
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
146-223 |
3.24e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 146 LSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMG--ILQELNraGNTIVMIT---------------HDPTIA 208
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELR--GKTRVLVTnqlhflsqvdriilvHEGMIK 818
|
90
....*....|....*
gi 489825110 209 SYGTRSIRIQDGKLF 223
Cdd:PLN03130 819 EEGTYEELSNNGPLF 833
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-201 |
4.58e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 23 KALDDVTFTVEQGEFLSIVGPSGSGKSTL-MNMIGcldvpdeGSY---------------HLDNVDvfKLSDNKL---SE 83
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFG-------RSYgrnisgtvfkdgkevDVSTVS--DAIDAGLayvTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 84 IRnKKIGFIFQ---QFNL----LPKLSAF----ENVELpliyaGLSVSAREKAAIEC---LEKVGllekrrnlptQLSGG 149
Cdd:NF040905 345 DR-KGYGLNLIddiKRNItlanLGKVSRRgvidENEEI-----KVAEEYRKKMNIKTpsvFQKVG----------NLSGG 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489825110 150 QQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMI 201
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-201 |
1.19e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 30 FTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIrnkkIGFIFQQFN---LLPKLSAFE 106
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNtdmLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 107 NVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRnlpTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMG 186
Cdd:PRK10938 100 RTTAEIIQDEVKDPARCEQLAQQFGITALLDRRF---KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170
....*....|....*
gi 489825110 187 ILQELNRAGNTIVMI 201
Cdd:PRK10938 177 LLASLHQSGITLVLV 191
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
144-203 |
1.23e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.87 E-value: 1.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 144 TQLSGGQQQRVAIARALAGKPQ-----ILlaDEPTgaldskTG------KEVMGILQELNRAGNTIVMITH 203
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKRSTgktlyIL--DEPT------TGlhfhdiRKLLEVLHRLVDKGNTVVVIEH 887
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-206 |
2.09e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 40 IVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdnklSEIRNKKIGFIFQQFNLLPKLSAFENVEL-PLIYaglS 118
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI--------NNIAKPYCTYIGHNLGLKLEMTVFENLKFwSEIY---N 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 119 VSAREKAAIECLEKVGLLEKRrnlPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTI 198
Cdd:PRK13541 100 SAETLYAAIHYFKLHDLLDEK---CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIV 176
|
....*...
gi 489825110 199 VMITHDPT 206
Cdd:PRK13541 177 LLSSHLES 184
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-228 |
5.42e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 4 PLIDMKNLTKTYTLGGETfKALDDVTFTVEQGEFLSIVGPSGSGKSTLMN-MIGCLDvpdegsyHLDNVDVfklsDNKLS 82
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELS-------HAETSSV----VIRGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKKIGFIFQQfnllpklSAFENVelplIYAGLSVSAREKAAIE--CLEKVGLLEKRRNLP------TQLSGGQQQRV 154
Cdd:PLN03232 681 VAYVPQVSWIFNA-------TVRENI----LFGSDFESERYWRAIDvtALQHDLDLLPGRDLTeigergVNISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825110 155 AIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQDGkLFHEEAT 228
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEG-MIKEEGT 822
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
144-203 |
7.74e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 7.74e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489825110 144 TQLSGGQQQRVAIARALAGKPQ-----ILlaDEPTgaldskTG------KEVMGILQELNRAGNTIVMITH 203
Cdd:PRK00349 829 TTLSGGEAQRVKLAKELSKRSTgktlyIL--DEPT------TGlhfediRKLLEVLHRLVDKGNTVVVIEH 891
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
79-218 |
1.67e-05 |
|
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: 45.34 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 79 NKLSEIRNKKIGFIFQQFnlLPKLSAFENVELP--------LIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTqLSGGQ 150
Cdd:TIGR00618 879 NGINQIKIQFDGDALIKF--LHEITLYANVRLAnqsegrfhGRYADSHVNARKYQGLALLVADAYTGSVRPSAT-LSGGE 955
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489825110 151 QQRVAIARALA--------GKPQI--LLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSIRIQ 218
Cdd:TIGR00618 956 TFLASLSLALAladllstsGGTVLdsLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVK 1033
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-210 |
1.88e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTL----MNMI----GCLDVP--DEGSYhldnvdvfklsdnKLSEIRnkkigfifQ 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLlltfMRMVevcgGEIRVNgrEIGAY-------------GLRELR--------R 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 95 QFNLLPKL------SAFENVElPLIYAGlsvSAREKAAiecLEKVGLLEK---------RRNLP--TQLSGGQQQRVAIA 157
Cdd:PTZ00243 1385 QFSMIPQDpvlfdgTVRQNVD-PFLEAS---SAEVWAA---LELVGLRERvasesegidSRVLEggSNYSVGQRQLMCMA 1457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 158 RALAGKPQ-ILLADEPTG----ALDSKTGKEVMGILqelnrAGNTIVMITHD-PTIASY 210
Cdd:PTZ00243 1458 RALLKKGSgFILMDEATAnidpALDRQIQATVMSAF-----SAYTVITIAHRlHTVAQY 1511
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-221 |
3.84e-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: 42.94 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 32 VEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVfklsdnklsEIRNKKIgfifqqfnllpklsafenvelp 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP---------VYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 112 liyaglsvsarekaaieclekvgllekrrnlptQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQEL 191
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|.
