|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
5.27e-125 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 353.63 E-value: 5.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQN 80
Cdd:COG1116 21 GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTD 160
Cdd:COG1116 101 VALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 161 LLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEIKVPFKHPRNR 216
Cdd:COG1116 181 LLRLWQETG---KTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDR 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-210 |
5.75e-115 |
|
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: 326.74 E-value: 5.75e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQN 80
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDALLPWLTVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTD 160
Cdd:cd03293 94 VALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 161 LLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEIKVPF 210
Cdd:cd03293 174 LLDIWRETG---KTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-210 |
4.48e-86 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 255.17 E-value: 4.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAG 84
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 85 LEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDL 164
Cdd:COG4525 101 LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 165 WTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEIKVPF 210
Cdd:COG4525 181 WQRTG---KGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDF 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-216 |
4.76e-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: 250.79 E-value: 4.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVL 78
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEkrNVGMVFQDYALFPHLTVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:COG3842 96 ENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMR 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 159 TDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVI-----AEIkvpFKHPRNR 216
Cdd:COG3842 176 EELRRL--QRELGI-TFIYVTHDQEEALALADRIAVMND--GRIEqvgtpEEI---YERPATR 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-204 |
2.50e-82 |
|
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: 243.97 E-value: 2.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVL 78
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvPPErrNIGMVFQDYALFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:cd03259 91 ENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 159 TDLLDLWTQGRMPiksVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:cd03259 171 EELKELQRELGIT---TIYVTHDQEEALALADRIAVMNE--GRIVQ 211
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-203 |
2.39e-79 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 242.32 E-value: 2.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE-------GVAMVFQTFALFPWLTV 77
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlsKKElrelrrkKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLtaetL 157
Cdd:COG4175 123 LENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL----I 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 158 RTD----LLDLwtQGRMPiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:COG4175 199 RREmqdeLLEL--QAKLK-KTIVFITHDLDEALRLGDRIAIMKD--GRIV 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-203 |
1.48e-74 |
|
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: 226.37 E-value: 1.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 9 DANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQ 79
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkkISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 160 DLLDLwtQGRMPiKSVLIVTHNIEEAVFMCDRILVLssNPGRVI 203
Cdd:cd03294 202 ELLRL--QAELQ-KTIVFITHDLDEALRLGDRIAIM--KDGRLV 240
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-216 |
1.45e-72 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 223.87 E-value: 1.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT---GPAE-GVAMVFQTFALFPWLTVLQNV 81
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlPPRErRVGFVFQHYALFPHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDL 161
Cdd:COG1118 97 AFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 162 LDLWTqgRMPIKSVLiVTHNIEEAVFMCDRILVLSSnpGRVIA-----EIkvpFKHPRNR 216
Cdd:COG1118 177 RRLHD--ELGGTTVF-VTHDQEEALELADRVVVMNQ--GRIEQvgtpdEV---YDRPATP 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-210 |
8.74e-71 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 216.10 E-value: 8.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGL 85
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 EALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLW 165
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 166 TQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEIKVPF 210
Cdd:PRK11248 176 QETG---KQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNF 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-205 |
7.16e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 205.30 E-value: 7.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTV 77
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrrrIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 158 RTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1131 171 WELLRELAAEG----KTVLLSTHYLEEAERLCDRVAIIDK--GRIVAD 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-216 |
8.22e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 209.16 E-value: 8.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVL 78
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlpPKDrNIAMVFQSYALYPHMTVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:COG3839 94 ENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 159 TDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLssNPGRVI-----AEIkvpFKHPRNR 216
Cdd:COG3839 174 AEIKRL--HRRLGT-TTIYVTHDQVEAMTLADRIAVM--NDGRIQqvgtpEEL---YDRPANL 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-205 |
1.42e-66 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 204.83 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFP 73
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelrrrIGMLFQGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVEAGL-EALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:COG1127 96 SLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 153 TAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1127 176 TSAVIDELIREL--RDELGL-TSVVVTHDLDSAFAIADRVAVLAD--GKIIAE 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-206 |
1.86e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 204.12 E-value: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFAL 71
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlrrrhIGFVFQFFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:COG1136 98 LPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 152 LTAETLRTDLLDLWTQGRMpikSVLIVTHNiEEAVFMCDRILVLSSnpGRVIAEI 206
Cdd:COG1136 178 KTGEEVLELLRELNRELGT---TIVMVTHD-PELAARADRVIRLRD--GRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-196 |
4.64e-66 |
|
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: 202.72 E-value: 4.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFP 73
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafrrrhIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:cd03255 96 DLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956089794 154 AETLRTDLLDLWTQGRmpiKSVLIVTHNiEEAVFMCDRILVLS 196
Cdd:cd03255 176 GKEVMELLRELNKEAG---TTIVVVTHD-PELAEYADRIIELR 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-216 |
8.23e-65 |
|
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: 200.16 E-value: 8.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PA--EGVAMVFQTFALFPWLTVL 78
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPhkRPVNTVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:cd03300 91 ENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 159 TDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLssNPGRvIAEIKVP---FKHPRNR 216
Cdd:cd03300 171 LELKRL--QKELGI-TFVFVTHDQEEALTMSDRIAVM--NKGK-IQQIGTPeeiYEEPANR 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
7-217 |
3.08e-63 |
|
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: 196.15 E-value: 3.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGLE 86
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 ALGVGAR--ERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDL 164
Cdd:TIGR01184 81 RVLPDLSksERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 165 WTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEI-KVPFKHPRNRL 217
Cdd:TIGR01184 161 WEEHRV---TVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFPRPRDRL 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-215 |
5.45e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 195.60 E-value: 5.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-------EGVAMVFQTFALFPW 74
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdinklrRKVGMVFQQFNLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VL 152
Cdd:COG1126 92 LTVLENVtLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpEL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 153 TAETLRTdLLDLWTQGR-MpiksvLIVTHNIEEAVFMCDRILVLSsnpGRVIAEIKVP---FKHPRN 215
Cdd:COG1126 172 VGEVLDV-MRDLAKEGMtM-----VVVTHEMGFAREVADRVVFMD---GGRIVEEGPPeefFENPQH 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-205 |
5.73e-63 |
|
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: 203.60 E-value: 5.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQ--TFAL 71
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrelrrrVQMVFQdpYSSL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVEAGLEALGVG-ARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:COG1123 356 NPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 150 DVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1123 436 DVSVQAQILNLLRDLQRELGL---TYLFISHDLAVVRYIADRVAVMYD--GRIVED 486
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-205 |
1.39e-61 |
|
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: 191.95 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE------GVAMVFQTFALFP 73
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAElyrlrrRMGMLFQSGALFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVEAGL-EALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:cd03261 91 SLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 153 TAETLRTDLLDLwtqGRMPIKSVLIVTHNIEEAVFMCDRILVLSsnPGRVIAE 205
Cdd:cd03261 171 ASGVIDDLIRSL---KKELGLTSIMVTHDLDTAFAIADRIAVLY--DGKIVAE 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-195 |
4.18e-61 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 190.41 E-value: 4.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQ--TFA 70
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirrkeIQMVFQdpMSS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 71 LFPWLTVLQNVEAGLEALGV--GARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:cd03257 95 LNPRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956089794 148 ALDVLT-AETLRTdLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 195
Cdd:cd03257 175 ALDVSVqAQILDL-LKKLQEELGL---TLLFITHDLGVVAKIADRVAVM 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-205 |
2.40e-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: 188.70 E-value: 2.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAEG---VAMVFQtfalFPWL 75
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkkNLRELrrkVGLVFQ----NPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 -----TVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:COG1122 87 qlfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1122 167 PRGRRELLELLKRLNKEG----KTVIIVTHDLDLVAELADRVIVLDD--GRIVAD 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-203 |
7.83e-60 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 189.92 E-value: 7.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE---GVAMVFQTFALFPWLTVLQN 80
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDldPVElrrRIGYVIQQIGLFPHMTVAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIGLD--GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:COG1125 97 IATVPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 159 TDLLDLwtQGRMPiKSVLIVTHNIEEAVFMCDRILVLssNPGRVI 203
Cdd:COG1125 177 DELLRL--QRELG-KTIVFVTHDIDEALKLGDRIAVM--REGRIV 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-208 |
9.75e-60 |
|
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: 187.70 E-value: 9.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-----VAMVFQ--TFALFPWLTVL 78
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafrrrVQMVFQdpYASLHPRHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGarERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AET 156
Cdd:COG1124 100 RILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqAEI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 157 LRTdLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKV 208
Cdd:COG1124 178 LNL-LKDLREERGL---TYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTV 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-197 |
1.17e-58 |
|
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: 182.77 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-------VAMVFQTFALFPW 74
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpplrrrIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNVeaglealgvgarerreralaaidligldgfenAYPreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 154
Cdd:cd03229 91 LTVLENI--------------------------------ALG--LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956089794 155 ETLRTDLLDLWTQGRMPiksVLIVTHNIEEAVFMCDRILVLSS 197
Cdd:cd03229 137 REVRALLKSLQAQLGIT---VVLVTHDLDEAARLADRVVVLRD 176
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
1.21e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 187.59 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE------GVAMVFQTFALF 72
Cdd:COG1135 15 GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlsERElraarrKIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvl 152
Cdd:COG1135 95 SSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 153 tAETLRtDLLDLwtqgrmpIKS--------VLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKVP--FKHPRNRL 217
Cdd:COG1135 173 -PETTR-SILDL-------LKDinrelgltIVLITHEMDVVRRICDRVAVLEN--GRIVEQGPVLdvFANPQSEL 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-215 |
3.77e-58 |
|
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: 183.31 E-value: 3.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVL 78
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpVQErNVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGAR----ERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 154
Cdd:cd03296 93 DNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 155 ETLRTDLLDLwtQGRMPIKSVLiVTHNIEEAVFMCDRILVLssNPGRVIaEIKVP---FKHPRN 215
Cdd:cd03296 173 KELRRWLRRL--HDELHVTTVF-VTHDQEEALEVADRVVVM--NKGRIE-QVGTPdevYDHPAS 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-214 |
1.11e-57 |
|
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: 182.01 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFP 73
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkarrrIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:cd03258 96 SRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 154 AETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKVP--FKHPR 214
Cdd:cd03258 176 TQSILALLRDI--NRELGL-TIVLITHEMEVVKRICDRVAVMEK--GEVVEEGTVEevFANPQ 233
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
2-203 |
7.40e-57 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 184.60 E-value: 7.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGL---------IEPTGGEVtylgKPLTGPA--------EGVAM 64
Cdd:TIGR03415 35 GLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLnpvsrgsvlVKDGDGSV----DVANCDAatlrrlrtHRVSM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 65 VFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:TIGR03415 111 VFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 145 PFSALDVLTAETLRTDLLDLwtQGRMPiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:TIGR03415 191 PFSALDPLIRTQLQDELLEL--QSKLK-KTIVFVSHDLDEALKIGNRIAIMEG--GRII 244
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-195 |
9.57e-57 |
|
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: 179.80 E-value: 9.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFPWLTVLQN 80
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVElrrKIGYVIQQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIGLD--GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:cd03295 96 IALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQ 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956089794 159 TDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:cd03295 176 EEFKRLQQELG---KTIVFVTHDIDEAFRLADRIAIM 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-193 |
2.15e-56 |
|
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: 178.11 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAE-------GVAMVFQTFALFPW 74
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninelrqKVGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV-L 152
Cdd:cd03262 91 LTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPeL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956089794 153 TAETLRTdLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRIL 193
