|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
32-287 |
5.64e-135 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 382.13 E-value: 5.64e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:COG1116 7 ALELRGVSKRF--PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 192 PFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPH-RDnpIERRKQAGMN 270
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRpRD--RELRTSPEFA 242
|
250
....*....|....*..
gi 1737829014 271 EYVAHLMELLKVGRDDH 287
Cdd:COG1116 243 ALRAEILDLLREEAERA 259
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
33-254 |
9.80e-127 |
|
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: 359.86 E-value: 9.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:cd03293 1 LEVRNVSKTY--GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDL 254
Cdd:cd03293 159 FSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
32-247 |
1.68e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 254.64 E-value: 1.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ-- 108
Cdd:COG3842 5 ALELENVSKRY------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEKrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRIE 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
47-257 |
6.76e-82 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 247.47 E-value: 6.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKDLLMPWRSIQK 126
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:COG4525 96 NVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 207 DLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHR 257
Cdd:COG4525 176 LLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRR 226
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
33-281 |
4.16e-80 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 242.34 E-value: 4.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:NF040729 2 LKIQNISKTFINN--KKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:NF040729 80 FQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHRDNpierRKQAGMNEY 272
Cdd:NF040729 160 LGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRN----RESEKYLEY 235
|
....*....
gi 1737829014 273 VAHLMELLK 281
Cdd:NF040729 236 KDHLTNILK 244
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
33-248 |
9.63e-78 |
|
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: 235.11 E-value: 9.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ--V 109
Cdd:cd03259 1 LELKGLSKTY------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvPPERrnI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRIVQ 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
33-253 |
7.02e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 219.63 E-value: 7.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK------PVRgpS 106
Cdd:COG1118 3 IEVRNISKRFGSFT------LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlPPR--E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDV 186
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 187 LLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRIEQVGTPD 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
33-241 |
1.76e-67 |
|
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: 209.27 E-value: 1.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------ 106
Cdd:cd03255 1 IELKNLSKTYGG--GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ---QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:cd03255 79 frrRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRD 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
53-257 |
7.93e-67 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 208.79 E-value: 7.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKDLLMPWRSIQKNVELGM 132
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQML 212
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHR 257
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARR 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
32-250 |
6.70e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 205.28 E-value: 6.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----- 106
Cdd:COG1136 4 LLELRNLTKSY--GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ----QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:COG1136 82 rlrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 183 EPDVLLMDEPFSALDAQT-KMVLQQdLAQMLASEGKTALMITHDLaEAIALSDRVFVMSErpGTIIEEI 250
Cdd:COG1136 162 RPKLILADEPTGNLDSKTgEEVLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRD--GRIVSDE 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
33-246 |
4.32e-64 |
|
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: 200.93 E-value: 4.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG---PSQQV 109
Cdd:cd03300 1 IELENVSKFY------GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTI 246
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK--GKI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
32-241 |
1.99e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 203.38 E-value: 1.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-------RG 104
Cdd:COG3839 3 SLELENVSKSY------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 psqqVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG3839 77 ----IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 185 DVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
33-248 |
2.64e-62 |
|
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: 196.75 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPSQ--- 107
Cdd:cd03295 1 IEFENVTKRYGGGK-----KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVElrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL--KGFENHYPHQLSGGMRQRAALARTLAVEPD 185
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEIVQ 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
33-250 |
5.47e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 198.01 E-value: 5.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PS---- 106
Cdd:COG1125 2 IEFENVTKRYPDGT-----VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDldPVelrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ------QQVAfmlqkdlLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL--KGFENHYPHQLSGGMRQRAALAR 178
Cdd:COG1125 77 rigyviQQIG-------LFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EEI 250
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIVqydtpEEI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-253 |
5.70e-62 |
|
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: 203.98 E-value: 5.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 17 ADARHAQPAAAPLpfaIEYRGVTRRFKNRqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG1123 248 GRAAPAAAAAEPL---LEVRNLSKRYPVR-GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 97 LAGKPVRGPSQQVAFMLQKDL----------LMPWRSIQKNVELGMQIRGR-SKAERAEVAKALLARCHL-KGFENHYPH 164
Cdd:COG1123 324 FDGKDLTKLSRRSLRELRRRVqmvfqdpyssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpG 244
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--G 481
|
....*....
gi 1737829014 245 TIIEEITVD 253
Cdd:COG1123 482 RIVEDGPTE 490
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
53-278 |
2.19e-61 |
|
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: 195.55 E-value: 2.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQKDLLMPWRS 123
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 204 LQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EEITVdlphrdNPierrkqagMNEYVAHLME 278
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLVqvgtpEEILT------NP--------ANDYVREFFR 262
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
56-255 |
3.73e-61 |
|
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: 193.45 E-value: 3.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPSQQVAFmlQKDLLMPWRSIQKNVELGMQ 133
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDRMVVF--QNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 --IRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQM 211
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737829014 212 LASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEI-TVDLP 255
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFP 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
33-253 |
9.86e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.59 E-value: 9.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQ 108
Cdd:COG1131 1 IEVRGLTKRYGDK------TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPaevrRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRIVADGTPD 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-241 |
2.24e-60 |
|
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: 191.78 E-value: 2.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---QQ 108
Cdd:cd03296 2 SIEVRNVSKRF------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqeRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGR----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 185 DVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
53-250 |
5.68e-60 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 195.32 E-value: 5.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGE-FVsLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---------VAFMLQKDLLMPWR 122
Cdd:COG4175 42 GVNDASFDVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrrkkMSMVFQHFALLPHR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM 202
Cdd:COG4175 121 TVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 203 VLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EEI 250
Cdd:COG4175 201 EMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRIVqigtpEEI 251
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
33-247 |
5.92e-60 |
|
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: 190.24 E-value: 5.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKnrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:COG1122 1 IELENLSFSYP-----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrelrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQkD----LLMPwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG1122 76 KVGLVFQ-NpddqLFAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDD--GRIV 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
41-241 |
1.88e-58 |
|
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: 185.75 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 41 RFKN---RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP-----SQQVAFM 112
Cdd:cd03225 1 ELKNlsfSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQK---DLLMPwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03225 81 FQNpddQFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-249 |
5.67e-56 |
|
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: 180.01 E-value: 5.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:cd03257 2 LEVKNLSVSFPT--GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLM----------PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL---KGFENHYPHQLSGGMRQRAALART 179
Cdd:cd03257 80 RRKEIQMvfqdpmsslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 180 LAVEPDVLLMDEPFSALDAQTK---MVLQQDLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQaqiLDLLKKLQEEL---GLTLLFITHDLGVVAKIADRVAVMYA--GKIVEE 227
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
36-239 |
8.50e-56 |
|
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: 183.70 E-value: 8.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF--M 112
Cdd:TIGR03265 8 DNIRKRF------GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDItRLPPQKRDYgiV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
33-241 |
9.08e-55 |
|
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: 175.45 E-value: 9.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---- 108
Cdd:cd03229 1 LELKNVSKRY------GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 ---VAFMLQKDLLMPWRSIQKNVELGmqirgrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPD 185
Cdd:cd03229 75 rrrIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
32-258 |
9.60e-55 |
|
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: 177.69 E-value: 9.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ---- 107
Cdd:COG1124 1 MLEVRNLSVSY--GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkafr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 -QVAFMLQ--KDLLMPWRSIQKNVELGMQIRGRskAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG1124 79 rRVQMVFQdpYASLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRD 258
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVADLLAG 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
32-261 |
3.59e-54 |
|
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: 175.94 E-value: 3.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----- 106
Cdd:COG1127 5 MIEVRNLTKSF------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ---QQVAFMLQKDLL---MpwrSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALART 179
Cdd:COG1127 79 elrRRIGMLFQGGALfdsL---TVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 180 LAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD-LPHRD 258
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD--GKIIAEGTPEeLLASD 233
|
...
gi 1737829014 259 NPI 261
Cdd:COG1127 234 DPW 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
33-239 |
4.39e-53 |
|
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: 172.05 E-value: 4.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQ-V 109
Cdd:cd03301 1 VELENVTKRFGNV------TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdLPPKDRdI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAE----VAKALlarcHLKGFENHYPHQLSGGMRQRAALARTLAVEPD 185
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDErvreVAELL----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
33-249 |
5.03e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.87 E-value: 5.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAfM 112
Cdd:COG1126 2 IEIENLHKSF------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN-K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDL--------LMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG1126 75 LRRKVgmvfqqfnLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 184 PDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG1126 155 PKVMLFDEPTSALDPElVGEVL--DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDG--GRIVEE 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
33-248 |
5.44e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 176.45 E-value: 5.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---V 109
Cdd:PRK11432 7 VVLKNITKRF------GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQqrdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK--GKIMQ 217
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
49-253 |
6.34e-53 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 176.58 E-value: 6.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQKDLLM 119
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpvelrevrrKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 200 TKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVD 253
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIM--KAGEIVQVGTPD 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
33-248 |
8.87e-53 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 172.29 E-value: 8.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQ--QV 109
Cdd:TIGR00968 1 IEIANISKRF------GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDAtRVHARdrKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:TIGR00968 75 GFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN--GKIEQ 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
30-256 |
2.03e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 166.78 E-value: 2.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 30 PFAIEyrGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtLAGK-PVRGPSQQ 108
Cdd:PRK11247 12 PLLLN--AVSKRYGER------TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTaPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARChlkgfeNHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRA------NEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPH 256
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDLPR 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
32-242 |
3.53e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 165.65 E-value: 3.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:COG1121 6 AIELENLTVSYGGR------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKdllmpwRSIQKN--------VELGMQ-----IRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALAR 178
Cdd:COG1121 80 VPQR------AEVDWDfpitvrdvVLMGRYgrrglFRRPSRADREAVDEAL-ERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSER 242
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
54-248 |
1.09e-49 |
|
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: 164.43 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---QQVAFMLQKDLLMPWRSIQKNVEL 130
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpekRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 GMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQ 210
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737829014 211 MLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIE 248
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQ 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
49-247 |
1.25e-49 |
|
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: 164.45 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQ--------- 114
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSrrelaRRIAYVPQeppapfglt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 -KDLLM----PWRSIqknvelgmqIRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:COG1120 92 vRELVAlgryPHLGL---------FGRPSAEDREAVEEAL-ERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD--GRIV 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
33-239 |
1.46e-49 |
|
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: 163.08 E-value: 1.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------ 106
Cdd:cd03262 1 IEIKNLHKSFGDFH------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 -QQVAFMLQKDLLMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03262 75 rQKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 185 DVLLMDEPFSALDAQT-KMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03262 155 KVMLFDEPTSALDPELvGEVL--DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-253 |
3.02e-49 |
|
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: 170.47 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS---EGQVTLAGKPVRGPS-- 106
Cdd:COG1123 4 LLEVRDLSVRY----PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ---QQVAFMLQ--KDLLMPWRsIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLA 181
Cdd:COG1123 80 lrgRRIGMVFQdpMTQLNPVT-VGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 182 VEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVD 253
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVEDGPPE 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
33-261 |
6.21e-49 |
|
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: 162.29 E-value: 6.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ----- 107
Cdd:cd03261 1 IELRGLTKSF------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 ---QVAFMLQKDLLMPWRSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:cd03261 75 lrrRMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQ---DLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD-LPHRDN 259
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDlirSLKKEL---GLTSIMVTHDLDTAFAIADRIAVLYD--GKIVAEGTPEeLRASDD 229
|
..
gi 1737829014 260 PI 261
Cdd:cd03261 230 PL 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
33-227 |
7.77e-49 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 161.76 E-value: 7.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAF 111
Cdd:COG2884 2 IRFENVSKRYPGGR-----EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQK------DL-LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG2884 77 LRRRigvvfqDFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 185 DVLLMDEPFSALDAQTKM-VLqqDLAQMLASEGKTALMITHDLA 227
Cdd:COG2884 157 ELLLADEPTGNLDPETSWeIM--ELLEEINRRGTTVLIATHDLE 198
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
33-281 |
1.28e-48 |
|
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: 161.56 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR----GPSQQ 108
Cdd:COG4555 2 IEVENLSKKYGKVP------ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkeprEARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDlphrdnpiERRKQAG 268
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHK--GKVVAQGSLD--------ELREEIG 224
|
250
....*....|...
gi 1737829014 269 MNEYVAHLMELLK 281
Cdd:COG4555 225 EENLEDAFVALIG 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
33-252 |
1.37e-48 |
|
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: 161.21 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--------RG 104
Cdd:cd03258 2 IELKNVSKVFGDT--GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgkelRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 185 DVLLMDEPFSALDAQ-TKMVLQ--QDLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV 252
Cdd:cd03258 160 KVLLCDEATSALDPEtTQSILAllRDINREL---GLTIVLITHEMEVVKRICDRVAVMEK--GEVVEEGTV 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
33-246 |
2.21e-48 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 165.12 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ--V 109
Cdd:PRK09452 15 VELRGISKSF------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENrhV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTI 246
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
32-250 |
6.06e-48 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 163.33 E-value: 6.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---QQ 108
Cdd:PRK10851 2 SIEIANIKKSFGRTQ------VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHardRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQI-----RGRSKAERAEVAKaLLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGLTVlprreRPNAAAIKAKVTQ-LLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGK-TALMITHDLAEAIALSDRVFVMSErpgTIIEEI 250
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQ-LHEELKfTSVFVTHDQEEAMEVADRVVVMSQ---GNIEQA 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
33-252 |
7.82e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 162.55 E-value: 7.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--------RG 104
Cdd:COG1135 2 IELENLSKTF--PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalserelRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 185 DVLLMDEPFSALDAQ-TKMVLQ--QDLAQMLaseGKTALMITHDLA--EAIAlsDRVFVMSErpGTIIEEITV 252
Cdd:COG1135 160 KVLLCDEATSALDPEtTRSILDllKDINREL---GLTIVLITHEMDvvRRIC--DRVAVLEN--GRIVEQGPV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
33-248 |
2.78e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 157.73 E-value: 2.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-----APSEGQVTLAGKPVRGPSQ 107
Cdd:cd03260 1 IELRDLNVYYGDKH------ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 -------QVAFMLQKDLLMPwRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLKGFENH--YPHQLSGGMRQRAALA 177
Cdd:cd03260 75 dvlelrrRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEgKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKI-EELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLN--GRLVE 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-240 |
3.81e-47 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 161.93 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 22 AQPAAAPLpfaIEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK- 100
Cdd:PRK11607 12 TRKALTPL---LEIRNLTKSFDGQH------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 101 -----PVRGPsqqVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAA 175
Cdd:PRK11607 83 lshvpPYQRP---INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
33-246 |
6.51e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.13 E-value: 6.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQGkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:COG4619 1 LELEGLSFRVGGKPI------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewrR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLmpWR-SIQKNVELGMQIRGRSKAEraEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPD 185
Cdd:COG4619 75 QVAYVPQEPAL--WGgTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTI 246
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL--EAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
33-239 |
1.37e-46 |
|
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: 154.09 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQ 108
Cdd:cd03230 1 IEVRNLSKRYGKK------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPeevkRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPwrsiqknvelgmqirgrskaeraevakallarcHLKGFENHYphqLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03230 75 IGYLPEEPSLYE---------------------------------NLTVRENLK---LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
69-240 |
1.64e-46 |
|
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: 158.81 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQ-VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEV 145
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtnVPPHLRhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 146 AKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHD 225
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*
gi 1737829014 226 LAEAIALSDRVFVMS 240
Cdd:TIGR01187 161 QEEAMTMSDRIAIMR 175
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
64-241 |
3.29e-46 |
|
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: 154.76 E-value: 3.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 64 GEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGPSQQ--VAFMLQKDLLMPWRSIQKNVELGMqi 134
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQrkIGLVFQQYALFPHLNVRENLAFGL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAS 214
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180
....*....|....*....|....*..
gi 1737829014 215 EGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
61-262 |
5.07e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.53 E-value: 5.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQ-VAFMLQKDLLMPWRSIQKNVELGMQIRGR 137
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlpPAERpVSMLFQENNLFPHLTVAQNIGLGLRPGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 -SKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAqtkmVLQQD----LAQML 212
Cdd:COG3840 102 lTAEQRAQVEQAL-ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP----ALRQEmldlVDELC 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIE 262
Cdd:COG3840 177 RERGLTVLMVTHDPEDAARIADRVLLVAD--GRIAADGPTAALLDGEPPP 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
52-239 |
1.22e-45 |
|
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: 153.07 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKdllmpwRSIQKN---- 127
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQR------RSIDRDfpis 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 128 ----VELGMQIRGR-----SKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:cd03235 87 vrdvVLMGLYGHKGlfrrlSKADKAKVDEAL-ERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 199 QTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03235 166 KTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
32-249 |
2.34e-45 |
|
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: 152.97 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP---------- 101
Cdd:COG4181 8 IIELRGLTKTV--GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 -VRGpsQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAEraEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTL 180
Cdd:COG4181 86 rLRA--RHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVMSErpGTIIEE 249
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRA--GRLVED 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
36-253 |
1.20e-44 |
|
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: 153.67 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP---SEGQVTLAGKPVRGPSQ----- 107
Cdd:COG0444 5 RNLKVYF--PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 ----QVAFMLQKDL--LMPWRSIQKNVELGMQI-RGRSKAERAEVAKALLARCHLKGFENH---YPHQLSGGMRQRAALA 177
Cdd:COG0444 83 irgrEIQMIFQDPMtsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 178 RTLAVEPDVLLMDEPFSALD----AQtkmVLQ--QDLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:COG0444 163 RALALEPKLLIADEPTTALDvtiqAQ---ILNllKDLQREL---GLAILFITHDLGVVAEIADRVAVMYA--GRIVEEGP 234
|
..