gi 489825110 192 N-RAGNTIVMITHDPTIASYGTRSIRIQDGK 221
Cdd:cd03222 118 SeEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-203 |
6.49e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.97 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTL----MNMIGCLDvpdeGSYHLDNVDVFKLS----DNKLSEIRNKKIGFIFQ-Q 95
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhtlRSRLSIILQDPILFSGSiR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 96 FNLLPKLSAFENVelplIYAGLSVsAREKAAIECLEKvGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGA 175
Cdd:cd03288 113 FNLDPECKCTDDR----LWEALEI-AQLKNMVKSLPG-GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190
....*....|....*....|....*....|.
gi 489825110 176 LDSKTGKevmgILQELNR---AGNTIVMITH 203
Cdd:cd03288 187 IDMATEN----ILQKVVMtafADRTVVTIAH 213
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
40-204 |
8.86e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 40 IVGPSGSGKSTLMNMI-----GCLDVPDEGSYHLDNVD--------VFKLSDN------------KLSEIRNKKIGFIFQ 94
Cdd:COG0419 28 IVGPNGAGKSTILEAIryalyGKARSRSKLRSDLINVGseeasvelEFEHGGKryrierrqgefaEFLEAKPSERKEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 95 QfnlLPKLSAFENVE--LPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPT-QLSGGQQQRVAIARALAgkpqiLLADe 171
Cdd:COG0419 108 R---LLGLEIYEELKerLKELEEALESALEELAELQKLKQEILAQLSGLDPIeTLSGGERLRLALADLLS-----LILD- 178
|
170 180 190
....*....|....*....|....*....|...
gi 489825110 172 pTGALDSKTGKEVMGILQELnragntiVMITHD 204
Cdd:COG0419 179 -FGSLDEERLERLLDALEEL-------AIITHV 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-177 |
1.03e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 113 IYAGLSVSArekaaieclekvgllEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALD 177
Cdd:PLN03073 327 ILAGLSFTP---------------EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-205 |
1.10e-04 |
|
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: 41.82 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 40 IVGPSGSGKSTLmnmIGCLDVPDEGSYHLDNVDVFKlsDNKLseIR-NKKIGFIFQQFNLLP--------KLSAFENVel 110
Cdd:cd03240 27 IVGQNGAGKTTI---IEALKYALTGELPPNSKGGAH--DPKL--IReGEVRAQVKLAFENANgkkytitrSLAILENV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 111 plIYaglsVSAREKAAIeclekvgLLEKRrnlpTQLSGGQQQ------RVAIARALAGKPQILLADEPTGALDSKTGKEV 184
Cdd:cd03240 98 --IF----CHQGESNWP-------LLDMR----GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEES 160
|
170 180
....*....|....*....|...