Cdd:cd03262 171 VGEVLDV-MKDLAEEG----MTMVVVTHEMGFAREVADRVI 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-205 |
2.52e-56 |
|
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: 178.90 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTV 77
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREarrqIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 158 RTDLLDLWTQGRMpiksVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG4555 172 REILRALKKEGKT----VLFSSHIMQEVEALCDRVVILHK--GKVVAQ 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-202 |
5.59e-56 |
|
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: 177.06 E-value: 5.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE-GVAMVFQTFALFPWLTVL 78
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlPPKDrDIAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:cd03301 91 DNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 159 TDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLssNPGRV 202
Cdd:cd03301 171 AELKRL--QQRLGT-TTIYVTHDQVEAMTMADRIAVM--NDGQI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-196 |
1.65e-55 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 175.73 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQ-----TFA 70
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelRRKVGLVFQnpddqFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 71 LfpwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:cd03225 91 P----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 151 VLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLS 196
Cdd:cd03225 167 PAGRRELLELLKKLKAEG----KTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
16-204 |
1.34e-54 |
|
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: 173.64 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 16 EGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPL--------TGPAE-GVAMVFQTFALFPWLTVLQNVEAGLE 86
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinLPPQQrKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 alGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWT 166
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956089794 167 QGRMPiksVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:cd03297 180 NLNIP---VIFVTHDLSEAEYLADRIVVMED--GRLQY 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-203 |
1.75e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 171.78 E-value: 1.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE------GVAMVFQTFALFPWLTV 77
Cdd:COG3638 18 ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalRGRAlrrlrrRIGMIFQQFNLVPRLSV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEA--------LGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:COG3638 98 LTNVLAGRLGrtstwrslLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 150 DVLTAETLRTDLLDLWTQGRMPiksVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:COG3638 178 DPKTARQVMDLLRRIAREDGIT---VVVNLHQVDLARRYADRIIGLRD--GRVV 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-204 |
9.28e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 169.08 E-value: 9.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAEGVA-------MVFQTFALFPWLTV 77
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPylrrrigVVFQDFRLLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAEtl 157
Cdd:COG2884 97 YENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSW-- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 158 rtDLLDLWTQ----GrmpiKSVLIVTHNIEeavfmcdrilVLSSNPGRVIA 204
Cdd:COG2884 175 --EIMELLEEinrrG----TTVLIATHDLE----------LVDRMPKRVLE 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-214 |
1.07e-52 |
|
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: 171.77 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP---TGGEVTYLGKPLTG--PAE-------GVAMVFQ- 67
Cdd:COG0444 15 RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsEKElrkirgrEIQMIFQd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 68 --TfALFPWLTVLQNVEAGLEA-LGVGARERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTILL 141
Cdd:COG0444 95 pmT-SLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 142 MDEPFSALDVLT-AETLRTdLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRV--IAEIKVPFKHPR 214
Cdd:COG0444 174 ADEPTTALDVTIqAQILNL-LKDLQRELGL---AILFITHDLGVVAEIADRVAVMYA--GRIveEGPVEELFENPR 243
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-216 |
1.51e-52 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 172.60 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA---EGVAMVFQTFALFPWLTVL 78
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqRDICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 159 TDLLDLwtQGRMPIKSvLIVTHNIEEAVFMCDRILVLssNPGRV--IAEIKVPFKHPRNR 216
Cdd:PRK11432 177 EKIREL--QQQFNITS-LYVTHDQSEAFAVSDTVIVM--NKGKImqIGSPQELYRQPASR 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-205 |
2.05e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.73 E-value: 2.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFAL---FPwLTVL 78
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdwdFP-ITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEA----LGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 154
Cdd:COG1121 96 DVVLMGRYGrrglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 155 ETLrTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSsnpGRVIAE 205
Cdd:COG1121 176 EAL-YELLRELRREGK---TILVVTHDLGAVREYFDRVLLLN---RGLVAH 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-202 |
2.35e-52 |
|
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: 166.42 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTV 77
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkrrIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVeaglealgvgarerreralaaidligldgfenayprELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:cd03230 91 RENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 158 RTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRV 202
Cdd:cd03230 135 WELLRELKKEG----KTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-215 |
3.55e-52 |
|
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: 167.90 E-value: 3.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQNVE 82
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlPPEkrDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLL 162
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 163 DLWTQGRMPiksVLIVTHNIEEAVFMCDRILVLssNPGRVIA--EIKVPFKHPRN 215
Cdd:cd03299 174 KIRKEFGVT---VLHVTHDFEEAWALADKVAIM--LNGKLIQvgKPEEVFKKPKN 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-208 |
1.77e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 166.08 E-value: 1.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 10 ANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVLQNVeagle 86
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlpPAErPVSMLFQENNLFPHLTVAQNI----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 ALGVGA-----RERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDL 161
Cdd:COG3840 93 GLGLRPglkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD----PALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 162 LDLWTQ-----GRmpikSVLIVTHNIEEAVFMCDRILVLssNPGRVIAEIKV 208
Cdd:COG3840 169 LDLVDElcrerGL----TVLMVTHDPEDAARIADRVLLV--ADGRIAADGPT 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-205 |
7.33e-51 |
|
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: 172.01 E-value: 7.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTG---GEVTYLGKPLTGPAEG-----VAMVFQTF--AL 71
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAlrgrrIGMVFQDPmtQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:COG1123 97 NP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 152 LTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLssNPGRVIAE 205
Cdd:COG1123 176 TTQAEILDLLRELQRERGT---TVLLITHDLGVVAEIADRVVVM--DDGRIVED 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-203 |
7.36e-51 |
|
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: 164.66 E-value: 7.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFPWLTV 77
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqIGMIFQQFNLIERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEA--------LGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:cd03256 96 LENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 150 DVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:cd03256 176 DPASSRQVMDLLKRINREEGI---TVIVSLHQVDLAREYADRIVGLKD--GRIV 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-205 |
1.68e-50 |
|
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: 163.76 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWL 75
Cdd:cd03219 11 GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlpPHEiarlGIGRTFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGLEALGVGA----------RERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:cd03219 91 TVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 146 FSAL-DVLTAETLRTdLLDLWTQGRmpikSVLIVTHNIeEAVF-MCDRILVLSSnpGRVIAE 205
Cdd:cd03219 171 AAGLnPEETEELAEL-IRELRERGI----TVLLVEHDM-DVVMsLADRVTVLDQ--GRVIAE 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
22-216 |
1.89e-49 |
|
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: 163.82 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 22 LLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRER 98
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNvPPHlrHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 99 ALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIKSVLiV 178
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI--QEQLGITFVF-V 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956089794 179 THNIEEAVFMCDRILVLSSnpGRvIAEIKVP---FKHPRNR 216
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRK--GK-IAQIGTPeeiYEEPANL 195
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-204 |
2.14e-49 |
|
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: 160.01 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFAL---FPwLTVLQNVE 82
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFP-ISVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEA----LGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLr 158
Cdd:cd03235 93 MGLYGhkglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 159 TDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSsnpGRVIA 204
Cdd:cd03235 172 YELLRELRREGM---TILVVTHDLGLVLEYFDRVLLLN---RTVVA 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-215 |
2.68e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 164.74 E-value: 2.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAEG--VAMVFQTFALFPWLTVLQNVE 82
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENrhVNTVFQSYALFPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLL 162
Cdd:PRK09452 109 FGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELK 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 163 DLwtQGRMPIKSVLiVTHNIEEAVFMCDRILVLssNPGRvIAEIKVP---FKHPRN 215
Cdd:PRK09452 189 AL--QRKLGITFVF-VTHDQEEALTMSDRIVVM--RDGR-IEQDGTPreiYEEPKN 238
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-205 |
8.33e-49 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 159.82 E-value: 8.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWL 75
Cdd:COG0411 15 GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpPHRiarlGIARTFQNPRLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGLEA-------------LGVGARER--RERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 140
Cdd:COG0411 95 TVLENVLVAAHArlgrgllaallrlPRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 141 LMDEPFSAL-DVLTAETLRTdLLDLWTQGRMpikSVLIVTHNIeEAVF-MCDRILVLSSnpGRVIAE 205
Cdd:COG0411 175 LLDEPAAGLnPEETEELAEL-IRRLRDERGI---TILLIEHDM-DLVMgLADRIVVLDF--GRVIAE 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
7-147 |
8.35e-49 |
|
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: 156.65 E-value: 8.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAE-----GVAMVFQTFALFPWLTVLQNV 81
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEALGVGARERRERALAAIDLIGLDGFEN----AYPRELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-197 |
1.05e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 164.05 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFALF 72
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrrkkIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:PRK10070 119 PHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 153 TAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSS 197
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQ---RTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-205 |
1.57e-48 |
|
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: 159.05 E-value: 1.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQTFALFPWLT 76
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLsrrelARRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAG----LEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVl 152
Cdd:COG1120 92 VRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 153 taeTLRTDLLDL-----WTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1120 171 ---AHQLEVLELlrrlaRERGR----TVVMVLHDLNLAARYADRLVLLKD--GRIVAQ 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
9-204 |
3.80e-48 |
|
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: 161.04 E-value: 3.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 9 DANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQ 79
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiflpphrrrIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEAlgVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRT 159
Cdd:COG4148 97 NLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD----LARKA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956089794 160 DLLD----LWTQGRMPIksvLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:COG4148 171 EILPylerLRDELDIPI---LYVSHSLDEVARLADHVVLLEQ--GRVVA 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-196 |
1.96e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 159.48 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG---PAEGVAMVFQTFALFPWLTVLQNVE 82
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhaRDRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEALgvgarERRERALAAI---------DLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:PRK10851 97 FGLTVL-----PRRERPNAAAikakvtqllEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956089794 154 AETLRTDLLDLWTQgrMPIKSVLiVTHNIEEAVFMCDRILVLS 196
Cdd:PRK10851 172 RKELRRWLRQLHEE--LKFTSVF-VTHDQEEAMEVADRVVVMS 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-205 |
9.18e-47 |
|
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: 154.13 E-value: 9.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG---------PAEGVAMVFQTFALF 72
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedararlRARHVGFVFQSFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVEAGLEAlgVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:COG4181 103 PTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 153 TAETLrTDLL-DLWTQGRMpikSVLIVTHNIEEAVfMCDRILVLSSnpGRVIAE 205
Cdd:COG4181 181 TGEQI-IDLLfELNRERGT---TLVLVTHDPALAA-RCDRVLRLRA--GRLVED 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-194 |
2.51e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 155.66 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQ-TFA-LFPWLT 76
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrplrrrMQMVFQdPYAsLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVG-ARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV-LT 153
Cdd:COG4608 114 VGDIIAEPLRIHGLAsKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsIQ 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956089794 154 AETLRTdLLDLwtQGRMPIkSVLIVTHNIeeAV--FMCDRILV 194
Cdd:COG4608 194 AQVLNL-LEDL--QDELGL-TYLFISHDL--SVvrHISDRVAV 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-196 |
5.27e-46 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 151.09 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTV 77
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARerRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:COG4133 93 RENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956089794 158 RTDLLDLWTQGRMpiksVLIVTHNIEEAVFmcDRILVLS 196
Cdd:COG4133 171 AELIAAHLARGGA----VLLTTHQPLELAA--ARVLDLG 203
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-197 |
5.95e-46 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 152.45 E-value: 5.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFPWLTV 77
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklrrrIGMIFQHYNLIERLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEA--------LGVGARERRERALAAIDLIGLDGFenAYPR--ELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:TIGR02315 97 LENVLHGRLGykptwrslLGRFSEEDKERALSALERVGLADK--AYQRadQLSGGQQQRVAIARALAQQPDLILADEPIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 148 ALDVLTAETLRTDLLDLwtqGRMPIKSVLIVTHNIEEAVFMCDRILVLSS 197
Cdd:TIGR02315 175 SLDPKTSKQVMDYLKRI---NKEDGITVIINLHQVDLAKKYADRIVGLKA 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-185 |
6.20e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 152.17 E-value: 6.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGV-------AMVFQTFALFPW 74
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNVEAG-LEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV-L 152
Cdd:PRK09493 92 LTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPeL 171
|
170 180 190
....*....|....*....|....*....|...