gi 1737829014 252 VD 253
Cdd:COG0444 235 VE 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
33-239 |
2.62e-44 |
|
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: 148.30 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQGKgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:cd03228 1 IEFKNVSFSYPGRPKP----VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDleslrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVelgmqirgrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03228 77 NIAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVM 239
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVL 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
33-249 |
4.36e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.86 E-value: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------ 106
Cdd:PRK09493 2 IEFKNVSKHF------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvderli 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 -QQVAFMLQKDLLMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:PRK09493 76 rQEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 185 DVLLMDEPFSALDAQTKM-VLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHeVLK--VMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAED 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
36-249 |
4.54e-44 |
|
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: 150.19 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA---- 110
Cdd:COG0411 8 RGLTKRF------GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 ---FmlQKDLLMPWRSIQKNVELGMQIRGRS-------------KAERAEVAKA--LLARCHLKGFENHYPHQLSGGMRQ 172
Cdd:COG0411 82 artF--QNPRLFPELTVLENVLVAAHARLGRgllaallrlprarREEREARERAeeLLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 173 RAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF--GRVIAE 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-239 |
1.37e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.04 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 24 PAAAPLpfaIEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLA 98
Cdd:COG4608 2 AMAEPL---LEVRDLKKHFPVRGGlfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 99 GKPVRGPSQQVAFMLQKDLLM----------PWRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLK-GFENHYPHQL 166
Cdd:COG4608 79 GQDITGLSGRELRPLRRRMQMvfqdpyaslnPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 167 SGGMRQRAALARTLAVEPDVLLMDEPFSALD----AQtkmV------LQQDLaqmlaseGKTALMITHDLAEAIALSDRV 236
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ---VlnlledLQDEL-------GLTYLFISHDLSVVRHISDRV 228
|
...
gi 1737829014 237 FVM 239
Cdd:COG4608 229 AVM 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-249 |
2.43e-43 |
|
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: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS--- 106
Cdd:COG2274 473 DIELENVSFRY----PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPAslr 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAL-LARCHlkGFENHYPH-----------QLSGGMRQRA 174
Cdd:COG2274 549 RQIGVVLQDVFLFS-GTIRENITL-----GDPDATDEEIIEAArLAGLH--DFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDK--GRIVED 690
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
34-241 |
2.77e-43 |
|
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: 145.08 E-value: 2.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 34 EYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRgpsqqvafml 113
Cdd:cd00267 1 EIENLSFRYGGR------TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 114 qkdllmpwrsiqknvelgmqiRGRSKAERAEVAkallarchlkgfenhYPHQLSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:cd00267 65 ---------------------KLPLEELRRRIG---------------YVPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737829014 194 SALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd00267 109 SGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
36-253 |
7.79e-43 |
|
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: 146.43 E-value: 7.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA---- 110
Cdd:cd03219 4 RGLTKRF------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIArlgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 ---FmlQKDLLMPWRSIQKNVELGMQIRGRS--------KAERAEVAKA--LLARCHLKGFENHYPHQLSGGMRQRAALA 177
Cdd:cd03219 78 grtF--QIPRLFPELTVLENVMVAAQARTGSglllararREEREARERAeeLLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQtkmvLQQDLAQM---LASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPE----ETEELAELireLRERGITVLLVEHDMDVVMSLADRVTVLDQ--GRVIAEGTPD 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
47-247 |
8.10e-43 |
|
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: 144.50 E-value: 8.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQkdllmpw 121
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSpkelaRKIAYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 rsiqknvelgmqirgrskaeraevakaLLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTK 201
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1737829014 202 MVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD--GRIV 177
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
33-241 |
1.89e-42 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 145.19 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKnrQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ----- 107
Cdd:TIGR02211 2 LKCENLGKRYQ--EGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSnerak 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 ----QVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:TIGR02211 80 lrnkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQT-KMVLqqDLAQMLASEGKTALMI-THDLaEAIALSDRVFVMSE 241
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNaKIIF--DLMLELNRELNTSFLVvTHDL-ELAKKLDRVLEMKD 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-249 |
1.03e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 151.06 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 17 ADARHAQPAAAPLPFAIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSYPGGR-----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 97 LAGKPVRGPS-----QQVAFMLQKDLLMPWrSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKGFENHYPH------- 164
Cdd:COG4988 396 INGVDLSDLDpaswrRQIAWVPQNPYLFAG-TIRENLRL-----GRPDASDEELEAA-LEAAGLDEFVAALPDgldtplg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 ----QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVMs 240
Cdd:COG4988 469 eggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR--LAKGRTVILITHRLA-LLAQADRILVL- 544
|
....*....
gi 1737829014 241 eRPGTIIEE 249
Cdd:COG4988 545 -DDGRIVEQ 552
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-249 |
3.29e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.93 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 17 ADARHAQPAAaPLPFAIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG1132 325 PDPPGAVPLP-PVRGEIEFENVSFSYPGDR-----PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 97 LAGKPVRGPSQ-----QVAFMLQKDLLMPwRSIQKNvelgmqIR-GRSKAERAEVAKAL-LARCH--LKGFENHYPHQ-- 165
Cdd:COG1132 399 IDGVDIRDLTLeslrrQIGVVPQDTFLFS-GTIREN------IRyGRPDATDEEVEEAAkAAQAHefIEALPDGYDTVvg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 -----LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVMS 240
Cdd:COG1132 472 ergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLD 548
|
....*....
gi 1737829014 241 ErpGTIIEE 249
Cdd:COG1132 549 D--GRIVEQ 555
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
54-242 |
3.49e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 141.47 E-value: 3.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP---SEGQVTLAGKPV-RGPSQQ--VAFMLQKDLLMPWRSIQKN 127
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLtALPAEQrrIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 128 VELGMQiRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQD 207
Cdd:COG4136 97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1737829014 208 LAQMLASEGKTALMITHDlAEAIALSDRVFVMSER 242
Cdd:COG4136 176 VFEQIRQRGIPALLVTHD-EEDAPAAGRVLDLGNW 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
33-240 |
4.97e-40 |
|
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: 138.79 E-value: 4.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:cd03263 1 LQIRNLTKTYKK----GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 L----QKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03263 77 LgycpQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMS 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-249 |
2.20e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.96 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL------AGKP---- 101
Cdd:PRK11264 3 AIEVKNLVKKFHGQ------TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSlsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 ---VRGPSQQVAFMLQKDLLMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALA 177
Cdd:PRK11264 77 kglIRQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQtkmVLQQDLAQM--LASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPE---LVGEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQ 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
54-194 |
2.28e-39 |
|
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: 134.70 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLMPWRSIQKNV 128
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENH----YPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
49-242 |
4.37e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.07 E-value: 4.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQVAFMLQKDLLMPWRSI 124
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyrRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QKNVELGMQIRGRSKAERAevAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:COG4133 93 RENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737829014 205 QQDLAQMLAsEGKTALMITHDLAEaiALSDRVFVMSER 242
Cdd:COG4133 171 AELIAAHLA-RGGAVLLTTHQPLE--LAAARVLDLGDF 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-247 |
5.12e-39 |
|
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: 134.48 E-value: 5.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSqqvafm 112
Cdd:cd03216 1 LELRGITKRF------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 lqkdllmPWRSIQKNVELgmqirgrskaeraeVakallarchlkgfenhypHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:cd03216 69 -------PRDARRAGIAM--------------V------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 193 FSAL-DAQTKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII 247
Cdd:cd03216 110 TAALtPAEVERLF--KVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL--RDGRVV 161
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
49-241 |
5.77e-39 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 140.13 E-value: 5.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS--EGQVTLAGKPV-RGPSQQ--VAFMLQKDLLMPWRS 123
Cdd:TIGR03258 16 GANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLtHAPPHKrgLALLFQNYALFPHLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:TIGR03258 96 VEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRAN 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1737829014 204 LQQDLAQMLASEGK-TALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR03258 176 MREEIAALHEELPElTILCVTHDQDDALTLADKAGIMKD 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
56-239 |
9.97e-39 |
|
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: 135.31 E-value: 9.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG------KPVRGPsqqVAFMLQKDLLMPWRSIQKNVE 129
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaaPPADRP---VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 LGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLA 209
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|
gi 1737829014 210 QMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
21-248 |
1.28e-38 |
|
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: 142.60 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 21 HAQPAAAPLPFAIEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK 100
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPG----AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 101 PVRGPS-----QQVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKGFENHYPH----------- 164
Cdd:COG4987 398 DLRDLDeddlrRRIAVVPQRPHLFD-TTLRENLRL-----ARPDATDEELWAA-LERVGLGDWLAALPDgldtwlgeggr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVMSErpG 244
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHRLA-GLERMDRILVLED--G 545
|
....
gi 1737829014 245 TIIE 248
Cdd:COG4987 546 RIVE 549
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
47-225 |
1.34e-38 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 135.15 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 47 GKGEM--TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ--------QVAFMLQKD 116
Cdd:TIGR02982 12 GHGSLrkQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKkqlvqlrrRIGYIFQAH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 LLMPWRSIQKNVELGMQI-RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:TIGR02982 92 NLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAA 171
|
170 180 190
....*....|....*....|....*....|..
gi 1737829014 196 LDAQT-KMVLqqDLAQMLASE-GKTALMITHD 225
Cdd:TIGR02982 172 LDSKSgRDVV--ELMQKLAKEqGCTILMVTHD 201
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
33-249 |
1.41e-38 |
|
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: 135.74 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-----GPSQ 107
Cdd:cd03249 1 IEFKNVSFRYPSRP---DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlnlrWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGmqIRGRSKAERAEVAKalLARCH--LKGFENHY-----PH--QLSGGMRQRAALAR 178
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRYG--KPDATDEEVEEAAK--KANIHdfIMSLPDGYdtlvgERgsQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVMSerPGTIIEE 249
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRLS-TIRNADLIAVLQ--NGQVVEQ 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-249 |
2.01e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 138.66 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 13 AEAYADARHAQPAAAPLpfaIEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLlnmGAGL 87
Cdd:COG4172 259 AEPRGDPRPVPPDAPPL---LEARDLKVWFPIKRGlfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL---GLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 88 YA--PSEGQVTLAGKPVRGPSQQVAFMLQKDL----------LMPWRSIQKNVELGMQI--RGRSKAERAEVAKALLARC 153
Cdd:COG4172 333 LRliPSEGEIRFDGQDLDGLSRRALRPLRRRMqvvfqdpfgsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 154 HLK-GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDaqtkMVLQQDLAQMLAS----EGKTALMITHDLAE 228
Cdd:COG4172 413 GLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDLLRDlqreHGLAYLFISHDLAV 488
|
250 260
....*....|....*....|.
gi 1737829014 229 AIALSDRVFVMSErpGTIIEE 249
Cdd:COG4172 489 VRALAHRVMVMKD--GKVVEQ 507
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-248 |
2.03e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 135.74 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTrrfKNRQGKGEmtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQ- 108
Cdd:PRK11650 3 GLKLQAVR---KSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVneLEPADRd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAER----AEVAKALlarcHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIeervAEAARIL----ELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 185 DVLLMDEPFSALDAQTK--MVLQ-QDLAQMLaseGKTALMITHDLAEAIALSDRVFVMS----ERPGTIIE 248
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRvqMRLEiQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNggvaEQIGTPVE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
33-252 |
2.11e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 135.31 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV--------TLAGKPVRG 104
Cdd:PRK11153 2 IELKNISKVF--PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 185 DVLLMDEPFSALDAQ-TKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV 252
Cdd:PRK11153 160 KVLLCDEATSALDPAtTRSILEL-LKDINRELGLTIVLITHEMDVVKRICDRVAVIDA--GRLVEQGTV 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
32-239 |
1.45e-36 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 129.63 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRQGKgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS--- 106
Cdd:cd03245 2 RIEFRNVSFSYPNQEIP----ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPAdlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFMLQkDLLMPWRSIQKNVELGMQIrgrskAERAEVAKAL-------LARCHLKGF-----ENHYphQLSGGMRQRA 174
Cdd:cd03245 78 RNIGYVPQ-DVTLFYGTLRDNITLGAPL-----ADDERILRAAelagvtdFVNKHPNGLdlqigERGR--GLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVM 239
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVM 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
33-225 |
1.52e-36 |
|
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: 129.45 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAF 111
Cdd:cd03292 1 IEFINVTKTYPN-----GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 M-------LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03292 76 LrrkigvvFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 185 DVLLMDEPFSALDAQTK---MVLQQDLAQMlaseGKTALMITHD 225
Cdd:cd03292 156 TILIADEPTGNLDPDTTweiMNLLKKINKA----GTTVVVATHA 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
53-253 |
1.76e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 134.39 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQKDLLMPWRS 123
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737829014 204 LQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN--GEVVQVGTPD 250
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
33-253 |
2.30e-36 |
|
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: 129.41 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV--- 109
Cdd:cd03265 1 IEVENLVKKY------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVrrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 -AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03265 75 iGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH--GRIIAEGTPE 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
33-257 |
4.24e-36 |
|
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: 129.22 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV--------TLAGKPVRG 104
Cdd:cd03256 1 IEVENLSKTYPN--GK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGM--------QIRGR-SKAERaEVAKALLARCHLKGFENHYPHQLSGGMRQRAA 175
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII-----EEI 250
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRIVfdgppAEL 232
|
....*..
gi 1737829014 251 TVDLPHR 257
Cdd:cd03256 233 TDEVLDE 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
33-250 |
4.48e-36 |
|
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: 128.10 E-value: 4.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---RGPSQQV 109
Cdd:cd03268 1 LKTNDLTKTYGKKR------VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqknIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVakalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 190 DEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEI 250
Cdd:cd03268 151 DEPTNGLDPDGIKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINK--GKLIEEG 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
56-241 |
8.87e-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: 131.38 E-value: 8.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RG---PSQQ--VAFMLQKDLLMPWRSIQK 126
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGiflPPHRrrIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQ--IRGRSKAERAEVAK-----ALLARchlkgfenhYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:COG4148 97 NLLYGRKraPRAERRISFDEVVEllgigHLLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737829014 200 TKMVLQQDLAQmLASEGKT-ALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4148 168 RKAEILPYLER-LRDELDIpILYVSHSLDEVARLADHVVLLEQ 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
49-239 |
2.13e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 130.53 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQ-VAFMLQKDLLMPWRSIQ 125
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvpPAERgVGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVELGMQIRGRSKAE---RAEVAKALLARCHLKgfeNHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM 202
Cdd:PRK11000 94 ENMSFGLKLAGAKKEEinqRVNQVAEVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1737829014 203 VLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
49-286 |
2.27e-35 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 129.05 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RGPSQQVAFMLQK----DLLMP 120
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvrepRKVRRSIGIVPQYasvdEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 121 WrsiqKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:TIGR01188 84 R----ENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 201 KMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV-DLPHR----------DNPIERRKQAGM 269
Cdd:TIGR01188 160 RRAI-WDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDH--GRIIAEGTPeELKRRlgkdtlesrpRDIQSLKVEVSM 236
|
250
....*....|....*....
gi 1737829014 270 --NEYVAHLMELLKVGRDD 286
Cdd:TIGR01188 237 liAELGETGLGLLAVTVDS 255
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
49-248 |
2.87e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 127.05 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----------KPVRGPSQQVAFMLQKDL 117
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPWRSIQKN-VELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK11124 93 LWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 197 DAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK11124 173 DPEiTAQIV--SIIRELAETGITQVIVTHEVEVARKTASRVVYMEN--GHIVE 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-249 |
5.31e-35 |
|
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: 126.19 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:cd03251 1 VEFKNVTFRY----PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQkDLLMPWRSIQKNVELgmqirGRSKAERAEVAKAL-LARCH--LKGFENHYPH-------QLSGGMRQRAALA 177
Cdd:cd03251 77 QIGLVSQ-DVFLFNDTVAENIAY-----GRPGATREEVEEAArAANAHefIMELPEGYDTvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLS-TIENADRIVVLED--GKIVER 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
52-241 |
6.16e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.77 E-value: 6.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAFML-----QKDLLMPWRSIQ 125
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRRavlpqHSSLAFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KnVELGMQIRGRSKAERAEVAKALLARCHLKGFEN-HYPhQLSGGMRQRAALARTLA-------VEPDVLLMDEPFSALD 197
Cdd:COG4559 95 V-VALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737829014 198 -AQTKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4559 173 lAHQHAVLR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQ 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
61-241 |
1.03e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.46 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQVAFML-QKDLLMPWRSIQKNVELGMQIRGR 137
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtpPSRRPVSMLfQENNLFSHLTVAQNIGLGLNPGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGK 217
Cdd:PRK10771 102 LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQL 181
|
170 180
....*....|....*....|....
gi 1737829014 218 TALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10771 182 TLLMVSHSLEDAARIAPRSLVVAD 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-241 |
1.38e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 125.65 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA 110
Cdd:PRK13548 2 MLEARNLSVRLGGR------TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 FML-----QKDLLMPWrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLA---- 181
Cdd:PRK13548 76 RRRavlpqHSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 182 --VEPDVLLMDEPFSALD-AQTKMVLQqdLAQMLASEGKTA-LMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDlAHQHHVLR--LARQLAHERGLAvIVVLHDLNLAARYADRIVLLHQ 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-272 |
1.68e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 126.38 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVA 110
Cdd:COG4152 1 MLELKGLTKRF------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 FMLQKdllmpwRSIQKNVELGMQI------RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG4152 75 YLPEE------RGLYPKMKVGEQLvylarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 185 DVLLMDEPFSALD--AQTKMVlqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDlphrdnpiE 262
Cdd:COG4152 149 ELLILDEPFSGLDpvNVELLK---DVIRELAAKGTTVIFSSHQMELVEELCDRIVIINK--GRKVLSGSVD--------E 215
|
250
....*....|
gi 1737829014 263 RRKQAGMNEY 272
Cdd:COG4152 216 IRRQFGRNTL 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
58-241 |
2.54e-34 |
|
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: 123.82 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 58 SIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQ-VAFMLQKDLLMPWRSIQKNVELGMQI 134
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGlaPYQRpVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAS 214
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180
....*....|....*....|....*..