gi 489825110 185 M-GILQELNRAGN-TIVMITHDP 205
Cdd:cd03240 161 LaEIIEERKSQKNfQLIVITHDE 183
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-204 |
1.18e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489825110 146 LSGGQQQRVAIARAL---AGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHD 204
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-210 |
1.40e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 5 LIDMKNLtKTYTLGGETFKALDdvtFTVEQGEFLSIVGPSGSGKSTL-MNMIGCLDVP-DEGSYHLDNVDVFKLSDnklS 82
Cdd:PRK09580 1 MLSIKDL-HVSVEDKAILRGLN---LEVRPGEVHAIMGPNGSGKSTLsATLAGREDYEvTGGTVEFKGKDLLELSP---E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 83 EIRNKKIGFIFQ----------QFNLLPKLSAFENvelpliYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQ-----LS 147
Cdd:PRK09580 74 DRAGEGIFMAFQypveipgvsnQFFLQTALNAVRS------YRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsvnvgFS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825110 148 GGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASY 210
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDY 210
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-217 |
2.05e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 22 FKALDDVTFTVEQGeFLSIVGPSGSGKSTLMNMIGCLdVPDEGSYHLDNVDVFKLSDNKLSEIR---------------- 85
Cdd:COG3593 11 FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLL-LGPSSSRKFDEEDFYLGDDPDLPEIEieltfgsllsrllrll 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 86 -----NKKIGFIFQQFN---------LLPKLSAFENVELPLIYAGLSVSAREKAAIECLEKVGLLEKRRNLPTQLSGGQQ 151
Cdd:COG3593 89 lkeedKEELEEALEELNeelkealkaLNELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825110 152 QRVAIA--RALA-----GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIAS-YGTRSIRI 217
Cdd:COG3593 169 RLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSeVPLENIRR 242
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
146-203 |
7.16e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 7.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825110 146 LSGGQQQRVAIARALA------GKPQI--LLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITH 203
Cdd:PRK10246 950 LSGGESFLVSLALALAlsdlvsHKTRIdsLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISH 1015
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-209 |
1.22e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489825110 146 LSGGQQQRVAIAR----ALAGKPQILlaDEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDP-TIAS 209
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEdTIRA 555
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
137-207 |
1.35e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 1.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489825110 137 EKRRNLP-TQLSGGQQQ---RVAIARALAGKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTI 207
Cdd:pfam13304 227 GGGGELPaFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-61 |
1.53e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489825110 26 DDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVP 61
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
146-217 |
1.74e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 146 LSGGQQQRVAIARALA----------GKPQILLADEPTGALDSKTGKEVMGILQELNRAGNTIVMITHDPTIASYGTRSI 215
Cdd:cd03279 124 LSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRL 203
|
..
gi 489825110 216 RI 217
Cdd:cd03279 204 EV 205
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
25-207 |
3.90e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 37.35 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLseirnkkigfifqqfnLLPKLSA 104
Cdd:PRK15177 3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGDALPLGANSF----------------ILPGLTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 105 FENVELPLIYAGLSvsaREKAAIECLEKVGLLEKRRNLPTQLSGGQQQRVAIARALAGKPQILLADEPTGALDSKTGKEV 184
Cdd:PRK15177 67 EENARMMASLYGLD---GDEFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRM 143
|
170 180
....*....|....*....|....
gi 489825110 185 MGILQ-ELNRAGntIVMITHDPTI 207
Cdd:PRK15177 144 QAALAcQLQQKG--LIVLTHNPRL 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-204 |
3.95e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.84 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 25 LDDVTFTVEQGEFLSIVGPSGSGKSTLMNMIGCLDVPDEGSYHLDNVDVFKLSDNKLSEIRNKKIGFIF---QQFNLLPK 101
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825110 102 LSAFENVE-----LPLIYAGLSV----SAREKAAiECLEKVGLLEKRRNLP-TQLSGGQQQRVAIARALAGKPQILLADE 171
Cdd:PRK10636 97 QLHDANERndghaIATIHGKLDAidawTIRSRAA-SLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190
....*....|....*....|....*....|...
gi 489825110 172 PTGALDSKTgkeVMGILQELNRAGNTIVMITHD 204
Cdd:PRK10636 176 PTNHLDLDA---VIWLEKWLKSYQGTLILISHD 205
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
27-55 |
4.15e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 4.15e-03
10 20
....*....|....*....|....*....
gi 489825110 27 DVTFTVeqGEFLSIVGPSGSGKSTLMNMI 55
Cdd:PRK00349 629 DVEIPL--GKFTCVTGVSGSGKSTLINET 655
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
40-55 |
4.37e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.62 E-value: 4.37e-03
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
23-55 |
5.90e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 36.77 E-value: 5.90e-03
10 20 30
....*....|....*....|....*....|...
gi 489825110 23 KALDDVtFTVEQGEFLSIVGPSGSGKSTLMNMI 55
Cdd:cd01136 56 RAIDGL-LTCGEGQRIGIFAGSGVGKSTLLGMI 87
|
|
| |