gi 1956089794 153 TAETLRTdLLDLWTQGrMpikSVLIVTHNIEEA 185
Cdd:PRK09493 172 RHEVLKV-MQDLAEEG-M---TMVIVTHEIGFA 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-216 |
6.35e-46 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 152.52 E-value: 6.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNV 81
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEAlgvgarERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDL 161
Cdd:PRK11247 103 GLGLKG------QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 162 LDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKVPFKHPRNR 216
Cdd:PRK11247 177 ESLWQQHGF---TVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDLPRPRRR 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-195 |
1.74e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 147.27 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAEG----VAMVFQTFALFPwLTVLQN 80
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwrrqVAYVPQEPALWG-GTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEAlgVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:COG4619 94 LPFPFQL--RERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956089794 160 DLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 195
Cdd:COG4619 172 LLREYLAEEGR---AVLWVSHDPEQIERVADRVLTL 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-203 |
6.21e-44 |
|
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: 146.56 E-value: 6.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIE-----PTGGEVTYLGKPLTGPAEG-------VAMVFQTF 69
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlelrrrVGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPwLTVLQNVEAGLEALGV-GARERRERALAAIDLIGLDGFEN--AYPRELSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:cd03260 91 NPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 147 SALD-VLTA--ETLRTDLLDLWTqgrmpiksVLIVTHNIEEAVFMCDRILVLssNPGRVI 203
Cdd:cd03260 170 SALDpISTAkiEELIAELKKEYT--------IVIVTHNMQQAARVADRTAFL--LNGRLV 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-216 |
8.31e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 150.18 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVtYLGKPLTG---PAE-GVAMVFQTFALFPWLTV 77
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNdvpPAErGVGMVFQSYALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:PRK11000 93 AENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 158 RTDLLDLWTQgrmpIKSVLI-VTHNIEEAVFMCDRILVLssNPGRvIAEIKVP---FKHPRNR 216
Cdd:PRK11000 173 RIEISRLHKR----LGRTMIyVTHDQVEAMTLADKIVVL--DAGR-VAQVGKPlelYHYPANR 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-204 |
1.73e-43 |
|
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: 145.34 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPL-TGPAE---GVAMVFQTFALFPWLT 76
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAarqSLGYCPQFDALFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVE--AGLEalGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTa 154
Cdd:cd03263 92 VREHLRfyARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 155 etlRTDLLDLwTQGRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:cd03263 169 ---RRAIWDL-ILEVRKGRSIILTTHSMDEAEALCDRIAIMSD--GKLRC 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-202 |
2.44e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 146.14 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVL 78
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElePADrDIAMVFQNYALYPHMSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:PRK11650 95 ENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 159 TDLLDLwtQGRMPIKSvLIVTHNIEEAVFMCDRILVLssNPGRV 202
Cdd:PRK11650 175 LEIQRL--HRRLKTTS-LYVTHDQVEAMTLADRVVVM--NGGVA 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-208 |
6.11e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 147.86 E-value: 6.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP--LTGPAE----GVAMVFQTFALFPWLTVLQ 79
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvrFRSPRDaqaaGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGA---RERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:COG1129 99 NIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 157 LRTDLLDLWTQGrmpiKSVLIVTHNIEEaVF-MCDRILVLSSnpGRVIAEIKV 208
Cdd:COG1129 179 LFRIIRRLKAQG----VAIIYISHRLDE-VFeIADRVTVLRD--GRLVGTGPV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-214 |
6.19e-42 |
|
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: 148.29 E-value: 6.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIePTGGEVTYLGKPLTGPAEG--------VAMVFQT-FA-L 71
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalrplrrrMQVVFQDpFGsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVEAGLEALGVG--ARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:COG4172 376 SPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 149 LDVLT-AETLrtDLL-DLwtQGRMPIkSVLIVTHNIeeAV--FMCDRILVLSSnpGRVI-----AEIkvpFKHPR 214
Cdd:COG4172 456 LDVSVqAQIL--DLLrDL--QREHGL-AYLFISHDL--AVvrALAHRVMVMKD--GKVVeqgptEQV---FDAPQ 518
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-217 |
1.08e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 144.17 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFP 73
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkarrqIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvlt 153
Cdd:PRK11153 96 SRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD--- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 154 AETLRTdLLDLWTQ--GRMPIKSVLIvTHNIEEAVFMCDRILVLSSnpGRVIAEIKVP--FKHPRNRL 217
Cdd:PRK11153 173 PATTRS-ILELLKDinRELGLTIVLI-THEMDVVKRICDRVAVIDA--GRLVEQGTVSevFSHPKHPL 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-195 |
2.71e-41 |
|
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: 137.90 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-----VAMVFQTFALFPwLTVLQN 80
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslrknIAYVPQDPFLFS-GTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VeaglealgvgarerreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTD 160
Cdd:cd03228 96 I-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1956089794 161 LLDLwtqgrMPIKSVLIVTHNIeEAVFMCDRILVL 195
Cdd:cd03228 139 LRAL-----AKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-205 |
3.26e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 141.78 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG---------PAE-GvamvfqtfaL 71
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigylPEErG---------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLqnveaglEAL-------GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:COG4152 83 YPKMKVG-------EQLvylarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 145 PFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKG----TTVIFSSHQMELVEELCDRIVIINK--GRKVLS 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
12-205 |
3.69e-41 |
|
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: 139.17 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 12 LSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVLQNVEAGLEAL 88
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAapPADrPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 89 GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWTQG 168
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD----PALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956089794 169 RMPIK-SVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03298 175 HAETKmTVLMVTHQPEDAKRLAQRVVFLDN--GRIAAQ 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-195 |
4.50e-41 |
|
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: 136.99 E-value: 4.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQtfalfpwlt 76
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPleelrRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 vlqnveaglealgvgarerreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956089794 157 LRTDLLDLWTQGRMpiksVLIVTHNIEEAVFMCDRILVL 195
Cdd:cd00267 119 LLELLRELAEEGRT----VIIVTHDPELAELAADRVIVL 153
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
2-205 |
6.30e-41 |
|
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: 140.99 E-value: 6.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGV----AMVFQTFALFPWLTV 77
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVrrsiGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 158 RTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLssNPGRVIAE 205
Cdd:TIGR01188 164 WDYIRALKEEG----VTILLTTHYMEEADKLCDRIAII--DHGRIIAE 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-217 |
7.49e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 142.67 E-value: 7.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA---EGVAMVFQTFALFPWLTVLQNVE 82
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyqRPINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLL 162
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 163 DLWTqgRMPIKSVLiVTHNIEEAVFMCDRILVLSSNPGRVIAEIKVPFKHPRNRL 217
Cdd:PRK11607 194 DILE--RVGVTCVM-VTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-195 |
1.02e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 138.00 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP---TGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQN 80
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlPAEqrRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEAlGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTD 160
Cdd:COG4136 97 LAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA----ALRAQ 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956089794 161 LLDL-WTQGRMPIKSVLIVTHNIEEAVFMcDRILVL 195
Cdd:COG4136 172 FREFvFEQIRQRGIPALLVTHDEEDAPAA-GRVLDL 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
11-202 |
1.16e-40 |
|
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: 137.69 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA---EGVAMVFQTFALFPWLTVLQNVEAGLE- 86
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLApyqRPVSMLFQENNLFAHLTVRQNIGLGLHp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 ALGVGArERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWT 166
Cdd:TIGR01277 98 GLKLNA-EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956089794 167 QGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRV 202
Cdd:TIGR01277 177 ERQR---TLLMVTHHLSDARAIASQIAVVSQ--GKI 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-205 |
1.30e-40 |
|
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: 136.41 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTgpaegvamvfqtfalfpwltvlqnveagl 85
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA----------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 ealgvgARERRERALA------AIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRT 159
Cdd:cd03214 65 ------SLSPKELARKiayvpqALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI----AHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 160 DLLDLWTQ-GRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03214 135 ELLELLRRlARERGKTVVMVLHDLNLAARYADRVILLKD--GRIVAQ 179
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-195 |
1.59e-40 |
|
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: 137.54 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAEGVA-------MVFQTFALFPWLTVL 78
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPylrrkigVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAetlr 158
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT---- 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956089794 159 TDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-204 |
3.57e-40 |
|
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: 136.64 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEgvamvfQTFA-------LFPW 74
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR------NRIGylpeergLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 154
Cdd:cd03269 85 MKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 155 ETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLssNPGRVIA 204
Cdd:cd03269 165 ELLKDVIRELARAG----KTVILSTHQMELVEELCDRVLLL--NKGRAVL 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-205 |
4.36e-40 |
|
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: 136.41 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG------PAEGVAMVFQTFALFPWL 75
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppherARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGLEALGVGARERR-ERALAAIDLigLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 154
Cdd:cd03224 91 TVEENLLLGAYARRRAKRKARlERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 155 ETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03224 169 EEIFEAIRELRDEGV----TILLVEQNARFALEIADRAYVLER--GRVVLE 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-205 |
4.57e-40 |
|
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: 144.98 E-value: 4.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFPwLTVLQ 79
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASlrrQIGVVLQDVFLFS-GTIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGvgarerRERALAAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:COG2274 568 NITLGDPDAT------DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 149 LDVLTAETLrTDLLDLWTQGRmpikSVLIVTHNiEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG2274 642 LDAETEAII-LENLRRLLKGR----TVIIIAHR-LSTIRLADRIIVLDK--GRIVED 690
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-205 |
5.36e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 136.70 E-value: 5.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--------------PAEgvAMVFQTfal 71
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkrarlgigylPQE--ASIFRK--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 fpwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:COG1137 93 ---LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 152 LTAETLRTDLLDLWTQGrmpIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1137 170 IAVADIQKIIRHLKERG---I-GVLITDHNVRETLGICDRAYIISE--GKVLAE 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-206 |
5.49e-40 |
|
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: 135.81 E-value: 5.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMV---FQTFALFPWLTVL 78
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIgalIEAPGFYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNveagLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:cd03268 91 EN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 159 TDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLssNPGRVIAEI 206
Cdd:cd03268 167 ELILSLRDQG----ITVLISSHLLSEIQKVADRIGII--NKGKLIEEG 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-208 |
7.85e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 142.47 E-value: 7.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE----GVAMVFQTFALFPWL 75
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirSPRDaialGIGMVHQHFMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGLEALGvGARERRERALAAI-DLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSaldV 151
Cdd:COG3845 96 TVAENIVLGLEPTK-GGRLDRKAARARIrELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA---V 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 152 LT---AETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKV 208
Cdd:COG3845 172 LTpqeADELFEILRRLAAEG----KSIIFITHKLREVMAIADRVTVLRR--GKVVGTVDT 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-205 |
1.10e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 136.40 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE---GVAMVFQTFAL-FPWlTVLQ 79
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwsPWElarRRAVLPQHSSLaFPF-TVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALV-----VDPT--ILLMDEPFSALDVL 152
Cdd:COG4559 95 VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepVDGGprWLFLDEPTSALDLA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 153 ----TAETLRTdlldlWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG4559 175 hqhaVLRLARQ-----LARRGG---GVVAVLHDLNLAAQYADRILLLHQ--GRLVAQ 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-205 |
1.04e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 134.13 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE---GVAMVFQTFAL-FPWlTVLQ 79
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAElarRRAVLPQHSSLsFPF-TVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALV------VDPTILLMDEPFSALDVLT 153
Cdd:PRK13548 96 VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 154 AETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13548 176 QHHVLRLARQLAHERGL---AVIVVLHDLNLAARYADRIVLLHQ--GRLVAD 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-195 |
1.99e-38 |
|
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: 132.48 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLT 76
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNeraklrnkkLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:TIGR02211 100 ALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956089794 157 LRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMcDRILVL 195
Cdd:TIGR02211 180 IFDLMLELNRELNT---SFLVVTHDLELAKKL-DRVLEM 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
2-195 |
2.20e-38 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 131.58 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK---PLTGPA------EGVAMVFQTFALF 72
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKaskfrrEKLGYLFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:TIGR03608 89 ENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956089794 153 TAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVfMCDRILVL 195
Cdd:TIGR03608 169 NRDEVLDLLLELNDEG----KTIIIVTHDPEVAK-QADRVIEL 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-185 |
5.62e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 131.67 E-value: 5.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPL-----TGPAEG------VAMVFQTFALFPW 74
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktPSDKAIrelrrnVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQN-VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV-L 152
Cdd:PRK11124 97 LTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeI 176
|
170 180 190
....*....|....*....|....*....|...