gi 1737829014 215 EGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQ 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
53-249 |
3.56e-34 |
|
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: 123.87 E-value: 3.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLMPwRSIQKN 127
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslrSMIGVVLQDTFLFS-GTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 128 VELgmqirGRSKAERAEVAKAL-LARCHL------KGFE---NHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:cd03254 97 IRL-----GRPNATDEEVIEAAkEAGAHDfimklpNGYDtvlGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 198 AQTKMVLQQDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03254 172 TETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDD--GKIIEE 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
33-239 |
7.95e-34 |
|
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: 122.39 E-value: 7.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-GPSQQVAF 111
Cdd:cd03269 1 LEVENVTKRF------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737829014 192 PFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
49-249 |
8.01e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.20 E-value: 8.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----------KPVRGPSQQVAFMLQKDL 117
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPWRSIQKN-VELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:COG4161 93 LWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 197 DAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG4161 173 DPEiTAQVV--EIIRELSQTGITQVIVTHEVEFARKVASQVVYMEK--GRIIEQ 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-248 |
1.01e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.22 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 24 PAAAPLPFAIEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLL---N-MGAgLYaPS---EGQVT 96
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQ------ALKDINLDIPENKVTALIGPSGCGKSTLLrclNrMND-LI-PGarvEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 97 LAGKPVRGPS-------QQVAFMLQKDLLMPWrSIQKNVELGMQIRG-RSKAERAEVAKALLARCHL----KGFENHYPH 164
Cdd:COG1117 75 LDGEDIYDPDvdvvelrRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALwdevKDRLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ-TKMVlqQDLAQMLASEgKTALMITHDLAEAIALSDRVFVMSErp 243
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKI--EELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYL-- 228
|
....*
gi 1737829014 244 GTIIE 248
Cdd:COG1117 229 GELVE 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-278 |
1.60e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP--------VRg 104
Cdd:PRK13635 6 IRVEHISFRYPD----AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdVR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 psQQVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK13635 81 --RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVMSE-------------RPGTIIEEI 250
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKgeileegtpeeifKSGHMLQEI 237
|
250 260
....*....|....*....|....*...
gi 1737829014 251 TVDLPHRDNPIERRKQAGMNEYVAHLME 278
Cdd:PRK13635 238 GLDVPFSVKLKELLKRNGILLPNTYLTM 265
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-253 |
3.56e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----- 106
Cdd:COG1129 4 LLEMRGISKSF------GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 -QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRS----KAERAEvAKALLAR--CHLKgfenhyPHQ----LSGGMRQRAA 175
Cdd:COG1129 78 aAGIAIIHQELNLVPNLSVAENIFLGREPRRGGlidwRAMRRR-ARELLARlgLDID------PDTpvgdLSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EE 249
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEReVERLF--RIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL--RDGRLVgtgpvAE 226
|
....
gi 1737829014 250 ITVD 253
Cdd:COG1129 227 LTED 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
52-236 |
3.80e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.03 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTlagkpvRGPSQQVAFMLQK---DLLMPWRSIQKnV 128
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRsevPDSLPLTVRDL-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGM-QIRGR----SKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:NF040873 79 AMGRwARRGLwrrlTRDDRAAVDDAL-ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|...
gi 1737829014 204 LQQDLAQmLASEGKTALMITHDLaEAIALSDRV 236
Cdd:NF040873 158 IIALLAE-EHARGATVVVVTHDL-ELVRRADPC 188
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-239 |
4.36e-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: 127.02 E-value: 4.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 24 PAAAPLPFAIEYRGVTRRFKnrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR 103
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYP-----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 104 GPSQ-----QVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKGFENHYP-----------HQLS 167
Cdd:TIGR02857 388 DADAdswrdQIAWVPQHPFLFA-GTIAENIRL-----ARPDASDAEIREA-LERAGLDEFVAALPqgldtpigeggAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVM 239
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA--LAQGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-241 |
6.29e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 122.61 E-value: 6.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----Q 107
Cdd:PRK13537 7 PIDFRNVEKRY------GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRArharQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVL 187
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMLASeGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
30-285 |
1.18e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.14 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 30 PFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV 109
Cdd:COG3845 3 PPALELRGITKRF------GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 A-----------FMLQKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFE---NHYPHQLSGGMRQRAA 175
Cdd:COG3845 77 AialgigmvhqhFMLVPNL-----TVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVdlp 255
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVL--RRGKVVGTVDT--- 225
|
250 260 270
....*....|....*....|....*....|
gi 1737829014 256 hrdnpierrKQAGMNEyVAHLMellkVGRD 285
Cdd:COG3845 226 ---------AETSEEE-LAELM----VGRE 241
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-251 |
1.25e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.58 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFkNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF 111
Cdd:COG1101 2 LELKNLSKTF-NPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 ML----QkDLLM---PWRSIQKNVELGMQiRGRS--------KAERAEVaKALLARCHLkGFENHYPHQ---LSGGMRQR 173
Cdd:COG1101 81 YIgrvfQ-DPMMgtaPSMTIEENLALAYR-RGKRrglrrgltKKRRELF-RELLATLGL-GLENRLDTKvglLSGGQRQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 174 AALARTLAVEPDVLLMDEPFSALDAQT-KMVLqqDLAQMLASEGK-TALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTaALVL--ELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHE--GRIILDVS 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-239 |
1.89e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 122.00 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFKNRQG--KGEMT--AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:PRK11308 9 IDLKKHYPVKRGlfKPERLvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLM----------PWRSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKG-FENHYPHQLSGGMRQRAALART 179
Cdd:PRK11308 89 LLRQKIQIvfqnpygslnPRKKVGQILEEPLLINTSlSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 180 LAVEPDVLLMDEPFSALD----AQT---KMVLQQDLaqmlaseGKTALMITHDLA--EAIAlsDRVFVM 239
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDvsvqAQVlnlMMDLQQEL-------GLSYVFISHDLSvvEHIA--DEVMVM 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
33-253 |
2.00e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.80 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF 111
Cdd:COG4604 2 IEIKNVSKRY------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLqkdllmpwrSI--QKNVeLGMQI--------------RGRSKAE-RAEVAKAlLARCHLKGFENHYPHQLSGGMRQRA 174
Cdd:COG4604 76 RL---------AIlrQENH-INSRLtvrelvafgrfpysKGRLTAEdREIIDEA-IAYLDLEDLADRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALD---AQTKMVLQQDLAQMLaseGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEIT 251
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmkhSVQMMKLLRRLADEL---GKTVVIVLHDINFASCYADHIVAM--KDGRVVAQGT 219
|
..
gi 1737829014 252 VD 253
Cdd:COG4604 220 PE 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
33-252 |
2.01e-32 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 120.30 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNR---QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPSQ 107
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFmlQKDLLM----------PWRSIQKNVELGMQ-IRGRSKAERAEVAKALLARCHLKG-FENHYPHQLSGGMRQRAA 175
Cdd:TIGR02769 83 RRAF--RRDVQLvfqdspsavnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV 252
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQIVEECDV 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
49-249 |
2.30e-32 |
|
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: 118.69 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ-----VAFMLQKDLLMPWR 122
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHEraragIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERA-EVAKALLARchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALdaQTK 201
Cdd:cd03224 91 TVEENLLLGAYARRRAKRKARlERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL--APK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1737829014 202 MVLQ-QDLAQMLASEGKTALMITHDLAEAIALSDRVFVMsERpGTIIEE 249
Cdd:cd03224 167 IVEEiFEAIRELRDEGVTILLVEQNARFALEIADRAYVL-ER-GRVVLE 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
47-240 |
2.77e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.73 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQQVAFMLQKDLLMPW 121
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssRQLARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELG----MQIRGR-SKAERAEVAKAlLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK11231 91 ITVRELVAYGrspwLSLWGRlSAEDNARVNQA-MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 197 DAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK11231 170 DINHQVEL-MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
59-242 |
3.34e-32 |
|
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: 118.41 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 59 IGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQK-----DLLMPWRSIQKNVELGM- 132
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRhefawDFPISVAHTVMSGRTGHi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 -QIRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQM 211
Cdd:TIGR03771 81 gWLRRPCVADFAAVRDAL-RRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TELFIE 158
|
170 180 190
....*....|....*....|....*....|.
gi 1737829014 212 LASEGKTALMITHDLAEAIALSDRVFVMSER 242
Cdd:TIGR03771 159 LAGAGTAILMTTHDLAQAMATCDRVVLLNGR 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
33-249 |
3.41e-32 |
|
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: 118.87 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTrrFKNRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQvafM 112
Cdd:cd03253 1 IEFENVT--FAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD---S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLM-PWRSIQKNVELGMQIR-GRSKAERAEV-AKALLARCH--LKGFENHYPHQ-------LSGGMRQRAALARTL 180
Cdd:cd03253 73 LRRAIGVvPQDTVLFNDTIGYNIRyGRPDATDEEViEAAKAAQIHdkIMRFPDGYDTIvgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEaIALSDRVFVMSErpGTIIEE 249
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST-IVNADKIIVLKD--GRIVER 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
33-253 |
5.12e-32 |
|
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: 118.41 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---------- 102
Cdd:cd03218 1 LRAENLSKRYGKRK------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhkrar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 103 RG----PSQQVAFmlqKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALAR 178
Cdd:cd03218 75 LGigylPQEASIF---RKL-----TVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQdLAQMLASEGkTALMIT-HDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQK-IIKILKDRG-IGVLITdHNVRETLSITDRAYIIYE--GKVLAEGTPE 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
46-225 |
7.41e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.96 E-value: 7.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 46 QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG---------PSQQVAFMLQKD 116
Cdd:PRK10584 18 QGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearaklRAKHVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 LLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK10584 98 MLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180
....*....|....*....|....*....
gi 1737829014 197 DAQTKMVLQQDLAQMLASEGKTALMITHD 225
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
53-289 |
1.02e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.64 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-------GPSQQVAFMLQK---DLLMPwr 122
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIVFQNpddQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD---AQ 199
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgAS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 200 TKMVLQQDLAQmlasEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDnpIERRKQAGMN-EYVAHLME 278
Cdd:PRK13639 175 QIMKLLYDLNK----EGITIIISTHDVDLVPVYADKVYVMSD--GKIIKEGTPKEVFSD--IETIRKANLRlPRVAHLIE 246
|
250
....*....|.
gi 1737829014 279 LLKvgRDDHLG 289
Cdd:PRK13639 247 ILN--KEDNLP 255
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
52-269 |
1.84e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.17 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQVAFmlQKDLLM---------- 119
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAF--RRDIQMvfqdsisavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQ-IRGRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK10419 104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 198 aqtkMVLQQDLAQMLAS---EGKTA-LMITHDLAEAIALSDRVFVMSErpGTIIEEITV-DLPHRDNPIERRKQAGM 269
Cdd:PRK10419 184 ----LVLQAGVIRLLKKlqqQFGTAcLFITHDLRLVERFCQRVMVMDN--GQIVETQPVgDKLTFSSPAGRVLQNAV 254
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
36-249 |
1.98e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 114.36 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----------RGp 105
Cdd:COG1137 7 ENLVKSYGKR------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 sqqVAFMLQ-----KDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTL 180
Cdd:COG1137 80 ---IGYLPQeasifRKL-----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 181 AVEPDVLLMDEPF------SALDAQtKMVLQqdlaqmLASEGkTALMIT-HDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG1137 152 ATNPKFILLDEPFagvdpiAVADIQ-KIIRH------LKERG-IGVLITdHNVRETLGICDRAYIISE--GKVLAE 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
44-241 |
2.61e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 113.12 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 44 NRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAFMLQKD----LL 118
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKERRKSIGYVMQDvdyqLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MpwrsiqKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:cd03226 86 T------DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737829014 199 QtKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03226 160 K-NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
45-249 |
6.84e-30 |
|
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: 117.86 E-value: 6.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 45 RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKS----TLLNMGAGLYAPSEGQVTLAGKP-----------VRGpsQQV 109
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllglserelrrIRG--NRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDL--LMPWRSIQKNVELGMQI-RGRSKAERAEVAKALLARCHLKGFE---NHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG4172 95 AMIFQEPMtsLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALD----AQtkmVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:COG4172 175 PDLLIADEPTTALDvtvqAQ---ILDL-LKDLQRELGMALLLITHDLGVVRRFADRVAVM--RQGEIVEQ 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-249 |
1.12e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.54 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 18 DARHAQPAAAPlPFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL 97
Cdd:PRK13536 28 EAKASIPGSMS-TVAIDLAGVSKSY------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 98 AGKPV----RGPSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQR 173
Cdd:PRK13536 101 LGVPVparaRLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 174 AALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAsEGKTALMITHDLAEAIALSDRVFVMSE-------RPGTI 246
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAgrkiaegRPHAL 259
|
...
gi 1737829014 247 IEE 249
Cdd:PRK13536 260 IDE 262
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
33-239 |
1.13e-29 |
|
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: 110.38 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS---Q 107
Cdd:cd03246 1 LEVENVSFRY----PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNelgD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVelgmqirgrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03246 77 HVGYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMLASeGKTALMITHDLaEAIALSDRVFVM 239
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVL 168
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-251 |
1.27e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 117.90 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:TIGR00958 479 IEFQDVSFSYPNRP---DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirgrsKAERAEV-AKALLARCH--LKGFENHY-----PH--QLSGGMRQRAALA 177
Cdd:TIGR00958 556 QVALVGQEPVLFS-GSVRENIAYGLT-----DTPDEEImAAAKAANAHdfIMEFPNGYdtevgEKgsQLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEEIT 251
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAHRLS-TVERADQILVLKK--GSVVEMGT 696
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-239 |
1.52e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 114.44 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 41 RFKNRQGKGEMtavsDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGPSQQ--VAF 111
Cdd:TIGR02142 4 RFSKRLGDFSL----DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEKrrIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGM-QIRGRSKAERAEVAKALLARCHLKGfenHYPHQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGMkRARPSERRISFERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1737829014 191 EPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
53-241 |
3.10e-29 |
|
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: 109.44 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFML---------QKDLLMPWRS 123
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELgmqirgrskaeraevakallarchlkgfenhyPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737829014 204 LQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03215 143 IYR-LIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
43-252 |
4.52e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 110.68 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 43 KNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFML 113
Cdd:PRK11629 14 RYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaelrnQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 114 QKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:PRK11629 94 QFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 194 SALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVfvmSERPGTIIEEITV 252
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL---EMRDGRLTAELSL 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
33-258 |
7.66e-29 |
|
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: 115.20 E-value: 7.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRqgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:TIGR02203 331 VEFRNVTFRYPGR----DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslrR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQkDLLMPWRSIQKNVELGmqirGRSKAERAEVAKALLArCHLKGFENHYP---HQ--------LSGGMRQRAAL 176
Cdd:TIGR02203 407 QVALVSQ-DVVLFNDTIANNIAYG----RTEQADRAEIERALAA-AYAQDFVDKLPlglDTpigengvlLSGGQRQRLAI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEEIT-VDLP 255
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLS-TIEKADRIVVMDD--GRIVERGThNELL 555
|
...
gi 1737829014 256 HRD 258
Cdd:TIGR02203 556 ARN 558
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
33-249 |
8.43e-29 |
|
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: 109.88 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:cd03252 1 ITFEHVRFRYK----PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpawlrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirGRSKAERAEVAKalLARCHL------KGFENHYPHQ---LSGGMRQRAALAR 178
Cdd:cd03252 77 QVGVVLQENVLFN-RSIRDNIALADP--GMSMERVIEAAK--LAGAHDfiselpEGYDTIVGEQgagLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEK--GRIVEQ 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
49-249 |
1.07e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.44 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP---VRGPSQQVAF-------MLQKDLL 118
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlVRDKDGQLKVadknqlrLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MPWR--------SIQKNV-ELGMQIRGRSKAERAEVAKALLARCHLKG-FENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK10619 96 MVFQhfnlwshmTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 189 MDEPFSALDAQ-TKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK10619 176 FDEPTSALDPElVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQ--GKIEEE 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
39-249 |
1.21e-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: 109.16 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 39 TRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFmlQKDLl 118
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGF--NPEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 mpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFEN----HYphqlSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:cd03220 100 ----TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDlpvkTY----SSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 195 ALDAQTKMVLQQDLAQMLaSEGKTALMITHDLAEAIALSDRVFVMsERpGTIIEE 249
Cdd:cd03220 172 VGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVL-EK-GKIRFD 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-253 |
1.26e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 114.67 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 19 ARHAQPAAAPLPF---AIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV 95
Cdd:PRK13657 318 DVRDPPGAIDLGRvkgAVEFDDVSFSYDNSR-----QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 96 TLAGKPVRGPS-----QQVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAL-LARCH------LKGFENHYP 163
Cdd:PRK13657 393 LIDGTDIRTVTraslrRNIAVVFQDAGLFN-RSIEDNIRV-----GRPDATDEEMRAAAeRAQAHdfierkPDGYDTVVG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 164 H---QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVMS 240
Cdd:PRK13657 467 ErgrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFD 543
|
250
....*....|...