gi 1956089794 153 TAETLRTdLLDLWTQGrmpIKSVlIVTHNIEEA 185
Cdd:PRK11124 177 TAQIVSI-IRELAETG---ITQV-IVTHEVEVA 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-205 |
6.13e-38 |
|
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: 130.95 E-value: 6.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGV----AMVFQTFALFPWLTV 77
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVrrriGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:cd03265 91 WENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 158 RTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03265 171 WEYIEKLKEEFGM---TILLTTHYMEEAEQLCDRVAIIDH--GRIIAE 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-205 |
1.02e-37 |
|
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: 130.74 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG------PAEGVAMVFQTFALFPWLTVLQ 79
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhkrARLGIGYLPQEASIFRKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 160 DLLDLWTQGrmpIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03218 175 IIKILKDRG---I-GVLITDHNVRETLSITDRAYIIYE--GKVLAE 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-205 |
1.35e-37 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 130.18 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLG-KPLTGPAE---GVAMVFQTFALFPWLTV 77
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEarrRLGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVE--AGLEalGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAE 155
Cdd:cd03266 96 RENLEyfAGLY--GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 156 TLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03266 174 ALREFIRQLRALG----KCILFSTHIMQEVERLCDRVVVLHR--GRVVYE 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-205 |
1.47e-37 |
|
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: 128.32 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE----GVAMVFQtfalfpwl 75
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfaSPRDarraGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 tvlqnveaglealgvgarerreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAE 155
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 156 TLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03216 120 RLFKVIRRLRAQG----VAVIFISHRLDEVFEIADRVTVLRD--GRVVGT 163
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-205 |
2.56e-37 |
|
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: 132.93 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 9 DANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQ 79
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppekrrIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEAlgVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:TIGR02142 95 NLRYGMKR--ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 160 DLLDLWTQGRMPIksvLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:TIGR02142 173 YLERLHAEFGIPI---LYVSHSLQEVLRLADRVVVLED--GRVAAA 213
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-214 |
2.60e-37 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 130.33 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT---------GPA---------EGVA 63
Cdd:TIGR03005 11 GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYhmpgrngplVPAdekhlrqmrNKIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 64 MVFQTFALFPWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLM 142
Cdd:TIGR03005 91 MVFQSFNLFPHKTVLDNVtEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLF 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 143 DEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLssNPGRVIAEIKVP--FKHPR 214
Cdd:TIGR03005 171 DEVTSALDPELVGEVLNVIRRLASEHDL---TMLLVTHEMGFAREFADRVCFF--DKGRIVEQGKPDeiFRQPK 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1-205 |
4.14e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 130.24 E-value: 4.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA------EGVAMVFQ------- 67
Cdd:TIGR04520 12 ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweirKKVGMVFQnpdnqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 68 -TfalfpwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:TIGR04520 92 gA-------TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 147 SALD------VL-TAETLRTDlldlwtQGrmpiKSVLIVTHNIEEAVfMCDRILVLssNPGRVIAE 205
Cdd:TIGR04520 165 SMLDpkgrkeVLeTIRKLNKE------EG----ITVISITHDMEEAV-LADRVIVM--NKGKIVAE 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-196 |
5.15e-37 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 128.52 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG------PA--EGVAMVFQTFALFPWLTVL 78
Cdd:TIGR02673 18 LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqlPLlrRRIGVVFQDFRLLPDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLR 158
Cdd:TIGR02673 98 ENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD----PDLS 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956089794 159 TDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVLS 196
Cdd:TIGR02673 174 ERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILD 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-213 |
6.70e-37 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.98 E-value: 6.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPL---TGPAEG--------VAMVFQTFA 70
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKairllrqkVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 71 LFPWLTVLQN-VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:COG4161 93 LWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 150 D-VLTAETLRTdLLDLwtqGRMPIKSVlIVTHNIEEAVFMCDRILVLSSnpGRVI----AEIkvpFKHP 213
Cdd:COG4161 173 DpEITAQVVEI-IREL---SQTGITQV-IVTHEVEFARKVASQVVYMEK--GRIIeqgdASH---FTQP 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-205 |
2.40e-36 |
|
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: 126.88 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK--PLTGPAEGvamvFQtfalfPWLTVLQ 79
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGLGGG----FN-----PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 160 DLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03220 184 RLRELLKQGK----TVILVSHDPSSIKRLCDRALVLEK--GKIRFD 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
11-194 |
2.68e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.01 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP--LTGPAE-GVAMVFQTFALFPWLTVLQNVEAGLE- 86
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtTTPPSRrPVSMLFQENNLFSHLTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 ALGVGARERRERALAAiDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWT 166
Cdd:PRK10771 99 GLKLNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD----PALRQEMLTLVS 173
|
170 180
....*....|....*....|....*....
gi 1956089794 167 Q-GRMPIKSVLIVTHNIEEAVFMCDRILV 194
Cdd:PRK10771 174 QvCQERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-205 |
3.71e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.12 E-value: 3.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK---PLtgpaeGVAMVFQtfalfPWLTVL 78
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLL-----ELGAGFH-----PELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:COG1134 107 ENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 159 TDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1134 187 ARIRELRESGR----TVIFVSHSMGAVRRLCDRAIWLEK--GRLVMD 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-217 |
4.00e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.88 E-value: 4.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQTF--ALFPWL 75
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafrrdIQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGLEAL-GVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VL 152
Cdd:PRK10419 107 TVREIIREPLRHLlSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlVL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 153 TAETLRTdLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLssNPGRVIAEIKV----PFKHPRNRL 217
Cdd:PRK10419 187 QAGVIRL-LKKLQQQFGT---ACLFITHDLRLVERFCQRVMVM--DNGQIVETQPVgdklTFSSPAGRV 249
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-205 |
1.12e-35 |
|
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: 125.00 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGeIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTVLQNV 81
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrrIGYLPQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDL 161
Cdd:cd03264 94 DYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 162 LDLWTQgrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03264 174 SELGED-----RIVILSTHIVEDVESLCNQVAVLNK--GKLVFE 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-198 |
1.29e-35 |
|
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: 124.68 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA--EGVAMVFQT--FALFPwLTVLQN 80
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrKSIGYVMQDvdYQLFT-DSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGvgarERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTD 160
Cdd:cd03226 93 LLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956089794 161 LLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSN 198
Cdd:cd03226 169 IRELAAQG----KAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-205 |
2.50e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.06 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFPwLTVLQN 80
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESlrrQIGVVPQDTFLFS-GTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VeagleALGvgaRER--RERALAAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:COG1132 434 I-----RYG---RPDatDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 148 ALDVLTAETLRTDLLDLwTQGRMpiksVLIVTHNIeEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG1132 506 ALDTETEALIQEALERL-MKGRT----TIVIAHRL-STIRNADRILVLDD--GRIVEQ 555
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-204 |
2.57e-35 |
|
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: 130.66 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-----VAMVFQTFALFPwLTVLQN 80
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlrrrIAVVPQRPHLFD-TTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 V-----EAGLEALgvgarerreraLAAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:COG4987 429 LrlarpDATDEEL-----------WAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 145 PFSALDVLTAETLRTDLLDlWTQGRmpikSVLIVTHNiEEAVFMCDRILVLSSnpGRVIA 204
Cdd:COG4987 498 PTEGLDAATEQALLADLLE-ALAGR----TVLLITHR-LAGLERMDRILVLED--GRIVE 549
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-216 |
5.45e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.48 E-value: 5.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTY------LGKPLTGPA-------EGVAMVFQTFALF 72
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKglirqlrQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:PRK11264 98 PHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 152 -LTAETLRTdLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLssNPGRVI--AEIKVPF---KHPRNR 216
Cdd:PRK11264 178 eLVGEVLNT-IRQLAQEKR----TMVIVTHEMSFARDVADRAIFM--DQGRIVeqGPAKALFadpQQPRTR 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-205 |
1.35e-34 |
|
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: 122.78 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAE-----GVAMVFQTFALFPWL 75
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlPPHriarlGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGleALGVGARERRERALAAIdligLDGFENAYPR------ELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:COG0410 94 TVEENLLLG--AYARRDRAEVRADLERV----YELFPRLKERrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 150 DVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG0410 168 APLIVEEIFEIIRRLNREG----VTILLVEQNARFALEIADRAYVLER--GRIVLE 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-195 |
2.47e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.77 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK--PLTGPAEG----------------VA 63
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtiNLVRDKDGqlkvadknqlrllrtrLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 64 MVFQTFALFPWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENA-YPRELSGGMRQRVGFARALVVDPTILL 141
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 142 MDEPFSALDV-LTAETLRTdLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK10619 176 FDEPTSALDPeLVGEVLRI-MQQLAEEG----KTMVVVTHEMGFARHVSSHVIFL 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-204 |
9.74e-34 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 120.00 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFpWLTV 77
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADlrrNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVeagleALGVGARErRERALAAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:cd03245 95 RDNI-----TLGAPLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 147 SALDvLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIeEAVFMCDRILVLSSnpGRVIA 204
Cdd:cd03245 169 SAMD-MNSEERLKERLRQLLGD----KTLIIITHRP-SLLDLVDRIIVMDS--GRIVA 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-195 |
1.35e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 120.27 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGE--LLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG---------PAEGVAMVFQTF 69
Cdd:PRK10584 18 QGEheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearaklRAKHVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPWLTVLQNVEagLEALGVGARER--RERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:PRK10584 98 MLIPTLNALENVE--LPALLRGESSRqsRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 148 ALDVLTAETLrTDLldLWTQGRMPIKSVLIVTHNIEEAVfMCDRILVL 195
Cdd:PRK10584 176 NLDRQTGDKI-ADL--LFSLNREHGTTLILVTHDLQLAA-RCDRRLRL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-205 |
1.78e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 121.28 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQT-FALFPWLTVLQN 80
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQVGMVFQNpDNQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD------VLta 154
Cdd:PRK13635 103 VAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrreVL-- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 155 ETLRtdllDLWTQGRMpikSVLIVTHNIEEAVFmCDRILVLssNPGRVIAE 205
Cdd:PRK13635 181 ETVR----QLKEQKGI---TVLSITHDLDEAAQ-ADRVIVM--NKGEILEE 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-205 |
4.52e-33 |
|
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: 124.49 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-----PAEGVAMVFQTFALFPWlTVLQN 80
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldpasWRRQIAWVPQNPYLFAG-TIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 veagleaLGVGARERRERAL-AAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:COG4988 431 -------LRLGRPDASDEELeAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 149 LDVLTAETLRTDLLDLWtQGRMpiksVLIVTHNIEEAVFMcDRILVLssNPGRVIAE 205
Cdd:COG4988 504 LDAETEAEILQALRRLA-KGRT----VILITHRLALLAQA-DRILVL--DDGRIVEQ 552
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-205 |
9.45e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.91 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA----EGVAMVFQTFALFPWLTV 77
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRArharQRVGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 158 RTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13537 178 WERLRSLLARG----KTILLTTHFMEEAERLCDRLCVIEE--GRKIAE 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-185 |
1.32e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.61 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLT 76
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|
gi 1956089794 157 LRTDLLDL-WTQGrmpiKSVLIVTHNIEEA 185
Cdd:PRK11629 184 IFQLLGELnRLQG----TAFLVVTHDLQLA 209
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-203 |
2.43e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 117.63 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQ--TFALFPWLTVL 78
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGdykyrCKHIRMIFQdpNTSLNPRLNIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLE-ALGVGARERRERALAAIDLIGLDGfENA--YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltae 155
Cdd:COG4167 108 QILEEPLRlNTDLTAEEREERIFATLRLVGLLP-EHAnfYPHMLSSGQKQRVALARALILQPKIIIADEALAALDM---- 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 156 TLRTD----LLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:COG4167 183 SVRSQiinlMLEL--QEKLGI-SYIYVSQHLGIVKHISDKVLVMHQ--GEVV 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-203 |
3.09e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.23 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-------EGVAMVFQ--TFALFPwLTV 77
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklsdirKKVGLVFQypEYQLFE-ETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLD--GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAE 155
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 156 TLRTDLLDLWTQGRMPIksvLIVTHNIEEAVFMCDRILVLssNPGRVI 203
Cdd:PRK13637 182 EILNKIKELHKEYNMTI---ILVSHSMEDVAKLADRIIVM--NKGKCE 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-205 |
6.27e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.39 E-value: 6.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAE----GVAMVFQTFALFPWLTV 77
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARlaraRIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:PRK13536 132 RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 158 RTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13536 212 WERLRSLLARG----KTILLTTHFMEEAERLCDRLCVLEA--GRKIAE 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
6-185 |
6.71e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.64 E-value: 6.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTylgkplTGPAEGVAMVFQTFAL---FPwLTVLQNVE 82
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRSEVpdsLP-LTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEA----LGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:NF040873 80 MGRWArrglWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180
....*....|....*....|....*...
gi 1956089794 159 tDLLDLWT-QGRmpikSVLIVTHNIEEA 185
Cdd:NF040873 160 -ALLAEEHaRGA----TVVVVTHDLELV 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-195 |
1.42e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.50 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 4 LLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAE--------GVAMVFQT--FALFP 73
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewravrsDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVEAGLEAL--GVGARERRERALAAIDLIGL-DGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PRK15079 114 RMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK15079 194 VSIQAQVVNLLQQL--QREMGL-SLIFIAHDLAVVKHISDRVLVM 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
12-205 |
2.05e-31 |
|
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: 114.18 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 12 LSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFAlFPW---LTVLQNVEAGLEAL 88
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHE-FAWdfpISVAHTVMSGRTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 89 gVGARERRERA-----LAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLD 163
Cdd:TIGR03771 80 -IGWLRRPCVAdfaavRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TELFI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956089794 164 LWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSsnpGRVIAE 205
Cdd:TIGR03771 158 ELAGAGT---AILMTTHDLAQAMATCDRVVLLN---GRVIAD 193
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
7.08e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.59 E-value: 7.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIE--P---TGGEVTYLGKPLTGPAEG-------VAMVFQTF 69
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIYDPDVDvvelrrrVGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPwLTVLQNVEAGLEALGVGAR----ERRERAL--AAI------DLigldgfeNAYPRELSGGMRQRVGFARALVVDP 137
Cdd:COG1117 102 NPFP-KSIYDNVAYGLRLHGIKSKseldEIVEESLrkAALwdevkdRL-------KKSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 138 TILLMDEPFSALD-VLTA------ETLRTDLldlwtqgrmpikSVLIVTHNIEEAVFMCDRILVLssNPGRVI-----AE 205
Cdd:COG1117 174 EVLLMDEPTSALDpISTAkieeliLELKKDY------------TIVIVTHNMQQAARVSDYTAFF--YLGELVefgptEQ 239
|
250
....*....|..
gi 1956089794 206 IkvpFKHPRNRL 217
Cdd:COG1117 240 I---FTNPKDKR 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-204 |
8.29e-31 |
|
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: 113.26 E-value: 8.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPT-GGEVTYLGKPLTG--PAE-----GVAMVFQTFALFP 73
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGedVWElrkriGLVSPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVEAGLEA-LGVGAR---ERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:COG1119 94 DETVLDVVLSGFFDsIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 150 DVLTAETLRtDLLDLWTQGRMPikSVLIVTHNIEEAVFMCDRILVLSsnPGRVIA 204
Cdd:COG1119 174 DLGARELLL-ALLDKLAAEGAP--TLVLVTHHVEEIPPGITHVLLLK--DGRVVA 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-207 |
3.69e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.75 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK---PLTGPA------EGVAMVFQTFAL 71
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADAlaqlrrEHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:PRK10535 98 LSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 152 LTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVfMCDRIL------VLSSNPGRVIAEIK 207
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGH----TVIIVTHDPQVAA-QAERVIeirdgeIVRNPPAQEKVNVA 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-195 |
5.42e-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: 115.94 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKS----TLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQ 67
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERelrrirgnrIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 68 ---TfALFPWLTVLQNVEAGLEA-LGVGARERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTIL 140
Cdd:COG4172 100 epmT-SLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 141 LMDEPFSALDVLT-AETLrtDLL-DLWTQGRMpikSVLIVTHNIeeAVF--MCDRILVL 195
Cdd:COG4172 179 IADEPTTALDVTVqAQIL--DLLkDLQRELGM---ALLLITHDL--GVVrrFADRVAVM 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-204 |
7.88e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 113.05 E-value: 7.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 9 DANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAM---------VFQTFALFPWLTVLQ 79
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekrrigyVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLealgvgARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:PRK11144 96 NLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 160 DLLDLWTQGRMPIksvLIVTHNIEEAVFMCDRILVLssNPGRVIA 204
Cdd:PRK11144 170 YLERLAREINIPI---LYVSHSLDEILRLADRVVVL--EQGKVKA 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-203 |
1.30e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTgPAEG----------VAMVFQtfalFPWL- 75
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT-PETGnknlkklrkkVSLVFQ----FPEAq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 ----TVLQNVEAGLEALGVGARERRERALAAIDLIGL-DGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PRK13641 98 lfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 151 VLTaetlRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:PRK13641 178 PEG----RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEH--GKLI 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-180 |
1.48e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.39 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYlgkpltGPAEGVAMVFQTFALFPWLTVLQNV 81
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------PKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEALGvGARERRERALAAID-------------------------------LIGLdGFENAYP----RELSGGMRQR 126
Cdd:COG0488 83 LDGDAELR-ALEAELEELEAKLAepdedlerlaelqeefealggweaearaeeiLSGL-GFPEEDLdrpvSELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 127 VGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGrmpikSVLIVTH 180
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PG-----TVLVVSH 207
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
8-208 |
2.60e-29 |
|
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: 109.00 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 8 DDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP----TGGEVTYLGKPLTGPA---EGVAMVFQT--FALFPWLTVL 78
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSirgRHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAE 155
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 156 TLrTDLLDLWTQGRMPikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKV 208
Cdd:TIGR02770 163 RV-LKLLRELRQLFGT--GILLITHDLGVVARIADEVAVMDD--GRIVERGTV 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-202 |
2.93e-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: 107.52 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMvfqtfalfpwltvlqnveagl 85
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI--------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 eALGVG--ARERRERALaaidLIGLDGFEN-AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLL 162
Cdd:cd03215 74 -RAGIAyvPEDRKREGL----VLDLSVAENiALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956089794 163 DLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRV 202
Cdd:cd03215 149 ELADAG----KAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-205 |
2.96e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.78 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-------VAMVFQT-----FAlfP 73
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrktVGIVFQNpddqlFA--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 wlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 154 AETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13639 173 ASQIMKLLYDLNKEG----ITIIISTHDVDLVPVYADKVYVMSD--GKIIKE 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-203 |
5.52e-29 |
|
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: 107.25 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTG--GEVTYLGKPLT--GPAEGVAMVFQTFALFPWLT 76
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDkrSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VlqnveagLEALGVGARERReralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:cd03213 99 V-------RETLMFAAKLRG----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 157 LRTDLLDLWTQGRmpikSVLIVTHNIEEAVF-MCDRILVLSsnPGRVI 203
Cdd:cd03213 150 VMSLLRRLADTGR----TIICSIHQPSSEIFeLFDKLLLLS--QGRVI 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-204 |
1.89e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.77 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP-----LTGPAEGVAMVFQT-FALFPWLT 76
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenLKEIRKKIGIIFQNpDNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:PRK13632 101 VEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 157 LRTDLLDLWTQGRmpiKSVLIVTHNIEEAVfMCDRILVLSSnpGRVIA 204
Cdd:PRK13632 181 IKKIMVDLRKTRK---KTLISITHDMDEAI-LADKVIVFSE--GKLIA 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-195 |
2.53e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.41 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLI---EPTGGEVTYLGKplTGPAEG------------VAMVFQTFAL 71
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGR--TVQREGrlardirksranTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVEAGleALGVG----------ARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILL 141
Cdd:PRK09984 98 VNRLSVLENVLIG--ALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 142 MDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGI---TVVVTLHQVDYALRYCERIVAL 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-181 |
2.99e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 105.73 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP--LTGPAEGVAMVFQTFALFPWLTVLQ 79
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDidDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGvgarERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAE 155
Cdd:PRK13539 93 NLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaavaLFAE 168
|
170 180
....*....|....*....|....*.