gi 1737829014 241 ErpGTIIEEITVD 253
Cdd:PRK13657 544 N--GRVVESGSFD 554
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-253 |
1.90e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.02 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFK----------------NRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV 95
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 96 TLAGKpvrgpsqqVAFML------QKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFEN----HYphq 165
Cdd:COG1134 84 EVNGR--------VSALLelgagfHPEL-----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDqpvkTY--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 lSGGMRQRAALARTLAVEPDVLLMDEPFSALDA--QTKMvlqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErp 243
Cdd:COG1134 148 -SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafQKKC---LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK-- 221
|
250
....*....|
gi 1737829014 244 GTIIEEITVD 253
Cdd:COG1134 222 GRLVMDGDPE 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
33-260 |
2.78e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.92 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAF 111
Cdd:PRK11300 6 LSVSGLMMRF------GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 M----------LQKD-------LLMPWRSIQKNVELGM----QIRgRSKAERAEVAKALLARCHLKGFENHYPHQLSGGM 170
Cdd:PRK11300 80 MgvvrtfqhvrLFREmtvienlLVAQHQQLKTGLFSGLlktpAFR-RAESEALDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 171 RQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII--- 247
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ--GTPLang 236
|
250
....*....|....*
gi 1737829014 248 --EEItvdlphRDNP 260
Cdd:PRK11300 237 tpEEI------RNNP 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
33-239 |
2.79e-28 |
|
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: 108.22 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV--- 109
Cdd:cd03266 2 ITADALTKRFRDV--KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEArrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 -AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03266 80 lGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
49-241 |
3.10e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.86 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQQVAFMLQKDLLMPWRS 123
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQI-RGR----SKAERAEVAKAlLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK09536 94 VRQVVEMGRTPhRSRfdtwTETDRAAVERA-MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737829014 199 QtKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK09536 173 N-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLAD 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
53-239 |
3.29e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.57 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKDLLM----PWRSIQKNV 128
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMifqdPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGmQIRGR---------SKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD- 197
Cdd:PRK15079 116 TIG-EIIAEplrtyhpklSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDv 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737829014 198 ---AQTKMVLQQDLAQMlaseGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK15079 195 siqAQVVNLLQQLQREM----GLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-247 |
5.40e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 106.48 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAGLYAPSEGQVTLAGKPV--RGPSQQ 108
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNalAGRRTGLGVSGEVLINGRPLdkRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 189 MDEPFSALDAQTK---MVLQQDLAQMlaseGKTALMITHDL-AEAIALSDRVFVMSerPGTII 247
Cdd:cd03213 135 LDEPTSGLDSSSAlqvMSLLRRLADT----GRTIICSIHQPsSEIFELFDKLLLLS--QGRVI 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
50-249 |
5.95e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 105.86 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP----SQQVAFMLQKDLLMPwRSIQ 125
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLekalSSLISVLNQRPYLFD-TTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVelgmqirGRskaeraevakallarchlkgfenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQ 205
Cdd:cd03247 93 NNL-------GR---------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 206 QDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03247 139 SLIFEVL--KDKTLIWITHHLT-GIEHMDKILFLEN--GKIIMQ 177
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
33-236 |
6.05e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.90 E-value: 6.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---------R 103
Cdd:PRK10535 5 LELKDIRRSYPS--GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadalaQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 104 GPSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAiALSDRV 236
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVA-AQAERV 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
37-247 |
8.99e-28 |
|
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: 106.97 E-value: 8.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 37 GVTRRFKNrQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGL---YAPSEGQVTLAGKPV-RGPSQQ-VAF 111
Cdd:cd03234 8 DVGLKAKN-WNK-YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRkPDQFQKcVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGR----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPrkssDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHD-LAEAIALSDRVFVMSErpGTII 247
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQ-LARRNRIVILTIHQpRSDLFRLFDRILLLSS--GEIV 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
49-244 |
1.28e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLMPwRS 123
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyrQQVSYCAQTPTLFG-DT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKalLARCHL------KGFEnhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDPAIFLDD--LERFALpdtiltKNIA-----ELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1737829014 198 AQTKMVLQQDLAQMLASEGKTALMITHDLAEaIALSDRVFVMSERPG 244
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAG 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
33-241 |
1.32e-27 |
|
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: 106.36 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFK--NRQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL--AGKPV---RGP 105
Cdd:COG4778 5 LEVENLSKTFTlhLQGGK-RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 SQQVAFMLQKDL--------LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKgfEN---HYPHQLSGGMRQRA 174
Cdd:COG4778 84 PREILALRRRTIgyvsqflrVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLP--ERlwdLPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
33-241 |
2.45e-27 |
|
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: 105.63 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQ 107
Cdd:cd03248 12 VKFQNVTFAYPTRP---DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyehKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirGRSKAERAEVAKALLARCHLKGFENHYP-------HQLSGGMRQRAALARTL 180
Cdd:cd03248 89 KVSLVGQEPVLFA-RSLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRL-STVERADQILVLDG 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
32-255 |
3.06e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.61 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrgpSQQVAF 111
Cdd:PRK13632 7 MIKVENVSFSYPN----SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWR---------SIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK13632 80 EIRKKIGIIFQnpdnqfigaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIaLSDRVFVMSE----RPGT---------IIEE 249
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgkliAQGKpkeilnnkeILEK 238
|
....*.
gi 1737829014 250 ITVDLP 255
Cdd:PRK13632 239 AKIDSP 244
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
53-253 |
3.17e-27 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 105.53 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP----SEGQVTLAGKPVRGP---SQQVAFMLQ--KDLLMPWRS 123
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLsirGRHIATIMQnpRTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGR-SKAERAEVAKALLARC--HLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:TIGR02770 81 MGNHAIETLRSLGKlSKQARALILEALEAVGlpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 201 KMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIVERGTVK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
33-239 |
9.94e-27 |
|
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: 103.70 E-value: 9.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQGKGEMTaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvrgpsqqVAFM 112
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFT-LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKdllmPW---RSIQKNVELGMQIRgrskAER-AEVAKAllarCHL-KGFENhYPHQ-----------LSGGMRQRAAL 176
Cdd:cd03250 72 SQE----PWiqnGTIRENILFGKPFD----EERyEKVIKA----CALePDLEI-LPDGdlteigekginLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQT-KMVLQQDLAQMLAsEGKTALMITHDLaEAIALSDRVFVM 239
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLL-NNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-226 |
1.02e-26 |
|
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: 108.99 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 3 RSIQLKDANVAEAYADArHAQPAAAPLPFAIEYRGVTRRFKnrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN 82
Cdd:TIGR02868 306 RIVEVLDAAGPVAEGSA-PAAGAVGLGKPTLELRDLSAGYP-----GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 83 MGAGLYAPSEGQVTLAGKPVRGPSQQ-----VAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKG 157
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVPVSSLDQDevrrrVSVCAQDAHLFD-TTVRENLRL-----ARPDATDEELWAA-LERVGLAD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 158 FENHYPH-----------QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDL 226
Cdd:TIGR02868 453 WLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA--ALSGRTVVLITHHL 530
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
33-247 |
2.27e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.17 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFkNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT-------LAGKPVRGP 105
Cdd:PRK13651 3 IKVKNIVKIF-NKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdekNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 SQQVAFMLQKDLLMPWR-----------------------SIQKNVELGMQIRGRSKAERAEVAKALLarcHLKGFENHY 162
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYI---ELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 163 ----PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVF 237
Cdd:PRK13651 159 lqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEIL--EIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|
gi 1737829014 238 VMSErpGTII 247
Cdd:PRK13651 237 FFKD--GKII 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
32-247 |
2.54e-26 |
|
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: 103.63 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRfknRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQ-VTLAGKPVRGPSqqva 110
Cdd:COG1119 3 LLELRNVTVR---RGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 fmlqkdllmpWRSIQKNV-----ELGMQIRGRSKAERA--------------------EVAKALLARCHLKGFENHYPHQ 165
Cdd:COG1119 73 ----------VWELRKRIglvspALQLRFPRDETVLDVvlsgffdsiglyreptdeqrERARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGT 245
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGR 220
|
..
gi 1737829014 246 II 247
Cdd:COG1119 221 VV 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
49-253 |
2.77e-26 |
|
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: 103.14 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ-----VAFMLQKDLLMPWR 122
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlPPHRiarlgIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERAEVAK--ALLARchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALdaQT 200
Cdd:COG0410 94 TVEENLLLGAYARRDRAEVRADLERvyELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL--AP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 201 KMVlqQDLAQM---LASEGKTALMITHDLAEAIALSDRVFVMsERpGTIIEEITVD 253
Cdd:COG0410 170 LIV--EEIFEIirrLNREGVTILLVEQNARFALEIADRAYVL-ER-GRIVLEGTAA 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
53-281 |
5.52e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.77 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrGPSQQVAFMLQKDLLMPWR---------S 123
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQdpdnqlfsaS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 204 LQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIERRKQAGMNEyVAHLMELLK 281
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE--GRVILQGNPKEVFAEKEMLRKVNLRLPR-IGHLMEILK 254
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
33-241 |
6.28e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 103.27 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----KPVRGPSQ 107
Cdd:PRK13650 5 IEVKNLTFKYKEDQ---EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDV 186
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 187 LLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEaIALSDRVFVMSE 241
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKN 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
55-225 |
1.15e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELGMQI 134
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLRIGYLPQEPPLDDDLTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSKAERAEVAKAL---------LARCHLK--------------------GFENHYPHQ----LSGGMRQRAALARTLA 181
Cdd:COG0488 89 LRALEAELEELEAKLaepdedlerLAELQEEfealggweaearaeeilsglGFPEEDLDRpvseLSGGWRRRVALARALL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 182 VEPDVLLMDEPFSALDAQTKMVLQqdlaQMLASEGKTALMITHD 225
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLESIEWLE----EFLKNYPGTVLVVSHD 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
53-241 |
1.16e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.51 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ-----VAFMLQK-DLLMPWRSIQK 126
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrskVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:PRK13647 100 DVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1737829014 207 DLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13647 180 ILDR-LHNQGKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
53-251 |
1.32e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQVA---FMLQKD-----LLMPwR 122
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVriRSPRDAIRagiAYVPEDrkgegLVLD-L 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGR-----SKAERAEVAKALLARCHLKGfenHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:COG1129 346 SIRENITLASLDRLSrggllDRRRERALAEEYIKRLRIKT---PSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 194 SALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:COG1129 423 RGIDVGAKAEIYRLIRE-LAAEGKAVIVISSELPELLGLSDRILVMRE--GRIVGELD 477
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-255 |
1.93e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.19 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQ--------VTLAGKPVR 103
Cdd:PRK13640 5 IVEFKHVSFTYPD----SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 104 GPSQQVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVM-------SERPGTI------IEE 249
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLddgkllaQGSPVEIfskvemLKE 239
|
....*.
gi 1737829014 250 ITVDLP 255
Cdd:PRK13640 240 IGLDIP 245
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-236 |
4.48e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.30 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 31 FAIEyrgvTRRFKNRQGKGEMtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-----APSEGQVTLAGKPVRGP 105
Cdd:PRK14267 3 FAIE----TVNLRVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 S-------QQVAFMLQKDLLMPWRSIQKNVELGMQIRG--RSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQ 172
Cdd:PRK14267 77 DvdpievrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 173 RAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRV 236
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYV 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
33-247 |
5.70e-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: 99.71 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQGKG---------------EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL 97
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 98 AGkpVRGPSQQVAFMLQKDLLMPWRS-------IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGM 170
Cdd:cd03267 81 AG--LVPWKRRKKFLRRIGVVFGQKTqlwwdlpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 171 RQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK--GRLL 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-197 |
6.66e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 104.44 E-value: 6.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 24 PAAAPLPFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV- 102
Cdd:NF033858 258 PADDDDEPAIEARGLTMRF------GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVd 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 103 ------RgpsQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAAL 176
Cdd:NF033858 332 agdiatR---RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSL 408
|
170 180
....*....|....*....|...
gi 1737829014 177 ArtLAV--EPDVLLMDEPFSALD 197
Cdd:NF033858 409 A--VAVihKPELLILDEPTSGVD 429
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
57-248 |
7.63e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 57 VSIGIKAGEFVSLIGPSGCGKSTLLNMGAGlYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLmPWRSIQKNVELG 131
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDpeswrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 132 mqirgRSKAERAEVaKALLARCHLKGFENHYPH-----------QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK11174 447 -----NPDASDEQL-QQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737829014 201 KMVLQQDLAQmlASEGKTALMITHDLaEAIALSDRVFVMseRPGTIIE 248
Cdd:PRK11174 521 EQLVMQALNA--ASRRQTTLMVTHQL-EDLAQWDQIWVM--QDGQIVQ 563
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
33-241 |
1.09e-24 |
|
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: 98.42 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVsLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---- 108
Cdd:cd03264 1 LQLENLTKRYGKKR------ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
49-234 |
1.26e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.47 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL---NMGAGLY--APSEGQVTLAGKPVRGPS-------QQVAFMLQKD 116
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIpgFRVEGKVTFHGKNLYAPDvdpvevrRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 LLMPwRSIQKNVELGMQIRGrSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK14243 101 NPFP-KSIYDNIAYGARING-YKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSD 234
Cdd:PRK14243 179 CSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-266 |
2.63e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 98.68 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRfknrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:PRK11831 8 VDMRGVSFT------RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRS--------IQKNVELGMQIRGRSKAE--RAEVAKALLArCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK11831 82 VRKRMSMLFQSgalftdmnVFDNVAYPLREHTQLPAPllHSTVMMKLEA-VGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERpgTIIEEITVDlPHRDNPIE 262
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADK--KIVAHGSAQ-ALQANPDP 237
|
....
gi 1737829014 263 RRKQ 266
Cdd:PRK11831 238 RVRQ 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
50-247 |
3.19e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.94 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL------AG------KPVRgpsQQVAFMLQkdl 117
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGkknkklKPLR---KKVGIVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 lMP-----WRSIQKNVELGMQIRGRSKAERAEVAKALLArchLKGFE----NHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK13634 93 -FPehqlfEETVEKDICFGPMNFGVSEEDAKQKAREMIE---LVGLPeellARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHK--GTVF 225
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
55-231 |
3.47e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.80 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRgpSQQVAFMLQ----------KDLLMPWrsi 124
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--RQRDEYHQDllylghqpgiKTELTAL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 qKNVELGMQIRGRSKAERAEVAkalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:PRK13538 93 -ENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170 180
....*....|....*....|....*..
gi 1737829014 205 QQDLAQMLAsEGKTALMITHDLAEAIA 231
Cdd:PRK13538 169 EALLAQHAE-QGGMVILTTHQDLPVAS 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
53-250 |
4.03e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ-----------VAFMLQKDLLMPw 121
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpvrkkvgVVFQFPESQLFE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELGMQIRGRSKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 201 KMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE-------RPGTIIEEI 250
Cdd:PRK13643 180 RIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKghiiscgTPSDVFQEV 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-249 |
1.41e-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: 100.28 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 23 QPAAAPLPfaieYRGVTRRFKN--------RQGkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQ 94
Cdd:COG5265 345 APDAPPLV----VGGGEVRFENvsfgydpeRPI------LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 95 VTLAGKPVRGPSQQ-------------VAFmlqkdllmpwrsiqkNVELGMQIR-GRSKAERAEVAKAllAR-CHLKGFE 159
Cdd:COG5265 415 ILIDGQDIRDVTQAslraaigivpqdtVLF---------------NDTIAYNIAyGRPDASEEEVEAA--ARaAQIHDFI 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 160 NHYPHQ-----------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAe 228
Cdd:COG5265 478 ESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE--VARGRTTLVIAHRLS- 554
|
250 260
....*....|....*....|.
gi 1737829014 229 AIALSDRVFVMSErpGTIIEE 249
Cdd:COG5265 555 TIVDADEILVLEA--GRIVER 573
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-255 |
1.72e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrQGKGEMTaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrgpSQQVAFM 112
Cdd:PRK13648 8 IVFKNVSFQY---QSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRS---------IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK13648 81 LRKHIGIVFQNpdnqfvgsiVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGK-TALMITHDLAEAIAlSDRVFVMSE-------RPGTIIE------E 249
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNL-LDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKgtvykegTPTEIFDhaeeltR 238
|
....*.
gi 1737829014 250 ITVDLP 255
Cdd:PRK13648 239 IGLDLP 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
46-249 |
2.62e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 46 QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQK-DLLM 119
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAE-VAKALLArCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13642 95 VGATVEDDVAFGMENQGIPREEMIKrVDEALLA-VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 199 QTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVMseRPGTIIEE 249
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVM--KAGEIIKE 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
53-248 |
3.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ------VAFMLQK-DLLMPWRSIQ 125
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqgirklVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVELGMQ------IRGRSKAERAevakalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:PRK13644 97 EDLAFGPEnlclppIEIRKRVDRA------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737829014 200 T-KMVLQQdlAQMLASEGKTALMITHDLaEAIALSDRVFVMsERPGTIIE 248
Cdd:PRK13644 171 SgIAVLER--IKKLHEKGKTIVYITHNL-EELHDADRIIVM-DRGKIVLE 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
33-251 |
3.73e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL--------------- 97
Cdd:PRK13633 5 IKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsdeenlwdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 98 --AGKPVRGPSQQ-VAFMLQKDllmpwrsiqknVELGMQIRGRSKAE-RAEVAKALlARCHLKGFENHYPHQLSGGMRQR 173
Cdd:PRK13633 85 nkAGMVFQNPDNQiVATIVEED-----------VAFGPENLGIPPEEiRERVDESL-KKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 174 AALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIAlSDRVFVMSErpGTIIEEIT 251
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS--GKVVMEGT 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
50-250 |
4.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.58 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQ-KDLLM 119
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqirKKVGLVFQfPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13649 99 FEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 199 QTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM-------SERPGTIIEEI 250
Cdd:PRK13649 179 KGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLekgklvlSGKPKDIFQDV 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
50-247 |
4.46e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.88 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQK-DLLMPW------- 121
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKvGLVFQYpeyqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELGMQIRGRSKAERAEVAKALLARCHLK--GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737829014 200 TKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNK--GKCE 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
36-248 |
5.18e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.99 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFKNRQGkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvRGPSQQVAFMLQK 115
Cdd:PRK11701 10 RGLTKLYGPRKG------CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR--DGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 116 DLLMPWRS----IQKNVELGMqiRGRSKAErAEVAKALLArchlKGfENHY------------------------PHQLS 167
Cdd:PRK11701 82 ERRRLLRTewgfVHQHPRDGL--RMQVSAG-GNIGERLMA----VG-ARHYgdiratagdwlerveidaariddlPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALD--AQTKMVlqqDLAQMLASE-GKTALMITHDLAEAIALSDRVFVMseRPG 244
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQARLL---DLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVM--KQG 228
|
....
gi 1737829014 245 TIIE 248
Cdd:PRK11701 229 RVVE 232
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
54-248 |
5.64e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 98.48 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF----MLQKDLLMPWRSIQKNVE 129
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAnsvaMVDQDIFLFEGTVRDNLT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 L---GMQIRGRSKAER-AEVAKALLARChlKGFENHYPH---QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM 202
Cdd:TIGR03796 575 LwdpTIPDADLVRACKdAAIHDVITSRP--GGYDAELAEggaNLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1737829014 203 VLQQDLAQmlasEGKTALMITHDLAeAIALSDRVFVMsERpGTIIE 248
Cdd:TIGR03796 653 IIDDNLRR----RGCTCIIVAHRLS-TIRDCDEIIVL-ER-GKVVQ 691
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
49-239 |
1.13e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.56 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS---EGQVTLAGKPV---------RGPSQQVAFMLQKD 116
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpekelnKLRAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 L--LMPWRSIQKNV-ELGMQIRGRSKAERAEVAKALL-------ARCHLKgfenHYPHQLSGGMRQRAALARTLAVEPDV 186
Cdd:PRK09473 107 MtsLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLdavkmpeARKRMK----MYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 187 LLMDEPFSALD----AQTkMVLQQDLAQmlasEGKTA-LMITHDLAEAIALSDRVFVM 239
Cdd:PRK09473 183 LIADEPTTALDvtvqAQI-MTLLNELKR----EFNTAiIMITHDLGVVAGICDKVLVM 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
47-257 |
1.59e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF---MLQKDLLMPWR 122
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARrigLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 -SIQKNVELG------MQIRGRSKAERAeVAKALLArCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:PRK10253 96 iTVQELVARGryphqpLFTRWRKEDEEA-VTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 196 LDAQTKMVLQQDLAQMLASEGKTALMITHDLAEA-------IALSDRVFVMSERPGTIieeITVDLPHR 257
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcryashlIALREGKIVAQGAPKEI---VTAELIER 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
50-251 |
1.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.08 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG---------KPVRGPSQQVAFMLQ------ 114
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVRKRIGMVFQfpesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 -KDllmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARChlkGFENHY----PHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK13646 99 fED------TVEREIIFGPKNFKMNLDEVKNYAHRLLMDL---GFSRDVmsqsPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE--GSIVSQTS 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
48-224 |
2.46e-22 |
|
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: 91.79 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---RGPSQQ-VAFMLQKDLLMPWRS 123
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqRDSIARgLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAevakalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEA------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|.