gi 1956089794 156 TLRTDLldlwTQGRMpiksVLIVTHN 181
Cdd:PRK13539 169 LIRAHL----AQGGI----VIAATHI 186
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
3.71e-28 |
|
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: 110.84 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAE-----GVAMVFQTFALFPWlT 76
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdswrdQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVeaGLEALGVGARERREralaAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:TIGR02857 412 IAENI--RLARPDASDAEIRE----ALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 146 FSALDVLTAETLRTDLLDLwTQGRmpikSVLIVTHNIEEAVfMCDRILVL 195
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRAL-AQGR----TVLLVTHRLALAA-LADRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-206 |
4.69e-28 |
|
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: 110.28 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEV-----------TYLGKPLTGPAEG-VAMVFQTFALFPW 74
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPDGRGRAKRyIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNVEaglEALGVGARERRERALAAIDLIGLdGFE--------NAYPRELSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:TIGR03269 380 RTVLDNLT---EAIGLELPDELARMKAVITLKMV-GFDeekaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 147 SALDVLTAETLRTDLLdlwtQGRMPI-KSVLIVTHNIEEAVFMCDRI-------LVLSSNPGRVIAEI 206
Cdd:TIGR03269 456 GTMDPITKVDVTHSIL----KAREEMeQTFIIVSHDMDFVLDVCDRAalmrdgkIVKIGDPEEIVEEL 519
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-195 |
1.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTgpAEGV-------AMVFQT-FALFPWLTVL 78
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENVwdirhkiGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956089794 159 TDLLDLWTQGRMpikSVLIVTHNIEEaVFMCDRILVL 195
Cdd:PRK13650 181 KTIKGIRDDYQM---TVISITHDLDE-VALSDRVLVM 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-191 |
1.19e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.24 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRII--AGLIEP---TGGEVTYLGKPLTGPA-------EGVAMVFQTFALFPw 74
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRtdtvdlrKEIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNVEAGLEALGVGARERRERALAAiDLIGLDGFENAYPR------ELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956089794 149 LDVLTAETLRTDLLDLWTQGRMpiksvLIVTHNIEEAVFMCDR 191
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTM-----LLVTRSMQQASRISDR 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-151 |
1.65e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.59 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAgLIE-PTGGEVTYLGKPLTGPAEG--------VAMVFQT-FA-LFPWL 75
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDLLKADPEaqkllrqkIQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 76 TVLQNVEAGLEA-LGVGARERRERALAAIDLIGLDG-FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:PRK11308 110 KVGQILEEPLLInTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-195 |
2.54e-27 |
|
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: 102.29 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFPWlTVLQN 80
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNElgdHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VeaglealgvgarerreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTD 160
Cdd:cd03246 96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1956089794 161 LLDLwtqgRMPIKSVLIVTHNIeEAVFMCDRILVL 195
Cdd:cd03246 139 IAAL----KAAGATRIVIAHRP-ETLASADRILVL 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-206 |
3.10e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.80 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE----GVAMV---FQTFALFPWLT 76
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirSPRDairaGIAYVpedRKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVE-AGLEALGVGA--RERRERALAA--IDLIGL---DGFENAypRELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:COG1129 347 IRENITlASLDRLSRGGllDRRRERALAEeyIKRLRIktpSPEQPV--GNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 149 LDVLT-AETLRTdLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEI 206
Cdd:COG1129 425 IDVGAkAEIYRL-IRELAAEG----KAVIVISSELPELLGLSDRILVMRE--GRIVGEL 476
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2-180 |
3.35e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 102.57 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT-------------GPAEGVAmvfqt 68
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyhqdllylGHQPGIK----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 69 falfPWLTVLQNVEAGLEALGVGARERRERALAAidlIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:PRK13538 87 ----TELTALENLRFYQRLHGPGDDEALWEALAQ---VGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190
....*....|....*....|....*....|..
gi 1956089794 149 LDVLTAETLRTDLLDLWTQGRMpiksVLIVTH 180
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQGGM----VILTTH 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-203 |
3.66e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 103.85 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK-----PLTGPAEG-VAMVFQTfalfPWL 75
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAeRRRLLRT----EWG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGL-----------EAL-GVGARE-RRERALAA-------IDLIGLDGFenayPRELSGGMRQRVGFARALVV 135
Cdd:PRK11701 93 FVHQHPRDGLrmqvsaggnigERLmAVGARHyGDIRATAGdwlerveIDAARIDDL----PTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 136 DPTILLMDEPFSALDVltaeTLRTDLLDLWTQ--GRMPIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:PRK11701 169 HPRLVFMDEPTGGLDV----SVQARLLDLLRGlvRELGL-AVVIVTHDLAVARLLAHRLLVMKQ--GRVV 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-205 |
6.85e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 6.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAE-----GVAMVFQ-----TFALfpwlT 76
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvrsKVGLVFQdpddqVFSS----T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956089794 157 LRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13647 177 LMEILDRLHNQG----KTVIVATHDVDLAAEWADQVIVLKE--GRVLAE 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-196 |
8.18e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 102.26 E-value: 8.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFPWLTVL 78
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflrrqIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLR 158
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALS 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956089794 159 TDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVLS 196
Cdd:PRK10908 174 EGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-216 |
1.06e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKST----LLRIIAgliepTGGEVTYLGKPLTG-------PAEG-VAMVFQ- 67
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNlnrrqllPVRHrIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 68 -TFALFPWLTVLQNVEAGLEA--LGVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMD 143
Cdd:PRK15134 371 pNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 144 EPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVI--AEIKVPFKHPRNR 216
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQL---AYLFISHDLHVVRALCHQVIVLRQ--GEVVeqGDCERVFAAPQQE 520
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2-204 |
1.40e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.31 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPL-----TGPAEGVAMVFQTFALFPWLT 76
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAG----LEALGvGARERRERAL-AAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD- 150
Cdd:PRK09536 94 VRQVVEMGrtphRSRFD-TWTETDRAAVeRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDi 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 151 ---VLTAETLRtdllDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:PRK09536 173 nhqVRTLELVR----RLVDDG----KTAVAAIHDLDLAARYCDELVLLAD--GRVRA 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
7-205 |
2.51e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.62 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-------VAMVFQT--FALFPwLTV 77
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklresVGMVFQDpdNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VLTAET 156
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpMGVSEI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956089794 157 LRtdlLDLWTQGRMPIkSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13636 181 MK---LLVEMQKELGL-TIIIATHDIDIVPLYCDNVFVMKE--GRVILQ 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-195 |
5.30e-26 |
|
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: 99.47 E-value: 5.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGkpltgpaeGVAMVFQTfalfPWL---TVLQNVE 82
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVSQE----PWIqngTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEALgvgaRERRERALAA----IDL----------IGLDGFEnaypreLSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:cd03250 88 FGKPFD----EERYEKVIKAcalePDLeilpdgdlteIGEKGIN------LSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 149 LDVLTAETLRTDLLdlwTQGRMPIKSVLIVTHNIeEAVFMCDRILVL 195
Cdd:cd03250 158 VDAHVGRHIFENCI---LGLLLNNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-205 |
5.44e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAEGVAmvfQTFALFPW------ 74
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLA---RRLALLPQhhltpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 -LTVLQNVEAG----LEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:PRK11231 90 gITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 150 DVltaeTLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK11231 170 DI----NHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLAN--GHVMAQ 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-203 |
7.42e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYL---GKPLTGPAEG------------------ 61
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdEKNKKKTKEKekvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 62 --------VAMVFQtFA---LFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGF 129
Cdd:PRK13651 99 kikeirrrVGVVFQ-FAeyqLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 130 ARALVVDPTILLMDEPFSALD-VLTAETLrtDLLD-LWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLssNPGRVI 203
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDpQGVKEIL--EIFDnLNKQG----KTIILVTHDLDNVLEWTKRTIFF--KDGKII 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-214 |
9.83e-26 |
|
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: 103.73 E-value: 9.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGL--IEPTGGEVTY----------------LGKP--------- 54
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGEPcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 55 -----LTGPAEGV--------AMVFQ-TFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELS 120
Cdd:TIGR03269 91 peevdFWNLSDKLrrrirkriAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 121 GGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIE-------EAVFMCDRIL 193
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGI---SMVLTSHWPEviedlsdKAIWLENGEI 247
|
250 260
....*....|....*....|.
gi 1956089794 194 VLSSNPGRVIAEIKVPFKHPR 214
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGVSEVE 268
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-205 |
1.40e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.22 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLtgPA----------EGVAMVFQTFA 70
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--PAmsrsrlytvrKRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 71 LFPWLTVLQNVEAGL-EALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:PRK11831 95 LFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 150 DVLTAETLrTDLLDLWTQGrMPIKSVlIVTHNIEEAVFMCDRILVLSSNpgRVIAE 205
Cdd:PRK11831 175 DPITMGVL-VKLISELNSA-LGVTCV-VVSHDVPEVLSIADHAYIVADK--KIVAH 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-202 |
1.76e-25 |
|
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: 99.08 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPwLTVLQ 79
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylhSKVSLVGQEPVLFA-RSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGARERRERALAAIDLIglDGFENAYPRE-------LSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:cd03248 107 NIAYGLQSCSFECVKEAAQKAHAHSFI--SELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 153 TAETLRTDLLDlWTQGRmpikSVLIVTHNIeEAVFMCDRILVLSSnpGRV 202
Cdd:cd03248 185 SEQQVQQALYD-WPERR----TVLVIAHRL-STVERADQILVLDG--GRI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-205 |
1.97e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLG------KPLTGPAEGVAMVFQT-FALFPWLTVLQ 79
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 160 DLLDLWTQGrmpiKSVLIVTHNIEEaVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13644 178 RIKKLHEKG----KTIVYITHNLEE-LHDADRIIVMDR--GKIVLE 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-205 |
2.31e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.78 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVtYLGKPLTGPAEGV-------AMVFQTfalfP-- 73
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLDTSDEENLwdirnkaGMVFQN----Pdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 ---WLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PRK13633 97 qivATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDLLDLwtQGRMPIKSVLIvTHNIEEAVfMCDRILVLSSnpGRVIAE 205
Cdd:PRK13633 177 PSGRREVVNTIKEL--NKKYGITIILI-THYMEEAV-EADRIIVMDS--GKVVME 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-204 |
2.65e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 102.30 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP------AEGVAMVFQTFALFPWLTVLQN 80
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAsttaalAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGL--EALGVGARER-RERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:PRK11288 100 LYLGQlpHKGGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 158 RTDLLDLWTQGRMpiksVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:PRK11288 180 FRVIRELRAEGRV----ILYVSHRMEEIFALCDAITVFKD--GRYVA 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-195 |
2.87e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.71 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTyLG-------------KPLTgpaEGVAMVFQtF 69
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGervitagkknkklKPLR---KKVGIVFQ-F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 A---LFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:PRK13634 94 PehqLFE-ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 146 FSALDvltaETLRTDLLD----LWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK13634 173 TAGLD----PKGRKEMMEmfykLHKEKGL---TTVLVTHSMEDAARYADQIVVM 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-151 |
3.18e-25 |
|
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: 97.43 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG----PAEGVAMVFQTFALFPWLTV 77
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrdePHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 78 LQNVEAgLEALGVGARERRERALAAIdliGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:TIGR01189 91 LENLHF-WAAIHGGAQRTIEDALAAV---GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-205 |
3.51e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.17 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK-PLTGPAEGVAM---VFQTFALFPW-LTVLQN 80
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKFLRRigvVFGQKTQLWWdLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRtD 160
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR-N 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 161 LLDLWTQGRMPikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03267 195 FLKEYNRERGT--TVLLTSHYMKDIEALARRVLVIDK--GRLLYD 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-196 |
3.76e-25 |
|
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: 97.89 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYL--GKPLT----GPAEGVAM-------VFQTF 69
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDlaqaSPREILALrrrtigyVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDgfEN---AYPRELSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:COG4778 103 RVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLP--ERlwdLPPATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 147 SALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIE--EAVfmCDRILVLS 196
Cdd:COG4778 181 ASLDAANRAVVVELIEEAKARGT----AIIGIFHDEEvrEAV--ADRVVDVT 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-203 |
8.23e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 97.56 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-----VAMVFQTFALFPwLTVLQ 79
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlrrqVGVVLQENVLFN-RSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEALGvgarerRERALAAIDLIGLDGFENAYPR-----------ELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:cd03252 95 NIALADPGMS------MERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 149 LDVLTAETLRTDLLDLwTQGRmpikSVLIVTHNIeEAVFMCDRILVLSSnpGRVI 203
Cdd:cd03252 169 LDYESEHAIMRNMHDI-CAGR----TVIIIAHRL-STVKNADRIIVMEK--GRIV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-205 |
9.83e-25 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 97.30 E-value: 9.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP-----LTGPAEGVAMVFQTFALFPwLTVLQN 80
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtLDSLRRAIGVVPQDTVLFN-DTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGleALGVGARERRERALAAI--DLIglDGFENAYPRE-------LSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:cd03253 95 IRYG--RPDATDEEVIEAAKAAQihDKI--MRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 152 LTAETLRTDLLDLwTQGRmpikSVLIVTHNIEEAVfMCDRILVLSSnpGRVIAE 205
Cdd:cd03253 171 HTEREIQAALRDV-SKGR----TTIVIAHRLSTIV-NADKIIVLKD--GRIVER 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-205 |
9.96e-25 |
|
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: 96.91 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPWlTVLQN 80
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGlealgvGARERRERALAAIDLIGLDGF----ENAYPRE-------LSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:cd03254 97 IRLG------RPNATDEEVIEAAKEAGAHDFimklPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 150 DVLTAETLRTDLLDLwtqgrMPIKSVLIVTHN---IEEAvfmcDRILVLssNPGRVIAE 205
Cdd:cd03254 171 DTETEKLIQEALEKL-----MKGRTSIIIAHRlstIKNA----DKILVL--DDGKIIEE 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-181 |
1.03e-24 |
|
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: 100.90 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-VAMVFQTFALFPWL---TVLQNV 81
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSVCAQDAHLfdtTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 eagLEALGVGARERRERALAAIDLI--------GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:TIGR02868 430 ---RLARPDATDEELWAALERVGLAdwlralpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
170 180
....*....|....*....|....*...
gi 1956089794 154 AETLRTDLLDLwtqgrMPIKSVLIVTHN 181
Cdd:TIGR02868 507 ADELLEDLLAA-----LSGRTVVLITHH 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-203 |
1.50e-24 |
|
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: 96.57 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP---TGGEVTYLGKPLTgPAE---GVAMVFQTFALFPWLT 76
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK-PDQfqkCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVE-AGLEALGVGARERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:cd03234 98 VRETLTyTAILRLPRKSSDAIRKKRVEDVLLRDLALTrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 153 TAETLRTDLLDLWTQGRMpiksVLIVTHNIEEAVF-MCDRILVLSSnpGRVI 203
Cdd:cd03234 178 TALNLVSTLSQLARRNRI----VILTIHQPRSDLFrLFDRILLLSS--GEIV 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-205 |
2.76e-24 |
|
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: 95.76 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPWlTVLQN 80
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGLVSQDVFLFND-TVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIglDGFENAYPRE-------LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:cd03251 96 IAYGRPGATREEVEEAARAANAHEFI--MELPEGYDTVigergvkLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 154 aETLRTDLLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILVLSSnpGRVIAE 205
Cdd:cd03251 174 -ERLVQAALERLMKNR----TTFVIAHrlsTIENA----DRIVVLED--GKIVER 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-203 |
3.10e-24 |
|
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: 99.79 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP-----LTGPAEGVAMVFQTFALFPwLTVLQN 80
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDladytLASLRRQVALVSQDVVLFN-DTIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGleALGVGARERRERALAAIDLIGL-----DGF-----ENAypRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:TIGR02203 426 IAYG--RTEQADRAEIERALAAAYAQDFvdklpLGLdtpigENG--VLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 151 VlTAETLRTDLLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILVLSSnpGRVI 203
Cdd:TIGR02203 502 N-ESERLVQAALERLMQGR----TTLVIAHrlsTIEKA----DRIVVMDD--GRIV 546
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-207 |
5.63e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.54 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-----VAMVFQ-----TfalF 72
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkrakyIGRVFQdpmmgT---A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNV--------EAGLeALGVGARER---RERaLAAIDLigldGFENaypR------ELSGGMRQRVGFARALVV 135
Cdd:COG1101 95 PSMTIEENLalayrrgkRRGL-RRGLTKKRRelfREL-LATLGL----GLEN---RldtkvgLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 136 DPTILLMDEPFSALDVLTAETlrtdLLDLwTQGRmpIK----SVLIVTHNIEEAVFMCDRILVLssNPGRVIAEIK 207
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAAL----VLEL-TEKI--VEennlTTLMVTHNMEQALDYGNRLIMM--HEGRIILDVS 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-205 |
5.67e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.02 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP---TGGEVTYLGKPLTGPA-----EGVAMVFQT-FALFPWLT 76
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTvwdirEKVGIVFQNpDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956089794 157 LRTDLLDLWTQGRMPIKSvliVTHNIEEAVfMCDRILVLssNPGRVIAE 205
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVIS---ITHDIDEAN-MADQVLVL--DDGKLLAQ 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-195 |
6.74e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.72 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP---TGGEVTYLGKP-LTGP--------AEGVAMVFQ-- 67
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREiLNLPekelnklrAEQISMIFQdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 68 TFALFPWLTV-LQNVEAGLEALGVGARERRE---RALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMD 143
Cdd:PRK09473 107 MTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEesvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 144 EPFSALDVLTAETLRTDLLDLwtqGRMPIKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNEL---KREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
6-203 |
7.33e-24 |
|
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: 98.86 E-value: 7.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPL-----TGPAEGVAMVFQTFALFPWlTVLQN 80
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPReeiprEVLANSVAMVDQDIFLFEG-TVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 V--------EAGLEalgvgarerreRAL--AAI-DLI-----GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:TIGR03796 573 LtlwdptipDADLV-----------RACkdAAIhDVItsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDE 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 145 PFSALDvltAETLRTDLLDLWTQGrmpiKSVLIVTHNIeEAVFMCDRILVLssNPGRVI 203
Cdd:TIGR03796 642 ATSALD---PETEKIIDDNLRRRG----CTCIIVAHRL-STIRDCDEIIVL--ERGKVV 690
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-217 |
1.16e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIE------PTGGEVTYLGKPL-----TGPAEGVAMVFQTFALFPW 74
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfqidaIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNVEAGLEALGVG-ARERRERALAAIDLIGLdgFENAYPR------ELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 148 ALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEIKVPFKHPRNRL 217
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-----IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-204 |
1.42e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.19 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK-----PLTGPA-EGVAMVFQTFALFPWLTVLQ 79
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARArRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEAL-GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:PRK10895 98 NLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 159 TDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:PRK10895 178 RIIEHLRDSGL----GVLITDHNVRETLAVCERAYIVSQ--GHLIA 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-206 |
2.47e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 4 LLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE----GVAMV---FQTFALFPW 74
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsPRErrrlGVAYIpedRLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNV---EAGLEALGVGARERRERALA-AIDLIglDGF------ENAYPRELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:COG3845 351 MSVAENLilgRYRRPPFSRGGFLDRKAIRAfAEELI--EEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 145 PFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEI 206
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAG----AAVLLISEDLDEILALSDRIAVMYE--GRIVGEV 484
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-214 |
3.72e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 94.81 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTG----GEVTYLGKPLTGPAEG---------VAMVFQ--TFAL 71
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKerrnlvgaeVAMIFQdpMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTV-LQNVEAGLEALGVGARERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:PRK11022 103 NPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 148 ALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKVP--FKHPR 214
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENM---ALVLITHDLALVAEAAHKIIVMYA--GQVVETGKAHdiFRAPR 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-201 |
5.44e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.47 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAEG----VAMVFQTFALF---- 72
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIyrqqVSYCAQTPTLFgdtv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 ------PWLTVLQNVEaglealgvgarerrERALAAidliGLDGFE------NAYPRELSGGMRQRVGFARALVVDPTIL 140