gi 1737829014 204 LQQDLAQMLAsEGKTALMITH 224
Cdd:cd03231 164 FAEAMAGHCA-RGGMVVLTTH 183
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
44-256 |
2.71e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 44 NRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG---KPVRGPSQQVAFMLQKDLLMP 120
Cdd:PRK13631 32 DEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyiGDKKNNHELITNPYSKKIKNF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 121 WR-------------------SIQKNVELGMQIRGRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTL 180
Cdd:PRK13631 112 KElrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 181 AVEPDVLLMDEPFSALD--AQTKMVlqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE----RPGT--------- 245
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDpkGEHEMM---QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKgkilKTGTpyeiftdqh 268
|
250
....*....|.
gi 1737829014 246 IIEEITVDLPH 256
Cdd:PRK13631 269 IINSTSIQVPR 279
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
33-254 |
6.73e-22 |
|
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: 94.87 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV-----------TLAGKP 101
Cdd:TIGR03269 280 IKVRNVSKRYISVD-RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 VRGPSQQ-VAFMLQKDLLMPWRSIQKNVELGMQIR-----GRSKAerAEVAKALlarchlkGFE--------NHYPHQLS 167
Cdd:TIGR03269 359 GRGRAKRyIGILHQEYDLYPHRTVLDNLTEAIGLElpdelARMKA--VITLKMV-------GFDeekaeeilDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII 247
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIV 507
|
250
....*....|..
gi 1737829014 248 -----EEITVDL 254
Cdd:TIGR03269 508 kigdpEEIVEEL 519
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
49-241 |
6.80e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 95.11 E-value: 6.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-------GPSqqVAFMLQKDLLMPw 121
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwdretfGKH--IGYLPQDVELFP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVElgmqiRGRSKAE-RAEVAKALLARCH--LKGFENHYPHQ-------LSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:TIGR01842 406 GTVAENIA-----RFGENADpEKIIEAAKLAGVHelILRLPDGYDTVigpggatLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737829014 192 PFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAeAIALSDRVFVMSE 241
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKA-LKARGITVVVITHRPS-LLGCVDKILVLQD 528
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
50-239 |
7.14e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.58 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG---------KPVRGPSQQVAFMLQ-KDLLM 119
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNLKKLRKKVSLVFQfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 199 QTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK13641 179 EGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
45-249 |
9.64e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 45 RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKS-TLLNMGAGLYAPS----EGQVTLAGKP-----------VRGpsQQ 108
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESllhaseqtlrgVRG--NK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDL--LMPWRSIQKNV-ELGMQIRG-RSKAERAEVAKAL--LARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK15134 94 IAMIFQEPMvsLNPLHTLEKQLyEVLSLHRGmRREAARGEILNCLdrVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QNGRCVEQ 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
52-241 |
9.78e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.11 E-value: 9.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT----------LAGKPVRGpsqqVAFMLQKDLLMPW 121
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllpLHARARRG----IGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK10895 93 LSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 201 KMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10895 173 VIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQ 212
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-247 |
1.09e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.46 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRQG--------KG-------EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG4586 1 IIEVENLSKTYRVYEKepglkgalKGlfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 97 LAGK-PVRgpsQQVAF-------MLQK-----DLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYP 163
Cdd:COG4586 81 VLGYvPFK---RRKEFarrigvvFGQRsqlwwDL-----PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 164 HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErp 243
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH-- 230
|
....
gi 1737829014 244 GTII 247
Cdd:COG4586 231 GRII 234
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
61-276 |
1.51e-21 |
|
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: 90.93 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF---MLQKDLLMpwrSIQKNVelgmqirGR 137
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAdyeGTVRDLLS---SITKDF-------YT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 SKAERAEVAKALlarchlkGFENHYPHQ---LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAS 214
Cdd:cd03237 92 HPYFKTEIAKPL-------QIEQILDREvpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 215 EGKTALMITHDLAEAIALSDRVFVMSERPGtiieEITVDLPhrdnPIERRkqAGMNEYVAHL 276
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVFEGEPS----VNGVANP----PQSLR--SGMNRFLKNL 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
54-273 |
1.61e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.25 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTL---LNMGAGLyapsEGQVTLAGK-------------PVRGPSQQVAFMLQKDL 117
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNEL----ESEVRVEGRveffnqniyerrvNLNRLRRQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPwRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLKGFENHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHR--DNPIERRKQagmn 270
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTKKifNSPHDSRTR---- 253
|
...
gi 1737829014 271 EYV 273
Cdd:PRK14258 254 EYV 256
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
42-239 |
2.07e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.24 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 42 FKNRQGKGEMTAVSDV-SIGIKAgefvsLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGPSQQ--VAF 111
Cdd:PRK11144 6 FKQQLGDLCLTVNLTLpAQGITA-----IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEKrrIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMqirgrSKAERAEVAK--ALLARCHLKgfeNHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGM-----AKSMVAQFDKivALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 190 DEPFSALDAQTKMVLQQDLaQMLASEGKTA-LMITHDLAEAIALSDRVFVM 239
Cdd:PRK11144 153 DEPLASLDLPRKRELLPYL-ERLAREINIPiLYVSHSLDEILRLADRVVVL 202
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
48-224 |
2.12e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.34 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RGPSQQVAFMLQKDLLMPWRS 123
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGrskAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:TIGR01189 90 ALENLHFWAAIHG---GAQRTIEDAL-AAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|.
gi 1737829014 204 LQQDLAQMLASEGkTALMITH 224
Cdd:TIGR01189 166 LAGLLRAHLARGG-IVLLTTH 185
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
54-246 |
3.30e-21 |
|
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: 93.27 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-------GPS-----QQVAfmlqkdlLMPw 121
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreelGRHigylpQDVE-------LFD- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVelgmqirGRSKAERAE--VAKALLARCH---LKgFENHY-------PHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:COG4618 420 GTIAENI-------ARFGDADPEkvVAAAKLAGVHemiLR-LPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAeAIALSDRVFVMseRPGTI 246
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHRPS-LLAAVDKLLVL--RDGRV 544
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-249 |
3.98e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 22 AQPAAAPLPFA------IEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTllnmgAGL--- 87
Cdd:PRK15134 259 SEPSGDPVPLPepasplLDVEQLQVAFPIRKGilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLall 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 88 -YAPSEGQVTLAGKPVRGPSQ----------QVAFMLQKDLLMPWRSIQKNVELGMQIRGR--SKAERAEVAKALLARCH 154
Cdd:PRK15134 334 rLINSQGEIWFDGQPLHNLNRrqllpvrhriQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 155 LKGFENH-YPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDaqtKMVLQQDLA--QMLASEGKTA-LMITHDLAEAI 230
Cdd:PRK15134 414 LDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD---KTVQAQILAllKSLQQKHQLAyLFISHDLHVVR 490
|
250
....*....|....*....
gi 1737829014 231 ALSDRVFVMseRPGTIIEE 249
Cdd:PRK15134 491 ALCHQVIVL--RQGEVVEQ 507
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-249 |
4.72e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.16 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 17 ADARHAQPAAAPLPFAIEYRGvtrrfknrqgkgeMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL------NMGAGLYAP 90
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGFAG-------------KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmNDKVSGYRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 91 SeGQVTLAGKPVRGPS------QQVAFMLQKDLLMPwRSIQKNVELGmqIRGRSKAERAE---VAKALLARCHL----KG 157
Cdd:PRK14271 80 S-GDVLLGGRSIFNYRdvlefrRRVGMLFQRPNPFP-MSIMDNVLAG--VRAHKLVPRKEfrgVAQARLTEVGLwdavKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 158 FENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVF 237
Cdd:PRK14271 156 RLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAA 233
|
250
....*....|..
gi 1737829014 238 VMSErpGTIIEE 249
Cdd:PRK14271 234 LFFD--GRLVEE 243
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
49-248 |
4.98e-21 |
|
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: 89.50 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpVRGPSQQVAFML---QKDLLM--PWRS 123
Cdd:TIGR02323 14 GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYI---MRSGAELELYQLseaERRRLMrtEWGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCH----------LKGFE------NHYPHQLSGGMRQRAALARTLAVEPDVL 187
Cdd:TIGR02323 91 VHQNPRDGLRMRVSAGANIGERLMAIGARHYgnirataqdwLEEVEidptriDDLPRAFSGGMQQRLQIARNLVTRPRLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:TIGR02323 171 FMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ--GRVVE 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
54-241 |
5.22e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLyAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDL---LMP-WRSI 124
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSaaelaRHRAYLSQQQSppfAMPvFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QknveLGMQirgrSKAERAEVAKALLARCHLKGFENHYP---HQLSGGMRQRAALARTL-----AVEPD--VLLMDEPFS 194
Cdd:COG4138 91 A----LHQP----AGASSEAVEQLLAQLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1737829014 195 ALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4138 163 SLDVAQQAALDRLLRE-LCQQGITVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-248 |
7.17e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 22 AQPAAAPLPFAIEYRGVTRRFKNRqgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP 101
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQ----PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 VRGPS-----QQVAFMLQK-DLLMpwRSIQKNVELGmqirgrskAERA--EVAKALLARCHL-KGFENHYP--------- 163
Cdd:PRK11160 404 IADYSeaalrQAISVVSQRvHLFS--ATLRDNLLLA--------APNAsdEALIEVLQQVGLeKLLEDDKGlnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 164 HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKmvlQQDLAQMLA-SEGKTALMITHDLAeAIALSDRVFVMSEr 242
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE---RQILELLAEhAQNKTVLMITHRLT-GLEQFDRICVMDN- 548
|
....*.
gi 1737829014 243 pGTIIE 248
Cdd:PRK11160 549 -GQIIE 553
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
49-241 |
7.74e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF------MLQKD--LLM 119
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNREVPFlrrqigMIFQDhhLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PwRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD-A 198
Cdd:PRK10908 93 D-RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737829014 199 QTKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10908 172 LSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
55-258 |
9.29e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.51 E-value: 9.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQVA--FML-----QKDLLMPWRSIQ 125
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdiRSPRDAIRagIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVEL---------GMQIRGRSKAERAEVAKALLArchlkgFENHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK11288 350 DNINIsarrhhlraGCLINNRWEAENADRFIRSLN------IKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 193 FSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpgtiiEEITVDLPHRD 258
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVLGVADRIVVMRE------GRIAGELAREQ 482
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
49-248 |
1.78e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.91 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN----MGAglYAPS---EGQVTLAGKPVRGPSQQVAfMLQKDLLMPW 121
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRsinrMND--LNPEvtiTGSIVYNGHNIYSPRTDTV-DLRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 R-------SIQKNVELGMQIRGRSKAER--AEVAKALLA---------RCHLKGFenhyphQLSGGMRQRAALARTLAVE 183
Cdd:PRK14239 93 QqpnpfpmSIYENVVYGLRLKGIKDKQVldEAVEKSLKGasiwdevkdRLHDSAL------GLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRV-FVMSerpGTIIE 248
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTgFFLD---GDLIE 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
50-241 |
4.40e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.94 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAG-LYAPSEGQVTLA--GKPVRGPSQQVAFMLQKDLLMPWRSIQK 126
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILAnnRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 N---VELGMQIRGRSKAERAEVAKAL-----LARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PLN03211 160 TlvfCSLLRLPKSLTKQEKILVAESViselgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 199 QTKMVLQQDLAQmLASEGKTALMITHDLAEAI-ALSDRVFVMSE 241
Cdd:PLN03211 240 TAAYRLVLTLGS-LAQKGKTIVTSMHQPSSRVyQMFDSVLVLSE 282
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
33-248 |
6.26e-20 |
|
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: 85.62 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS---Q 107
Cdd:cd03244 3 IEFKNVSLRYRP----NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHdlrS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELgmqirgRSKAERAEVAKALlARCHLKGFENHYPHQL-----------SGGMRQRAAL 176
Cdd:cd03244 79 RISIIPQDPVLFS-GTIRSNLDP------FGEYSDEELWQAL-ERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLaEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRL-DTIIDSDRILVLDK--GRVVE 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-234 |
6.55e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 6.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ--V 109
Cdd:PRK15056 6 GIVVNDVTVTWRNGH-----TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLmPWRS---IQKNVELG----MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK15056 81 AYVPQSEEV-DWSFpvlVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSD 234
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARI-ISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
54-244 |
8.80e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkPvrgPSQQVAFMLQKdLLMPWRSiqknveLGMQ 133
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P---AGARVLFLPQR-PYLPLGT------LREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 I---RGRSKAERAEVAKALlARCHLKGF------ENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTkmvl 204
Cdd:COG4178 446 LlypATAEAFSDAELREAL-EAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN---- 520
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1737829014 205 QQDLAQMLASE--GKTALMITHDlAEAIALSDRVFVMSERPG 244
Cdd:COG4178 521 EAALYQLLREElpGTTVISVGHR-STLAAFHDRVLELTGDGS 561
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
49-224 |
1.18e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS--QQVAFMLQKDLLMPWRSIQK 126
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRSKAERAEVAKAL-LARC-HLKGfenhypHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAALEAVgLAPLaHLPF------GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|
gi 1737829014 205 QQDLAQMLASEGkTALMITH 224
Cdd:PRK13539 167 AELIRAHLAQGG-IVIAATH 185
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-263 |
1.19e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.62 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTrrFKNRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV-- 109
Cdd:PRK10790 340 RIDIDNVS--FAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 --AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAE-VAKALLARCHLKGFENHYPHQ---LSGGMRQRAALARTLAVE 183
Cdd:PRK10790 415 qgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALEtVQLAELARSLPDGLYTPLGEQgnnLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAqmLASEGKTALMITHDLAeaialsdrvfvmserpgTIIEEITVDLPHRDNPIER 263
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALA--AVREHTTLVVIAHRLS-----------------TIVEADTILVLHRGQAVEQ 555
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
54-241 |
1.37e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 88.34 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-APSEGQVTLAGKPV--RGPSQQVAFML-------QKDLLMPWRS 123
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVdiRNPAQAIRAGIamvpedrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGM--QIRGRSKAERAEVAKALLA---RCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:TIGR02633 356 VGKNITLSVlkSFCFKMRIDAAAELQIIGSaiqRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 198 AQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR02633 436 VGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
55-242 |
2.60e-19 |
|
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: 82.11 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgpsqqvafmlqkdllmpwrsiqKNVELGmqi 134
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------------------STVKIG--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 rgrskaeraevakallarchlkgfenhYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVlqqdLAQMLAS 214
Cdd:cd03221 67 ---------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA----LEEALKE 115
|
170 180 190
....*....|....*....|....*....|
gi 1737829014 215 EGKTALMITHD--LAEAIAlsDRVFVMSER 242
Cdd:cd03221 116 YPGTVILVSHDryFLDQVA--TKIIELEDG 143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-248 |
2.82e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ 107
Cdd:PRK10261 314 LQVRNLVTRFPLRSGllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLM----PWRSIQKNVELGMQIR--------GRSKAERAEVAKaLLARCHLKgfENH---YPHQLSGGMRQ 172
Cdd:PRK10261 394 GKLQALRRDIQFifqdPYASLDPRQTVGDSIMeplrvhglLPGKAAAARVAW-LLERVGLL--PEHawrYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 173 RAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL--GQIVE 544
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
33-248 |
2.90e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.84 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQG---KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RG 104
Cdd:PRK15112 5 LEVRNLSKTFRYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQ--KDLLMPWRSIQKNVELGMQIR-GRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTL 180
Cdd:PRK15112 85 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ--GEVVE 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
33-248 |
3.99e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.00 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:PRK11176 342 IEFRNVTFTY---PGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaslrN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirgrSKAERAEVAKAllAR-CHLKGFENHYPH-----------QLSGGMRQRAA 175
Cdd:PRK11176 418 QVALVSQNVHLFN-DTIANNIAYART----EQYSREQIEEA--ARmAYAMDFINKMDNgldtvigengvLLSGGQRQRIA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVMSErpGTIIE 248
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEILVVED--GEIVE 558
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
49-249 |
5.32e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.81 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL---NMGAGLY--APSEGQVTLAGK-----PVRGPSQQVAFMLQKDLL 118
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYpeARVSGEVYLDGQdifkmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MPWRSIQKNVELGMQIR--GRSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK14247 94 IPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYK--GQIVEW 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
57-240 |
7.04e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 57 VSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYaPSEGQVTLAGKPVRGPS-----QQVAFMLQKD---LLMPwrsiqknV 128
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSaaelaRHRAYLSQQQtppFAMP-------V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENHYP---HQLSGGMRQRAALART-LAVEPDV------LLMDEPFSALDA 198
Cdd:PRK03695 87 FQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGrsvNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1737829014 199 QTKMVLQQDLAQMlASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK03695 167 AQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLK 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
50-248 |
9.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQvTLAG-----------KPVRGPSQQVAFMLQ-KDL 117
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyaipanlkkiKEVKRLRKEIGLVFQfPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK13645 102 QLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 197 DAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE--GKVIS 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-248 |
9.91e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 9.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 1 MLRSIQLKDANVAEAYADARHAQPAAAPLPfAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTL 80
Cdd:COG0488 285 ALEKLEREEPPRRDKTVEIRFPPPERLGKK-VLELEGLSKSY------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 81 LNMGAGLYAPSEGQVTlagkpvRGPSQQVAFMLQK-DLLMPWRSIQKNVElgmqiRGRSKAERAEVAkALLARCHLKGFE 159
Cdd:COG0488 358 LKLLAGELEPDSGTVK------LGETVKIGYFDQHqEELDPDKTVLDELR-----DGAPGGTEQEVR-GYLGRFLFSGDD 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 160 NHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQqdlaQMLAS-EGkTALMITHD--LAEAIAlsDR 235
Cdd:COG0488 426 AFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE----EALDDfPG-TVLLVSHDryFLDRVA--TR 498
|
250
....*....|...
gi 1737829014 236 VFVMseRPGTIIE 248
Cdd:COG0488 499 ILEF--EDGGVRE 509
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
48-241 |
1.26e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS---EGQVTLAGKPVRGPSQQV--AFMLQKDLLMPWR 122
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNV----ELGMQiRGRSKAERAEVAKALLARCHLK-------GFENHYpHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:TIGR00955 115 TVREHLmfqaHLRMP-RRVTKKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 192 PFSALDA-QTKMVLQqdLAQMLASEGKTALMITHD-LAEAIALSDRVFVMSE 241
Cdd:TIGR00955 193 PTSGLDSfMAYSVVQ--VLKGLAQKGKTIICTIHQpSSELFELFDKIILMAE 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-253 |
1.28e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:PRK09700 6 ISMAGIGKSF------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 L------QKDLLMPWRSIQKNVELG-------MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALART 179
Cdd:PRK09700 80 LgigiiyQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 180 LAVEPDVLLMDEPFSAL-DAQTK---MVLQQdlaqmLASEGKTALMITHDLAEAIALSDRVFVMSErpGT-----IIEEI 250
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLtNKEVDylfLIMNQ-----LRKEGTAIVYISHKLAEIRRICDRYTVMKD--GSsvcsgMVSDV 232
|
...
gi 1737829014 251 TVD 253
Cdd:PRK09700 233 SND 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
53-241 |
2.06e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYA---PSEGQVTLAGKPV----------RGPSQQVAFMLQKDLLM 119
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVqregrlardiRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQ---------IRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQAL-TRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 191 EPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
49-236 |
2.15e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtlagkpVRGPSQQVAFMLQKDLLMPwrSIQKNV 128
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDT--TLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKaeRAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDL 208
Cdd:PRK09544 87 NRFLRLRPGTK--KEDILPAL-KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170 180
....*....|....*....|....*...
gi 1737829014 209 AQMLASEGKTALMITHDLAEAIALSDRV 236
Cdd:PRK09544 164 DQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
56-249 |
2.56e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.03 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAGLYAPSEGQVTLAGKPVrgpsqqvafmlqKDLLMPWRSiQKNVELGMQ 133
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKtiMGHPKYEVTEGEILFKGEDI------------TDLPPEERA-RLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 irgrSKAERAEVAKALLARCHLKGFenhyphqlSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ-TKMVlqQDLAQML 212
Cdd:cd03217 85 ----YPPEIPGVKNADFLRYVNEGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDaLRLV--AEVINKL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1737829014 213 ASEGKTALMITH--DLAEAIAlSDRVFVMSErpGTIIEE 249
Cdd:cd03217 151 REEGKSVLIITHyqRLLDYIK-PDRVHVLYD--GRIVKS 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
45-239 |
4.00e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 45 RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQK--------- 115
Cdd:PRK10261 23 MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQsaaqmrhvr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 116 --DLLM----PWRSIQKNVELGMQI-------RGRSKAERAEVAKALLARCHL---KGFENHYPHQLSGGMRQRAALART 179
Cdd:PRK10261 103 gaDMAMifqePMTSLNPVFTVGEQIaesirlhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 180 LAVEPDVLLMDEPFSALDA-------QTKMVLQQDLAQmlasegkTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVtiqaqilQLIKVLQKEMSM-------GVIFITHDMGVVAEIADRVLVM 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
48-253 |
1.00e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.00 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP-----VRGPSQQVAFMLQK-DLLMPW 121
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenIREVRKFVGLVFQNpDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELG---MQIRGRSKAERAEVAKALLARCHLKgfeNHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13652 94 PTVEQDIAFGpinLGLDEETVAHRVSSALHMLGLEELR---DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 199 QTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK--GRIVAYGTVE 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
33-262 |
1.01e-17 |
|
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: 82.93 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGL--YAPSEGQV--------------- 95
Cdd:TIGR03269 1 IEVKNLTKKFDGKE------VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 96 -TLAGKPV----------------------RGPSQQVAFMLQKDL-LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLA 151
Cdd:TIGR03269 75 pSKVGEPCpvcggtlepeevdfwnlsdklrRRIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 152 RCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITH------D 225
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1737829014 226 LAE-AIALSDRVFVMSERPGTIIEEI--TVDLPHRDNPIE 262
Cdd:TIGR03269 235 LSDkAIWLENGEIKEEGTPDEVVAVFmeGVSEVEKECEVE 274
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
54-241 |
1.85e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-APSEGQVTLAGKPV--RGPSQQVAF---ML----QKDLLMPWRS 123
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPVkiRNPQQAIAQgiaMVpedrKRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGM--QIRGRS---KAERAEVAKALLARCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK13549 358 VGKNITLAAldRFTGGSridDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737829014 198 AQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13549 438 VGAKYEIYK-LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
54-248 |
2.07e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.74 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP----SEGQVTLAGKPVRG---PSQQVAFMLQ--KDLLMPWRSI 124
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPcalRGRKIATIMQnpRSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QKNVELGMQIRGRSKAERAevakaLLARCHLKGFENH------YPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK10418 99 HTHARETCLALGKPADDAT-----LTAALEAVGLENAarvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737829014 199 QTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIVE 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-239 |
2.72e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.41 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY--APSEGQVTLAGKPVRGPS---- 106
Cdd:TIGR02633 2 LEMKGIVKTF------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNirdt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 --QQVAFMLQKDLLMPWRSIQKNVELGMQI--RGRSKAERAEV--AKALLARCHLKGFENHYP-HQLSGGMRQRAALART 179
Cdd:TIGR02633 76 erAGIVIIHQELTLVPELSVAENIFLGNEItlPGGRMAYNAMYlrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 180 LAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEIL-LDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-251 |
3.21e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 34 EYRGVTRRFKNRqgkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAfmL 113
Cdd:PRK09700 267 EVRNVTSRDRKK--------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA--V 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 114 QKDL-----------LMPWRSIQKNVELGMQIR------------GRSKAERAEVAKALLA-RCHLKgfeNHYPHQLSGG 169
Cdd:PRK09700 337 KKGMayitesrrdngFFPNFSIAQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLAlKCHSV---NQNITELSGG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 170 MRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCE--GRLTQI 490
|
..
gi 1737829014 250 IT 251
Cdd:PRK09700 491 LT 492
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
52-249 |
3.39e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQQVAFMLQkdllmpwrsiQK 126
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswssKAFARKVAYLPQ----------QL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIR-----------------GRSKAERAEVAKALLArchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK10575 95 PAAEGMTVRelvaigrypwhgalgrfGAADREKVEEAISLVG---LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALD-AQTKMVLQqdLAQMLASE-GKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:PRK10575 172 DEPTSALDiAHQVDVLA--LVHRLSQErGLTVIAVLHDINMAARYCDYLVAL--RGGEMIAQ 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
53-241 |
4.54e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.60 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR----GPSQQVAFMLQKDLLMPWRSIQKNV 128
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDL 208
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|...
gi 1737829014 209 AQMlaSEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR01257 1105 LKY--RSGRTIIMSTHHMDEADLLGDRIAIISQ 1135
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-192 |
5.18e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.94 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP------ 105
Cdd:NF033858 1 VARLEGVSHRY------GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrrav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 SQQVAFMLQ---KDlLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:NF033858 75 CPRIAYMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170
....*....|
gi 1737829014 183 EPDVLLMDEP 192
Cdd:NF033858 154 DPDLLILDEP 163
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-248 |
6.02e-17 |
|
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: 80.61 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 2 LRSIQLKDANVAEAYADArhAQPAAAPLPFAIEYRGVTRRFKNRQGkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL 81
Cdd:COG4615 299 IEELELALAAAEPAAADA--AAPPAPADFQTLELRGVTYRYPGEDG-DEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 82 NMGAGLYAPSEGQVTLAGKPVRGPS-----QQVA-----FMLQKDLLmpwrsiqknvelgmqirGRSKAERAEVAKALLA 151
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTADNreayrQLFSavfsdFHLFDRLL-----------------GLDGEADPARARELLE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 152 RCHLKG---FENHY--PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHD- 225
Cdd:COG4615 439 RLELDHkvsVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDd 518
|
250 260
....*....|....*....|....*..
gi 1737829014 226 ----LAeaialsDRVFVMSErpGTIIE 248
Cdd:COG4615 519 ryfdLA------DRVLKMDY--GKLVE 537
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
69-239 |
6.03e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RG---PSQQVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKA 140
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGllaLRQQVATVFQDpEQQIFYTDIDSDIAFSLRNLGVPEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 141 ERAEVAKALLARCHLKGFEnHYPHQ-LSGGMRQRAALARTLAVEPDVLLMDEPFSALD--AQTKMVLqqdLAQMLASEGK 217
Cdd:PRK13638 112 EITRRVDEALTLVDAQHFR-HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpaGRTQMIA---IIRRIVAQGN 187
|
170 180
....*....|....*....|..
gi 1737829014 218 TALMITHDLAEAIALSDRVFVM 239
Cdd:PRK13638 188 HVIISSHDIDLIYEISDAVYVL 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
51-226 |
6.56e-17 |
|
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: 77.76 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 51 MTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---------VAFMLQKdllmPW 121
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnrysVAYAAQK----PW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 ---RSIQKNVELGMQIRGRSkaeraevAKALLARCHLKGFENHYPH-----------QLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03290 90 llnATVEENITFGSPFNKQR-------YKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1737829014 188 LMDEPFSALDAQ-TKMVLQQDLAQMLASEGKTALMITHDL 226
Cdd:cd03290 163 FLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-225 |
6.63e-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: 80.36 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkpvrGPSQQVAFM 112
Cdd:TIGR03719 323 IEAENLTKAF------GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQ-KDLLMPWRSIQKNVELG---MQIRGRSKAERAEVAkallaRCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVL 187
Cdd:TIGR03719 391 DQsRDALDPNKTVWEEISGGldiIKLGKREIPSRAYVG-----RFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLaqmLASEGkTALMITHD 225
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEAL---LNFAG-CAVVISHD 499
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
48-240 |
7.70e-17 |
|
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: 80.76 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQvafMLQKDllmpwrSIQKN 127
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQA---WIQND------SLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 128 VELGMQIRGRSKAERAEvAKALLARCHL-----------KGFenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLE-ACALLPDLEIlpsgdrteigeKGV------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737829014 197 DAQT-KMVLQQDLAQMLASEGKTALMITHDLAeAIALSDRVFVMS 240
Cdd:TIGR00957 792 DAHVgKHIFEHVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMS 835
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
49-239 |
1.00e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.61 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV------RGPSQQVAFMLQKDLLMPWR 122
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtaKIMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSK-AERAEVAKALLARCHLKGFENhyPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALdaqTK 201
Cdd:PRK11614 96 TVEENLAMGGFFAERDQfQERIKWVYELFPRLHERRIQR--AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---AP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1737829014 202 MVLQQ--DLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK11614 171 IIIQQifDTIEQLREQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
63-258 |
1.18e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 63 AGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQVAFML--QKDLLMPWRSIQKNVELGMQIRG 136
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakaHQLGIYLvpQEPLLFPNLSVKENILFGLPKRQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 137 RSKAERAEVAKALlaRCHLKgfenhyPHQLSGGM----RQRAALARTLAVEPDVLLMDEPFSALD-AQTKMVLQQdlAQM 211
Cdd:PRK15439 116 ASMQKMKQLLAAL--GCQLD------LDSSAGSLevadRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSR--IRE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737829014 212 LASEGKTALMITHDLAEAIALSDRVFVMseRPGTI-IEEITVDLPHRD 258
Cdd:PRK15439 186 LLAQGVGIVFISHKLPEIRQLADRISVM--RDGTIaLSGKTADLSTDD 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-238 |
1.34e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 34 EYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------Q 107
Cdd:PRK11288 6 SFDGIGKTFPGVK------ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASttaalaA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPWRSIQKNVELGmQIRGRS----KAERAEVAKALLARCHLKgFENHYP-HQLSGGMRQRAALARTLAV 182
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLG-QLPHKGgivnRRLLNYEAREQLEHLGVD-IDPDTPlKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFV 238
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
53-263 |
1.34e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GP--SQQ--VAFMLQKDLLMPWRSIQK 126
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPksSQEagIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRS-----KAERAEvAKALLARCHLKgfenHYPHQLSG----GMRQRAALARTLAVEPDVLLMDEPFSAL- 196
Cdd:PRK10762 99 NIFLGREFVNRFgridwKKMYAE-ADKLLARLNLR----FSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 197 DAQTKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVDLPHRDNPIER 263
Cdd:PRK10762 174 DTETESLFR--VIRELKSQGRGIVYISHRLKEIFEICDDVTVF--RDGQFIAEREVADLTEDSLIEM 236
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-248 |
1.75e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 6 QLKDANVAEAYADarHAQPAAAPLPFAIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGA 85
Cdd:PRK10522 298 KLNKLALAPYKAE--FPRPQAFPDWQTLELRNVTFAYQDNG-----FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 86 GLYAPSEGQVTLAGKPVrGPSQQVAFMLQkdllmpWRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLKG---FENH 161
Cdd:PRK10522 371 GLYQPQSGEILLDGKPV-TAEQPEDYRKL------FSAVFTDFHLFDQLLGpEGKPANPALVEKWLERLKMAHkleLEDG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 162 Y--PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIaLSDRVFVM 239
Cdd:PRK10522 444 RisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFI-HADRLLEM 522
|
....*....
gi 1737829014 240 seRPGTIIE 248
Cdd:PRK10522 523 --RNGQLSE 529
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-224 |
2.93e-16 |
|
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: 74.50 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTrrFKNRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtlaGKPVRGpsqQVAFM 112
Cdd:cd03223 1 IELENLS--LATPDGR---VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE---DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLmpwrsiqknvelgmqIRGRSKAeraevakALLarchlkgfenhYP--HQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:cd03223 70 PQRPYL---------------PLGTLRE-------QLI-----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 1737829014 191 EPFSALDAQTkmvlQQDLAQMLASEGKTALMITH 224
Cdd:cd03223 117 EATSALDEES----EDRLYQLLKELGITVISVGH 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
31-230 |
3.00e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 31 FAIEYRGVTRRFknrqgkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY--APSEGQVTLagkpvrgpsqq 108
Cdd:COG2401 34 FGVELRVVERYV-----------LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 vafmlqkdllmPWRSIQKNVELGMQI-RGRSKAEraevAKALLARChlkGFENHY-----PHQLSGGMRQRAALARTLAV 182
Cdd:COG2401 92 -----------PDNQFGREASLIDAIgRKGDFKD----AVELLNAV---GLSDAVlwlrrFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITH--DLAEAI 230
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDL 203
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
32-242 |
3.70e-16 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 78.08 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RGPSQ 107
Cdd:TIGR01194 337 SIELKDVHMNPKAPEGS-EGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVsadsRDDYR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QV------AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERaevakallaRCHLKGFENHYPHQLSGGMRQRAALARTLA 181
Cdd:TIGR01194 416 DLfsaifaDFHLFDDLIGPDEGEHASLDNAQQYLQRLEIAD---------KVKIEDGGFSTTTALSTGQQKRLALICAWL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 182 VEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDlaeaialsDRVFVMSER 242
Cdd:TIGR01194 487 EDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHD--------DQYFELADQ 539
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
56-241 |
4.18e-16 |
|
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: 76.43 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvrgpsqqVAFMLQKDLLMPwRSIQKNVELGM--- 132
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQFSWIMP-GTIKENIIFGVsyd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSkaeraeVAKAllarCHLKGFENHYPHQ-----------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT- 200
Cdd:cd03291 126 EYRYKS------VVKA----CQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTe 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 201 KMVLQQDLAQMLASegKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03291 196 KEIFESCVCKLMAN--KTRILVTSKM-EHLKKADKILILHE 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
56-241 |
1.98e-15 |
|
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: 76.49 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvrgpsqqVAFMLQKDLLMPwRSIQKNVELGM--- 132
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------ISFSPQTSWIMP-GTIKDNIIFGLsyd 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSkaeraeVAKAllarCHLKGFENHYPHQ-----------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT- 200
Cdd:TIGR01271 515 EYRYTS------VIKA----CQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTe 584
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 201 KMVLQQDLAQMLASegKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:TIGR01271 585 KEIFESCLCKLMSN--KTRILVTSKL-EHLKKADKILLLHE 622
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
52-253 |
2.12e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSqqVAFMLQKDL-----------LMP 120
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS--PRERRRLGVayipedrlgrgLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 121 WRSIQKNVELGMQIRGR-------SKAERAEVAKALLARCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:COG3845 350 DMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 193 FSALDAQ-TKMVLQQDLAqmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:COG3845 430 TRGLDVGaIEFIHQRLLE--LRDAGAAVLLISEDLDEILALSDRIAVMYE--GRIVGEVPAA 487
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-238 |
2.24e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 30 PFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYaPS---EGQVTLAGKPVRGPS 106
Cdd:PRK13549 3 EYLLEMKNITKTF------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ------QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEV---AKALLARCHLKGFENHYPHQLSGGMRQRAALA 177
Cdd:PRK13549 76 irdterAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMylrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFV 238
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICV 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
53-249 |
2.43e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKS--TLLNMGAGLYAP--SEGQVTLAGKPVRGPSQQ---------VAFMLQKdllm 119
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsSLAIMGLIDYPGrvMAEKLEFNGQDLQRISEKerrnlvgaeVAMIFQD---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQI-------RGRSKAERAEVAKALLARCHLKGFENH---YPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK11022 98 PMTSLNPCYTVGFQImeaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM--YAGQVVET 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
61-276 |
2.82e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.59 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEG----QVTLAGKPvrgpsQQV---AFMLQKDLLMpwRSIQKNVElgmq 133
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdeDLKISYKP-----QYIspdYDGTVEEFLR--SANTDDFG---- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 irgrSKAERAEVAKAL-LARCHLKGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQML 212
Cdd:COG1245 432 ----SSYYKTEIIKPLgLEKLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSERPGTiieeitvdLPHRDNPIERRKqaGMNEYVAHL 276
Cdd:COG1245 503 ENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGV--------HGHASGPMDMRE--GMNRFLKEL 556
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
61-276 |
9.53e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV----TLAGKPVR-GPSQQvafMLQKDLLmpwRSIQKNVelgmqir 135
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKISYKPQYiKPDYD---GTVEDLL---RSITDDL------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 136 gRSKAERAEVAKALlarchlkGFENHYPHQ---LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQML 212
Cdd:PRK13409 429 -GSSYYKSEIIKPL-------QLERLLDKNvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSERPGTiieeitvdLPHRDNPIERRKqaGMNEYVAHL 276
Cdd:PRK13409 501 EEREATALVVDHDIYMIDYISDRLMVFEGEPGK--------HGHASGPMDMRE--GMNRFLKEL 554
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
31-228 |
1.17e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.77 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 31 FAIEYRGVTRRFK-------------NRQGKGEM-TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:PRK13545 3 YKVKFEHVTKKYKmynkpfdklkdlfFRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 97 lagkpVRGPSQQVAFM--LQKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRA 174
Cdd:PRK13545 83 -----IKGSAALIAISsgLNGQL-----TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAE 228
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGDQTfTKKCL--DKMNEFKEQGKTIFFISHSLSQ 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
53-239 |
2.20e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.51 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP----VRGPSQQVAFMLQKDLLMPWRSIQKNV 128
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDL 208
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190
....*....|....*....|....*....|.
gi 1737829014 209 AQMLaSEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR01257 2114 VSII-REGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-265 |
2.35e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV------TLAGKPVRGPS 106
Cdd:PTZ00265 383 IQFKNVRFHYDTRK---DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFMLQKDLLMPwRSIQKNVEL------------------------GMQIRGRSKAERA------------------- 143
Cdd:PTZ00265 460 SKIGVVSQDPLLFS-NSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAgdlndmsnttdsneliemr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 144 ------------EVAKALLARCHLKGFENHY-------PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:PTZ00265 539 knyqtikdsevvDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 205 QQDLAQMLASEGKTALMITHDLAeAIALSDRVFVMS--ERPGTIIEEITVDLPHRDNPIERRK 265
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSnrERGSTVDVDIIGEDPTKDNKENNNK 680
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
42-241 |
2.53e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.98 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 42 FKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGL---YAPSEGQVTLAGKPVRG----PSQQVAFMLQ 114
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEfaekYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 KDLLMPwrsiqknvELgmqirgrskaeraEVAKALLARCHLKGfeNHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:cd03233 91 EDVHFP--------TL-------------TVRETLDFALRCKG--NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737829014 195 ALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAI-ALSDRVFVMSE 241
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYE 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
54-241 |
3.31e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQVAFML-------QKDLLMPWRSI 124
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGLANGIvyisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QKNVEL---------GMQIRGrsKAERAEVAKallarcHLKGFENHYPHQ------LSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK10762 348 KENMSLtalryfsraGGSLKH--ADEQQAVSD------FIRLFNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLAsEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHE 470
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
34-285 |
3.84e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 34 EYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYaPS---EGQVTLAGKPVR----GPS 106
Cdd:NF040905 3 EMRGITKTF------PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRfkdiRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFML--QKDLLMPWRSIQKNVELGMQIRGRSKAERAEV---AKALLARCHLKgfENhyPHQLSG----GMRQRAALA 177
Cdd:NF040905 76 EALGIVIihQELALIPYLSIAENIFLGNERAKRGVIDWNETnrrARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 178 RTLAVEPDVLLMDEPFSAL-DAQTKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEeiTVDLpH 256
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAALL--DLLLELKAQGITSIIISHKLNEIRRVADSITVL--RDGRTIE--TLDC-R 224
|
250 260
....*....|....*....|....*....
gi 1737829014 257 RDNPIERRKQAGMneyvahlmellkVGRD 285
Cdd:NF040905 225 ADEVTEDRIIRGM------------VGRD 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
56-225 |
7.18e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELGMQ-I 134
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ------PGIKVGYLPQEPQLDPTKTVRENVEEGVAeI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSK--------------------AERAEV-------------------AKALlaRChlkgfenhyP------HQLSGG 169
Cdd:TIGR03719 97 KDALDrfneisakyaepdadfdklaAEQAELqeiidaadawdldsqleiaMDAL--RC---------PpwdadvTKLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 170 MRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlasEGkTALMITHD 225
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY---PG-TVVAVTHD 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
62-244 |
1.12e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 69.32 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 62 KAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTlaGKP--------VRGPSQQVAF--MLQKDLlmpwRSIQK--NVE 129
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD--DPPdwdeildeFRGSELQNYFtkLLEGDV----KVIVKpqYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 L-GMQIRGR-----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03236 98 LiPKAVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 204 LQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPG 244
Cdd:cd03236 178 AAR-LIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
48-239 |
1.28e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.93 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAglyAPSEGQVT-----LAGKPVRG--PSQQVAFMlQKDLL 118
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaiCGI---TKDNWHVTadrfrWNGIDLLKlsPRERRKII-GREIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 M----PWRSIQKNVELGMQI---------RG---RSKAERAEVAKALLarcHLKGFENH------YPHQLSGGMRQRAAL 176
Cdd:COG4170 93 MifqePSSCLDPSAKIGDQLieaipswtfKGkwwQRFKWRKKRAIELL---HRVGIKDHkdimnsYPHELTEGECQKVMI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
54-236 |
1.62e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-----------GPSQQVAFMLQKDLLMPWR 122
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRG-RSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK14246 106 SIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 198 aqtkMVLQQDLAQMLASEGK--TALMITHDLAEAIALSDRV 236
Cdd:PRK14246 186 ----IVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
52-248 |
5.41e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--------RGpsqQVAFMLQKDLLMPwRS 123
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswRS---RLAVVSQTPFLFS-DT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGmqirgRSKAERAEVAK-ALLARCH------LKGFENHYPHQ---LSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:PRK10789 405 VANNIALG-----RPDATQQEIEHvARLASVHddilrlPQGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 194 SALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVMSErpGTIIE 248
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQW--GEGRTVIISAHRLS-ALTEASEILVMQH--GHIAQ 529
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
61-244 |
6.01e-13 |
|
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: 65.67 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVafmlqkdllmpwrsiqknvelgmqirgrska 140
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 141 eraevakallarchlkgfenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTAL 220
Cdd:cd03222 71 ------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170 180
....*....|....*....|....
gi 1737829014 221 MITHDLAEAIALSDRVFVMSERPG 244
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
56-239 |
6.09e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.11 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS--EGQVTLAGKPVRGPSQ-QVAFMLQKDLLMPwrsiqknvelgm 132
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQrSTGYVEQQDVHSP------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 qirgrskaeRAEVAKALLARCHLKGfenhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLaQML 212
Cdd:cd03232 93 ---------NLTVREALRFSALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL-KKL 154
|
170 180
....*....|....*....|....*...
gi 1737829014 213 ASEGKTALMITHDLAEAI-ALSDRVFVM 239
Cdd:cd03232 155 ADSGQAILCTIHQPSASIfEKFDRLLLL 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
61-243 |
9.15e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP--SQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRS 138
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 139 KAERAEVAKALLArchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGkT 218
Cdd:PRK13543 114 AKQMPGSALAIVG---LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGG-A 189
|
170 180
....*....|....*....|....*
gi 1737829014 219 ALMITHDLAEAIALSDRVFVMSERP 243
Cdd:PRK13543 190 ALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
69-225 |
1.08e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELGMQ----IRGR------- 137
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPA------PGIKVGYLPQEPQLDPEKTVRENVEEGVAevkaALDRfneiyaa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 -------------------------------SKAERAevAKALlaRChlkgfenhyPH------QLSGGMRQRAALARTL 180
Cdd:PRK11819 112 yaepdadfdalaaeqgelqeiidaadawdldSQLEIA--MDAL--RC---------PPwdakvtKLSGGERRRVALCRLL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlasEGkTALMITHD 225
Cdd:PRK11819 179 LEKPDMLLLDEPTNHLDAESVAWLEQFLHDY---PG-TVVAVTHD 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-225 |
1.88e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkpvrGPSQQVAFM 112
Cdd:PRK11819 325 IEAENLSKSF------GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQ-KDLLMPWRSIQKNVELG---MQIRGRSKAERAEVAkallaRCHLKGfenhyPHQ------LSGGMRQRAALARTLAV 182
Cdd:PRK11819 393 DQsRDALDPNKTVWEEISGGldiIKVGNREIPSRAYVG-----RFNFKG-----GDQqkkvgvLSGGERNRLHLAKTLKQ 462
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLaqmLASEGkTALMITHD 225
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEAL---LEFPG-CAVVISHD 501
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
48-273 |
2.57e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP-SEGQVTLAGKpvrgpsqqVAFMLQkdllMPW---RS 123
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT--------VAYVPQ----VSWifnAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRgRSKAERAEVAKAL-----------LARCHLKGFenhyphQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PLN03130 695 VRDNILFGSPFD-PERYERAIDVTALqhdldllpggdLTEIGERGV------NISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 193 FSALDAQtkmVLQQDLAQMLASE--GKTALMITHDLaEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIERR--KQAG 268
Cdd:PLN03130 768 LSALDAH---VGRQVFDKCIKDElrGKTRVLVTNQL-HFLSQVDRIILVHE--GMIKEEGTYEELSNNGPLFQKlmENAG 841
|
....*.
gi 1737829014 269 -MNEYV 273
Cdd:PLN03130 842 kMEEYV 847
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-251 |
4.06e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkpVRGpsqQVAFMLQkdllMPW---RSI 124
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV----IRG---SVAYVPQ----VSWifnATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QKNVELGmqirgrSKAERAEVAKAL--LARCH-LKGFENHYPHQL-------SGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:PLN03232 696 RENILFG------SDFESERYWRAIdvTALQHdLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 195 ALDAQtkmVLQQDLAQMLASE--GKTALMITHDLaEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:PLN03232 770 ALDAH---VAHQVFDSCMKDElkGKTRVLVTNQL-HFLPLMDRIILVSE--GMIKEEGT 822
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
56-249 |
7.33e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAGLYAPSEGQVTLAGK---------------------PVRGPSQQVAFM 112
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKvlMGHPKYEVTSGSILLDGEdilelspderaragiflafqyPVEIPGVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 L------QKDLLMPWRSIQKNVelgmqirgRSKAERAEVAKALLARCHLKGFenhyphqlSGGMRQRAALARTLAVEPDV 186
Cdd:COG0396 98 LrtalnaRRGEELSAREFLKLL--------KEKMKELGLDEDFLDRYVNEGF--------SGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 187 LLMDEPFSALDAQT-KMVlqQDLAQMLASEGKTALMITH-----DLAEAialsDRVFVMSErpGTIIEE 249
Cdd:COG0396 162 AILDETDSGLDIDAlRIV--AEGVNKLRSPDRGILIITHyqrilDYIKP----DFVHVLVD--GRIVKS 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
62-244 |
1.12e-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: 64.81 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 62 KAGEFVSLIGPSGCGKSTLLNMGAGLYAP------------------------------SEGQVTLAGKPvrgpsQQVaf 111
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVAHKP-----QYV-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 mlqkDLLmPwRSIQKNV-ELGMQIRGRSKAEraEVAKALlarcHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:COG1245 170 ----DLI-P-KVFKGTVrELLEKVDERGKLD--ELAEKL----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 191 EPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPG 244
Cdd:COG1245 238 EPSSYLDIYQRLNVAR-LIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPG 290
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
56-248 |
1.26e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.43 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK-----PVRGPSQQVAFMLQKDLLMPwRSIQKNVEL 130
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTIIPQDPTLFS-GTIRSNLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 gmqirgRSKAERAEVAKALLARchlKGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQ 210
Cdd:cd03369 105 ------FDEYSDEEIYGALRVS---EGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737829014 211 MLAseGKTALMITHDLaEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03369 171 EFT--NSTILTIAHRL-RTIIDYDKILVMDA--GEVKE 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
55-239 |
1.30e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----------------QQVAFMLQKDLL 118
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlarglvylpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MPWRSIQKNvELGMQIRGrsKAERAEVAK---ALLARChlkgfeNHyPHQ----LSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:PRK15439 360 WNVCALTHN-RRGFWIKP--ARENAVLERyrrALNIKF------NH-AEQaartLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737829014 192 PFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK15439 430 PTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-248 |
2.53e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 31 FAIEYRGVTRRFKNRQGKGEMtavsdvSIGIK-AGEFvSLIGPSGCGK-STLLNmgaglyapSEGQVTLAGKPV-----R 103
Cdd:PTZ00265 1228 FKNEHTNDMTNEQDYQGDEEQ------NVGMKnVNEF-SLTKEGGSGEdSTVFK--------NSGKILLDGVDIcdynlK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 104 GPSQQVAFMLQKDLLMPwRSIQKNVELGMQIRGRSKAERAEVAKALLArcHLKGFENHY-----PH--QLSGGMRQRAAL 176
Cdd:PTZ00265 1293 DLRNLFSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAIDE--FIESLPNKYdtnvgPYgkSLSGGQKQRIAI 1369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAeAIALSDRVFVMS--ERPGTIIE 248
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNnpDRTGSFVQ 1442
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
53-228 |
4.80e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGkpvrgpsqQVAFMLQKDLLMPWRSIQKNVELGM 132
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDaQTkmVLQQDLAQM- 211
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-QT--FAQKCLDKIy 187
|
170
....*....|....*...
gi 1737829014 212 -LASEGKTALMITHDLAE 228
Cdd:PRK13546 188 eFKEQNKTIFFVSHNLGQ 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
32-253 |
5.32e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.45 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLnMGAGLYAPSEGQV---------------- 95
Cdd:NF000106 13 AVEVRGLVKHF------GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRpwrf*twcanrralrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 96 TLAG-KPVRGPSQQvAFMLQKDLLMpwrsiqknveLGMQIRGRSKAERAEvAKALLARCHLKGFENHYPHQLSGGMRQRA 174
Cdd:NF000106 86 TIG*hRPVR*GRRE-SFSGRENLYM----------IGR*LDLSRKDARAR-ADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLaSEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDR--GRVIADGKVD 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
64-239 |
8.87e-11 |
|
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: 58.92 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 64 GEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGkpvrgpsqqvafmlqkdllmpwrsiqknvelgmqirgrskaerA 143
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------G 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 144 EVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQD-----LAQMLASEGKT 218
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLT 118
|
170 180
....*....|....*....|....*.
gi 1737829014 219 ALMITHDL-----AEAIALSDRVFVM 239
Cdd:smart00382 119 VILTTNDEkdlgpALLRRRFDRRIVL 144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
166-251 |
1.72e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM----VLQQdlaqmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYeiytIINE-----LAAEGKGVIVISSELPELLGMCDRIYVMNE 479
|
90
....*....|
gi 1737829014 242 rpGTIIEEIT 251
Cdd:NF040905 480 --GRITGELP 487
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
52-225 |
2.85e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTlagkpvRGPSQQVAFMLQ-KDLLMPWRSIQKNVEL 130
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH------CGTKLEVAYFDQhRAELDPEKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 GMQ---IRGRSKAeraevakallARCHLKGFENHyPHQ-------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK11147 407 GKQevmVNGRPRH----------VLGYLQDFLFH-PKRamtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
170 180
....*....|....*....|....*
gi 1737829014 201 KMVLQqdlaQMLASEGKTALMITHD 225
Cdd:PRK11147 476 LELLE----ELLDSYQGTVLLVSHD 496
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
54-224 |
3.18e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP----SQQVAFMLQKDLLMPWRSIQKNVE 129
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlctyQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 LGMQIrgrskaerAEVAKALLARCHLKGFENH--YP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:PRK13540 97 YDIHF--------SPGAVGITELCRLFSLEHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170
....*....|....*...
gi 1737829014 207 DLaQMLASEGKTALMITH 224
Cdd:PRK13540 169 KI-QEHRAKGGAVLLTSH 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
56-239 |
4.36e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtLAGKPVRGPSQQVAFM---LQKDLLmpWRSIQKNVELGM 132
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAWIMnatVRGNIL--FFDEEDAARLAD 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIR-GRSKAERAEVAKALLARCHLKGFenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT-KMVLQQDLAQ 210
Cdd:PTZ00243 755 AVRvSQLEADLAQLGGGLETEIGEKGV------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLG 828
|
170 180
....*....|....*....|....*....
gi 1737829014 211 MLAseGKTALMITHDLaEAIALSDRVFVM 239
Cdd:PTZ00243 829 ALA--GKTRVLATHQV-HVVPRADYVVAL 854
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
61-244 |
6.50e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG------KPVRGPSQQVAF--MLQKDLlmpwRSIQKN--VEL 130
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlKRFRGTELQNYFkkLYNGEI----KVVHKPqyVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 -GMQIRGR-----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV- 203
Cdd:PRK13409 172 iPKVFKGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNv 251
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737829014 204 --LQQDLAqmlasEGKTALMITHDLAEAIALSDRVFVMSERPG 244
Cdd:PRK13409 252 arLIRELA-----EGKYVLVVEHDLAVLDYLADNVHIAYGEPG 289
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-240 |
1.69e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 36 RGVTRRFKNRQGK-GEMT------------AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV 102
Cdd:PRK10982 233 RSLTQRFPDKENKpGEVIlevrnltslrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 103 RGPSQQVA----FMLQKD----------LLMPWRSIQKNVE-----LGMQIRGRSKAERAEVAKALLARChlkgfENHYP 163
Cdd:PRK10982 313 NNHNANEAinhgFALVTEerrstgiyayLDIGFNSLISNIRnyknkVGLLDNSRMKSDTQWVIDSMRVKT-----PGHRT 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 164 H--QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK10982 388 QigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQ-LIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
56-263 |
4.41e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS--------EGQVTLAGKPVRG-PSQQVAfMLQKDLLMPWR---- 122
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAiDAPRLA-RLRAVLPQAAQpafa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 -SIQKNVELGMQIRGRSKAERA----EVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLA---------VEPDVLL 188
Cdd:PRK13547 98 fSAREIVLLGRYPHARRAGALThrdgEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 189 MDEPFSALD-AQTKMVLqqDLAQMLASEGKT-ALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIER 263
Cdd:PRK13547 178 LDEPTAALDlAHQHRLL--DTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLAD--GAIVAHGAPADVLTPAHIAR 250
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
33-239 |
6.70e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.96 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLyAPSEGQVT-------------LAG 99
Cdd:PRK15093 4 LDIRNLTIEFKT--SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrfddidllrLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 100 KPVR---GPSQQVAFMLQKDLLMPWRSIQKNVEL---GMQIRGRSKAE---RAEVAKALLarcHLKGFENH------YPH 164
Cdd:PRK15093 81 RERRklvGHNVSMIFQEPQSCLDPSERVGRQLMQnipGWTYKGRWWQRfgwRKRRAIELL---HRVGIKDHkdamrsFPY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-241 |
1.40e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 8 KDANVAEAYADARhAQPAAAPLPFAIEYRGVTRRFKNRQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGA-- 85
Cdd:TIGR00956 33 KNLSAYGVAADSD-YQPTFPNALLKILTRGFRKLKKFRDTK-TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 86 --GLYAPSEGQVTLAG-------KPVRGpsqQVAFMLQKDLLMPWRSIQKNVELGMQIR-------GRSKAERAE----V 145
Cdd:TIGR00956 111 tdGFHIGVEGVITYDGitpeeikKHYRG---DVVYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKhiadV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 146 AKALLARCHLKGFE--NHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMIT 223
Cdd:TIGR00956 188 YMATYGLSHTRNTKvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAI 267
|
250
....*....|....*....
gi 1737829014 224 HDLAE-AIALSDRVFVMSE 241
Cdd:TIGR00956 268 YQCSQdAYELFDKVIVLYE 286
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
61-200 |
1.52e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrgpsqqVAfMLQKDllmPWRSIQKNV---------ELG 131
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI------VA-RLQQD---PPRNVEGTVydfvaegieEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 132 MQIRG----RSKAERAEVAKAL--LARC-----HLKG--FENHY----------PHQ----LSGGMRQRAALARTLAVEP 184
Cdd:PRK11147 96 EYLKRyhdiSHLVETDPSEKNLneLAKLqeqldHHNLwqLENRInevlaqlgldPDAalssLSGGWLRKAALGRALVSNP 175
|
170
....*....|....*.
gi 1737829014 185 DVLLMDEPFSALDAQT 200
Cdd:PRK11147 176 DVLLLDEPTNHLDIET 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-239 |
1.66e-08 |
|
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: 55.72 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 22 AQPAAAPLPFAIEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTllnMGAGLY---APSEGQVTLA 98
Cdd:TIGR00957 1274 APPSGWPPRGRVEFRNYCLRYR----EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIID 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 99 GkpvrgpsQQVAFMLQKDL-----LMPWRSIQKNVELGMQIRGRSKAERAEVAKAL-LArcHLKGFENHYP----HQ--- 165
Cdd:TIGR00957 1347 G-------LNIAKIGLHDLrfkitIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALeLA--HLKTFVSALPdkldHEcae 1417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 166 ----LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLaEAIALSDRVFVM 239
Cdd:TIGR00957 1418 ggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF--EDCTVLTIAHRL-NTIMDYTRVIVL 1492
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
58-222 |
8.93e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 58 SIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLA-GKPVRGPSQQvafmLQKDLLMPWrsiQKN----VELGM 132
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRLSFEQ----LQKLVSDEW---QRNntdmLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSKAE--RAEVAKAllARCHLKGFENHYPH-------QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:PRK10938 96 DDTGRTTAEiiQDEVKDP--ARCEQLAQQFGITAlldrrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|....*....
gi 1737829014 204 LQQDLAQmLASEGKTALMI 222
Cdd:PRK10938 174 LAELLAS-LHQSGITLVLV 191
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
46-239 |
1.60e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 46 QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNmgaglyapsegQVTLAgkpvrgpsqqvafmlqkdLLMpwRSIQ 125
Cdd:cd03227 3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD-----------AIGLA------------------LGG--AQSA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVELGMQIRGRSKAERAEVAKALlarchlkgfenhypHQLSGGMRQRAALARTLA---VEPDVL-LMDEPFSALDAQTk 201
Cdd:cd03227 52 TRRRSGVKAGCIVAAVSAELIFTR--------------LQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRD- 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737829014 202 mvlQQDLAQMLAS---EGKTALMITHDLaEAIALSDRVFVM 239
Cdd:cd03227 117 ---GQALAEAILEhlvKGAQVIVITHLP-ELAELADKLIHI 153
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-240 |
2.45e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 21 HAQPAAAPLPFAIEYRGVTRRFKNrqgkgEMTAV-SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG 99
Cdd:PLN03130 1226 NRPPPGWPSSGSIKFEDVVLRYRP-----ELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 100 KPVR----------------GP---SQQVAFMLQ-------KDLlmpWRSIQKnVELGMQIRGRSKAERAEVAKallarc 153
Cdd:PLN03130 1301 CDISkfglmdlrkvlgiipqAPvlfSGTVRFNLDpfnehndADL---WESLER-AHLKDVIRRNSLGLDAEVSE------ 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 154 hlkGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASegKTALMITHDLAEAIAlS 233
Cdd:PLN03130 1371 ---AGEN-----FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIID-C 1439
|
....*..
gi 1737829014 234 DRVFVMS 240
Cdd:PLN03130 1440 DRILVLD 1446
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-253 |
2.90e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA 110
Cdd:PRK15064 319 ALEVENLTKGFDNG------PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 FMLQKDL-LMPWRSiqknvelgmQIRGRSKAEraEVAKALLARCHLKGFE-NHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK15064 393 YDFENDLtLFDWMS---------QWRQEGDDE--QAVRGTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMlasEGkTALMITHdlaeaialsDRVFVMSerPGTIIEEITVD 253
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKY---EG-TLIFVSH---------DREFVSS--LATRIIEITPD 511
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-248 |
7.88e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 13 AEAYADARHAQPAAA-PLPFAIEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS 91
Cdd:PLN03232 1214 SEATAIIENNRPVSGwPSRGSIKFEDVHLRYR----PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 92 EGQVTLAGKPVrgpsqqVAFMLqKDL-----LMPWRSIQKNVELGMQIRGRSKAERAEVAKALlARCHLKGFENHYPHQL 166
Cdd:PLN03232 1290 KGRIMIDDCDV------AKFGL-TDLrrvlsIIPQSPVLFSGTVRFNIDPFSEHNDADLWEAL-ERAHIKDVIDRNPFGL 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 167 -----------SGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASegKTALMITHDLaEAIALSDR 235
Cdd:PLN03232 1362 daevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRL-NTIIDCDK 1438
|
250
....*....|...
gi 1737829014 236 VFVMSErpGTIIE 248
Cdd:PLN03232 1439 ILVLSS--GQVLE 1449
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
56-213 |
1.16e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLyAPSEGQVTLAGKPVRGPSQQV---AF-MLQKDLLMPWRSIQKNVELG 131
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTwrkAFgVIPQKVFIFSGTFRKNLDPY 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 132 MQIrgrSKAERAEVAKALLARCHLKGFENHYPHQL-------SGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:TIGR01271 1316 EQW---SDEEIWKVAEEVGLKSVIEQFPDKLDFVLvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392
|
....*....
gi 1737829014 205 QQDLAQMLA 213
Cdd:TIGR01271 1393 RKTLKQSFS 1401
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
42-224 |
1.55e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 42 FKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGpsqQVAFMLQ 114
Cdd:PRK13541 4 LHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCT---YIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 KDLLMpwrSIQKNVELGMQIRgrskaERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:PRK13541 81 LKLEM---TVFENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180 190
....*....|....*....|....*....|
gi 1737829014 195 ALDAQTKMVLqQDLAQMLASEGKTALMITH 224
Cdd:PRK13541 153 NLSKENRDLL-NNLIVMKANSGGIVLLSSH 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-227 |
2.03e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 4 SIQLKDANVAEAYA-DARHAQPAAAPLpfaIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN 82
Cdd:PRK10938 234 SEQLEGVQLPEPDEpSARHALPANEPR---IVLNNGVVSYNDR------PILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 83 MGAGLYAPS-EGQVTLAGKPvRGPSQQVAFMLQK------DLLMPWR--SIQKNVEL-------GMqIRGRSKAERaEVA 146
Cdd:PRK10938 305 LITGDHPQGySNDLTLFGRR-RGSGETIWDIKKHigyvssSLHLDYRvsTSVRNVILsgffdsiGI-YQAVSDRQQ-KLA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 147 KALLARCHLKGFENHYP-HQLSGGmRQRAAL-ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLaSEGKTALM--- 221
Cdd:PRK10938 382 QQWLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLI-SEGETQLLfvs 459
|
250
....*....|....*
gi 1737829014 222 ---------ITHDLA 227
Cdd:PRK10938 460 hhaedapacITHRLE 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
165-224 |
2.73e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.73e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaseGKTALMITH 224
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSH 399
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
54-202 |
2.98e-06 |
|
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: 48.21 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYapsegqvtlagkPVRG-----PSQQVAFMLQKDLLMPWRSIQKNV 128
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW------------PVYGgrltkPAKGKLFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 -----ELGMQIRGRSKAEraevAKALLARCHLK-------GFE--NHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:TIGR00954 536 iypdsSEDMKRRGLSDKD----LEQILDNVQLThileregGWSavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170
....*....|
gi 1737829014 195 AL--DAQTKM 202
Cdd:TIGR00954 612 AVsvDVEGYM 621
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
61-224 |
3.72e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGlyAPSEGQVTLAGKPVRGPSQQVAF------MLQKDLLMPWRSIQKNVELGMQI 134
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFqrsigyVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSKAERAEVAKALLARCHLKGFENhYPHQLSG----GM----RQRAALARTLAVEPDVLL-MDEPFSALDAQTKMVLQ 205
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEVIKLLEMES-YADAVVGvpgeGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*....
gi 1737829014 206 QdLAQMLASEGKTALMITH 224
Cdd:TIGR00956 943 K-LMRKLADHGQAILCTIH 960
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
61-260 |
4.44e-06 |
|
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: 46.83 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----KPVRGPSQQVAFMLQKDLLMPwRSIQKNVELGMQIR 135
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRLSIILQDPILFS-GSIRFNLDPECKCT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 136 GRSKAERAEVA------KAL---LARCHLKGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:cd03288 123 DDRLWEALEIAqlknmvKSLpggLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 207 DLaqMLASEGKTALMITHdLAEAIALSDRVFVMSErpGTIIEEITVD--LPHRDNP 260
Cdd:cd03288 198 VV--MTAFADRTVVTIAH-RVSTILDADLVLVLSR--GILVECDTPEnlLAQEDGV 248
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
56-241 |
8.66e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtlagkpVRGPSQQVAFMLQK--DLLmpwrSIQKNVELGMq 133
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVRMAVFSQHhvDGL----DLSSNPLLYM- 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 irgrSKAERAEVAKALlaRCHLKGF--------ENHYphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQ 205
Cdd:PLN03073 596 ----MRCFPGVPEQKL--RAHLGSFgvtgnlalQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
170 180 190
....*....|....*....|....*....|....*.
gi 1737829014 206 QDLAqmLASEGktALMITHDLAEAIALSDRVFVMSE 241
Cdd:PLN03073 668 QGLV--LFQGG--VLMVSHDEHLISGSVDELWVVSE 699
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
53-239 |
1.32e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF-----MLQKDL-LMPWRSIQK 126
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengisMVHQELnLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELG-MQIRG----RSKAERAevAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTK 201
Cdd:PRK10982 93 NMWLGrYPTKGmfvdQDKMYRD--TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737829014 202 MVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK10982 171 NHLFT-IIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
52-241 |
1.58e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.62 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYApSEGQVTLAG-----KPVRGPSQQVAFMLQKDLLMPwRSIQK 126
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnsVPLQKWRKAFGVIPQKVFIFS-GTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQirgRSKAERAEVAKALlarcHLKGFENHYPHQL-----------SGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:cd03289 96 NLDPYGK---WSDEEIWKVAEEV----GLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1737829014 196 LDAQTKMVLQQDLAQMLAseGKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03289 169 LDPITYQVIRKTLKQAFA--DCTVILSEHRI-EAMLECQRFLVIEE 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
61-225 |
4.09e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGkpvrgpSQQVAFMLQKDLLMPWRSIQ---------KNVELG 131
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------NWQLAWVNQETPALPQPALEyvidgdreyRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 132 MQ-------------IRGRSKAERAEVAKALLARC-HLKGFENHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:PRK10636 98 LHdanerndghaiatIHGKLDAIDAWTIRSRAASLlHGLGFSNEQLERpvsdFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190
....*....|....*....|....*....|..
gi 1737829014 194 SALDAQTKMVLQqdlaQMLASEGKTALMITHD 225
Cdd:PRK10636 178 NHLDLDAVIWLE----KWLKSYQGTLILISHD 205
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
61-197 |
5.19e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 61 IKAGEFVSLIGPSGCGKSTLLNMGAGL--YAPSEGQVTLAGK---------------------PVRGPSQQVAFMLQKDL 117
Cdd:PRK09580 24 VRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllelspedragegifmafqyPVEIPGVSNQFFLQTAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 --LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFenhyphqlSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:PRK09580 104 naVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGF--------SGGEKKRNDILQMAVLEPELCILDESDSG 175
|
..
gi 1737829014 196 LD 197
Cdd:PRK09580 176 LD 177
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-225 |
6.11e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 24 PAAAPLPFAIEYRG-------VTRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:PRK10636 291 PAHVDNPFHFSFRApeslpnpLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 97 LAgKPVRgpsqqVAFMLQKDL--LMPWRS-IQKNVELGMQirgrskaeraEVAKALlaRCHLKGFENH------YPHQLS 167
Cdd:PRK10636 371 LA-KGIK-----LGYFAQHQLefLRADESpLQHLARLAPQ----------ELEQKL--RDYLGGFGFQgdkvteETRRFS 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALDaqtkMVLQQDLAQMLASEGKTALMITHD 225
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHD 486
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
69-225 |
7.30e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELG-------MQIRGR--SK 139
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD------PNERLGKLRQDQFAFEEFTVLDTVIMGhtelwevKQERDRiyAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 140 AERAE-----VAKALLARCHLKGF-----------------ENHYP--HQLSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:PRK15064 106 PEMSEedgmkVADLEVKFAEMDGYtaearagelllgvgipeEQHYGlmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNN 185
|
170 180 190
....*....|....*....|....*....|
gi 1737829014 196 LDAQTKmvlqQDLAQMLASEGKTALMITHD 225
Cdd:PRK15064 186 LDINTI----RWLEDVLNERNSTMIIISHD 211
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
69-226 |
1.21e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 69 LIGPSGCGKSTLLN-MGAGLYAPSEGQVTLAGKPVRGPSQQVAFML------------------QKDLLMPWRSIQKNVE 129
Cdd:COG0419 28 IVGPNGAGKSTILEaIRYALYGKARSRSKLRSDLINVGSEEASVELefehggkryrierrqgefAEFLEAKPSERKEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 --LGM----QIRGRSKAERAEVAKALLARCHLKGFENHY---------PHQLSGGMRQRAALARTLAvepdvLLMDepFS 194
Cdd:COG0419 108 rlLGLeiyeELKERLKELEEALESALEELAELQKLKQEIlaqlsgldpIETLSGGERLRLALADLLS-----LILD--FG 180
|
170 180 190
....*....|....*....|....*....|..
gi 1737829014 195 ALDAQTKmvlqQDLAQMLasegKTALMITHDL 226
Cdd:COG0419 181 SLDEERL----ERLLDAL----EELAIITHVI 204
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
166-244 |
2.65e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 LSGGMRQRAALARTLAVEPD--VLLMDEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDlAEAIALSDRVFVMSERP 243
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLIN-VIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGPGA 554
|
.
gi 1737829014 244 G 244
Cdd:PRK00635 555 G 555
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
71-244 |
9.41e-04 |
|
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: 39.56 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 71 GPSGCGKSTLLNmgAGLYApsegqvtLAGKPVRGPSQQ---VAFMLQKDLLmpwrsiqkNVELGMQIRGRS-KAER---- 142
Cdd:cd03279 35 GPTGAGKSTILD--AITYA-------LYGKTPRYGRQEnlrSVFAPGEDTA--------EVSFTFQLGGKKyRVERsrgl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 143 -AEVAK--ALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP----------DVLLMDEPFSALDAQTKMVLQQDLA 209
Cdd:cd03279 98 dYDQFTriVLLPQGEFDRFLARPVSTLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGFGTLDPEALEAVATALE 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1737829014 210 QmLASEGKTALMITH--DLAEAIALsdRVFVMSERPG 244
Cdd:cd03279 178 L-IRTENRMVGVISHveELKERIPQ--RLEVIKTPGG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-239 |
1.43e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 24 PAAAPLPF---AIEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK 100
Cdd:PTZ00243 1297 TSAAPHPVqagSLVFEGVQMRYR----EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 101 PV-----RGPSQQVAfMLQKDLLMPWRSIQKNVELGMQirgrskAERAEVAKAL---------------LARCHLKGFEN 160
Cdd:PTZ00243 1373 EIgayglRELRRQFS-MIPQDPVLFDGTVRQNVDPFLE------ASSAEVWAALelvglrervasesegIDSRVLEGGSN 1445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 161 HyphqlSGGMRQRAALARTLAVE-PDVLLMDEPFS----ALDAQTKMVLqqdlaqMLASEGKTALMITHDLaEAIALSDR 235
Cdd:PTZ00243 1446 Y-----SVGQRQLMCMARALLKKgSGFILMDEATAnidpALDRQIQATV------MSAFSAYTVITIAHRL-HTVAQYDK 1513
|
....
gi 1737829014 236 VFVM 239
Cdd:PTZ00243 1514 IIVM 1517
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
3-80 |
3.23e-03 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 38.96 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 3 RSIQLKDANVAEAYADARHAQPAAAPLPFAIEYRGVTRRFKNRQGKGEM--TAVSDVSIGIKAGEFVSLIGPSGCGKSTL 80
Cdd:cd14894 38 RFTSIYDEQVVLTYADTANAETVLAPHPFAIAKQSLVRLFFDNEHTMPLpsTISSNRSMTEGRGQSLFLCGESGSGKTEL 117
|
|
|