Cdd:PRK10247 98 ydnlifPWQIRNQQPD--------------PAIFLD----DLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 141 LMDEPFSALDvltaETLRTDLLDLWTQ-GRMPIKSVLIVTHNIEEaVFMCDRILVLSSNPGR 201
Cdd:PRK10247 160 LLDEITSALD----ESNKHNVNEIIHRyVREQNIAVLWVTHDKDE-INHADKVITLQPHAGE 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-204 |
5.59e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.75 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-PAE-----GVAMVFQTFALFPWL 75
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHqiarmGVVRTFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQN--------VEAGL-------EALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 140
Cdd:PRK11300 96 TVIENllvaqhqqLKTGLfsgllktPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 141 LMDEPFSALDvlTAETlrTDLLDLWTQGRMPIK-SVLIVTHNIEEAVFMCDRILVLssNPGRVIA 204
Cdd:PRK11300 176 MLDEPAAGLN--PKET--KELDELIAELRNEHNvTVLLIEHDMKLVMGISDRIYVV--NQGTPLA 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-208 |
9.80e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.24 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK------PLTGPAEGVAMVFQTFALFPWLTVLQN 80
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldHKLAAQLGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGL----EALGVGA---RERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:PRK09700 101 LYIGRhltkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 154 AETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL---SSNPGRVIAEIKV 208
Cdd:PRK09700 181 VDYLFLIMNQLRKEG----TAIVYISHKLAEIRRICDRYTVMkdgSSVCSGMVSDVSN 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-205 |
1.24e-22 |
|
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: 90.06 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP----AEGVAMVFQTFALFPwLTVL 78
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLekalSSLISVLNQRPYLFD-TTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNveaglealgVGARerreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:cd03247 93 NN---------LGRR-------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 159 TDLLDLwtqgrMPIKSVLIVTHNIeEAVFMCDRILVLSSnpGRVIAE 205
Cdd:cd03247 139 SLIFEV-----LKDKTLIWITHHL-TGIEHMDKILFLEN--GKIIMQ 177
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
7-204 |
1.41e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEV---------TYLGKPLTGPAEGVAMVFQtfalFPWL-- 75
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvssTSKQKEIKPVRKKVGVVFQ----FPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 ---TVLQNVEAGLEALGVGARERRERALAAIDLIGLDG-FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDv 151
Cdd:PRK13643 98 feeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 152 ltaETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:PRK13643 177 ---PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEK--GHIIS 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-203 |
1.50e-22 |
|
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: 91.82 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 9 DANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPlTGPAEGVAMV---FQTFALFPWLTVLQNVEAGL 85
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRS-GAELELYQLSeaeRRRLMRTEWGFVHQNPRDGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 EA------------LGVGARER-RERALAA-------IDLIGLDGFenayPRELSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:TIGR02323 100 RMrvsaganigerlMAIGARHYgNIRATAQdwleeveIDPTRIDDL----PRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 146 FSALDVltaeTLRTDLLDLwTQG--RMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:TIGR02323 176 TGGLDV----SVQARLLDL-LRGlvRDLGLAVIIVTHDLGVARLLAQRLLVMQQ--GRVV 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-217 |
3.53e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIE-----PTGGEVTYLGK-----PLTGPAEGVAMVFQTFAL 71
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQdifkmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVEAGLE--ALGVGARERRERALAAIDLIGL-DGFEN---AYPRELSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:PRK14247 94 IPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLwDEVKDrldAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 146 FSALDVLTAETLRTDLLDLwtQGRMPIksvLIVTHNIEEAVFMCDRILVLSSnpGRVIAE--IKVPFKHPRNRL 217
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL--KKDMTI---VLVTHFPQQAARISDYVAFLYK--GQIVEWgpTREVFTNPRHEL 240
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-203 |
3.61e-22 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 90.29 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTllriIAGLIE----PTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFP 73
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDIRDLNlrwlrSQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 wLTVLQNVEAGLEALGVGARERRERALAAIDLIglDGFENAY-----PR--ELSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:cd03249 91 -GTIAENIRYGKPDATDEEVEEAAKKANIHDFI--MSLPDGYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 147 SALDVLTaETLRTDLLDLWTQGRMpiksVLIVTHNIeEAVFMCDRILVLSsnPGRVI 203
Cdd:cd03249 168 SALDAES-EKLVQEALDRAMKGRT----TIVIAHRL-STIRNADLIAVLQ--NGQVV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-203 |
3.63e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYlgkpltgpAEGVAMVFqtFA-----LFPWLT 76
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------GETVKIGY--FDqhqeeLDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEalgvGARERRERA-LAAIDLIGLDGFENAypRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAE 155
Cdd:COG0488 396 VLDELRDGAP----GGTEQEVRGyLGRFLFSGDDAFKPV--GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLE 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 156 TLrTDLLDLWtQGrmpikSVLIVTHNIEeavFM---CDRILVLSsnPGRVI 203
Cdd:COG0488 470 AL-EEALDDF-PG-----TVLLVSHDRY---FLdrvATRILEFE--DGGVR 508
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-196 |
3.79e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVT----YLGKPLTGPAEG----------------- 61
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELItnpyskkiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 62 VAMVFQ--TFALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPT 138
Cdd:PRK13631 118 VSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 139 ILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLS 196
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNK----TVFVITHTMEHVLEVADEVIVMD 250
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-203 |
4.04e-22 |
|
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: 89.86 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPWl 75
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlhdlrSRISIIPQDPVLFSG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNV--------EAGLEAL-GVGARERRERALAAIDLIGLDGFENaypreLSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:cd03244 93 TIRSNLdpfgeysdEELWQALeRVGLKEFVESLPGGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 147 SALDVLTA----ETLRTdlldlwtqgRMPIKSVLIVTHNIeEAVFMCDRILVLSSnpGRVI 203
Cdd:cd03244 168 ASVDPETDaliqKTIRE---------AFKDCTVLTIAHRL-DTIIDSDRILVLDK--GRVV 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-217 |
5.13e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.29 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIE-----PTGGEVTYLGKPLTGPA-------EGVAMVFQTF 69
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDvdpievrREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPWLTVLQNVEAGLE--ALGVGARERRERALAAIDLIGL-DGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMD 143
Cdd:PRK14267 95 NPFPHLTIYDNVAIGVKlnGLVKSKKELDERVEWALKKAALwDEVKdrlNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 144 EPFSALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEIKVPFKHPRNRL 217
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKE-----YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
2-205 |
5.43e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.14 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQTFALFPWLT 76
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpsrelAKRLAILRQENHINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAG--------LEAlgvgarERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:COG4604 92 VRELVAFGrfpyskgrLTA------EDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 149 LDVLTA----ETLR--TDLLDlwtqgrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:COG4604 166 LDMKHSvqmmKLLRrlADELG---------KTVVIVLHDINFASCYADHIVAMKD--GRVVAQ 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-195 |
5.70e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 13 SLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT-----GPAEGVAMVFQ--TFALFPWLTVLQNVEAGL 85
Cdd:PRK15112 35 TLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysYRSQRIRMIFQdpSTSLNPRQRISQILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 EA-LGVGARERRERALAAIDLIGL-DGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLD 163
Cdd:PRK15112 115 RLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM----SMRSQLIN 190
|
170 180 190
....*....|....*....|....*....|....
gi 1956089794 164 LW--TQGRMPIkSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK15112 191 LMleLQEKQGI-SYIYVTQHLGMMKHISDQVLVM 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-202 |
5.81e-22 |
|
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: 93.54 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP----LTGPAEGVAMVFQTFALFPWLTVLQNVE 82
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDietnLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLL 162
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI-WDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956089794 163 DLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRV 202
Cdd:TIGR01257 1105 LKYRSGR----TIIMSTHHMDEADLLGDRIAIISQ--GRL 1138
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-195 |
7.22e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPWlTV 77
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGARERRERALAAIDLIGldGFENAYPRE-------LSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDLldlwTQGRMPiksVLIVTHNIeEAVFMCDRILVL 195
Cdd:TIGR00958 650 AECEQLLQESR----SRASRT---VLLIAHRL-STVERADQILVL 686
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-198 |
7.81e-22 |
|
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: 87.12 E-value: 7.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTylgkplTGPAEGVAMVFQtfalfpwltvlqnv 81
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------WGSTVKIGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 eaglealgvgarerreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDL 161
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956089794 162 LDLwtQGrmpikSVLIVTHNIEeavFM---CDRILVLSSN 198
Cdd:cd03221 114 KEY--PG-----TVILVSHDRY---FLdqvATKIIELEDG 143
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-206 |
7.91e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 7.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG---------VAMVFQtfalFPWL-- 75
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikqirkkVGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 ---TVLQNVEAGLEALGVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:PRK13649 99 feeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 152 LTaetlRTDLLDLWTQGRMPIKSVLIVTH------NIEEAVFMCDR-ILVLSSNPGRVIAEI 206
Cdd:PRK13649 179 KG----RKELMTLFKKLHQSGMTIVLVTHlmddvaNYADFVYVLEKgKLVLSGKPKDIFQDV 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
12-205 |
9.46e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 9.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 12 LSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQTFALFPWLTVLQNVEAGLE 86
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsskafARKVAYLPQQLPAAEGMTVRELVAIGRY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 ----ALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLL 162
Cdd:PRK10575 112 pwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI----AHQVDVL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 163 DLWTQ-GRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK10575 188 ALVHRlSQERGLTVIAVLHDINMAARYCDYLVALRG--GEMIAQ 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1-196 |
2.21e-21 |
|
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: 91.64 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT-------GPAegVAMVFQTFALFP 73
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwdretfGKH--IGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WlTVLQNVeaglealgvgARERR----ERALAAIDLIGLD----GFENAYPRE-------LSGGMRQRVGFARALVVDPT 138
Cdd:TIGR01842 406 G-TVAENI----------ARFGEnadpEKIIEAAKLAGVHelilRLPDGYDTVigpggatLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 139 ILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIeeAVFMC-DRILVLS 196
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGI----TVVVITHRP--SLLGCvDKILVLQ 527
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-204 |
2.86e-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: 90.96 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT-------GPAegVAMVFQTFALFPWlTVL 78
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreelGRH--IGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNV--------EAGLEAlgvgARerreraLAAI-DLIGL--DGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:COG4618 424 ENIarfgdadpEKVVAA----AK------LAGVhEMILRlpDGYDtriGEGGARLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 145 PFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIeEAVFMCDRILVLssNPGRVIA 204
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARG----ATVVVITHRP-SLLAAVDKLLVL--RDGRVQA 546
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-186 |
3.25e-21 |
|
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: 87.16 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP----AEGVAMVFQTFALFPWLT 76
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrdsiARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAgLEALGvgareRRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:cd03231 90 VLENLRF-WHADH-----SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 1956089794 157 LRTDLLDLWTQGRMpiksVLIVTH---NIEEAV 186
Cdd:cd03231 164 FAEAMAGHCARGGM----VVLTTHqdlGLSEAG 192
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-192 |
3.51e-21 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 88.33 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKpltgpaegVAMVFQTFALFPWLTVLQNVEAGLE 86
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------VSVIAISAGLSGQLTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 ALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWT 166
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD----QTFAQKCLDKIY 187
|
170 180
....*....|....*....|....*.
gi 1956089794 167 QGRMPIKSVLIVTHNIEEAVFMCDRI 192
Cdd:PRK13546 188 EFKEQNKTIFFVSHNLGQVRQFCTKI 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-195 |
1.16e-20 |
|
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: 89.50 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGlIEPTG---GEVTYLGKPLTG------PAEGVAMVFQTFALF 72
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKAsnirdtERAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVEAGLEALGVGAR----ERRERALAAIDLIGLDGFENAYP-RELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:TIGR02633 91 PELSVAENIFLGNEITLPGGRmaynAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 148 ALDVLTAETLRTDLLDLWTQGrmpIKSVLIvTHNIEEAVFMCDRILVL 195
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHG---VACVYI-SHKLNEVKAVCDTICVI 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-204 |
1.52e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.41 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 8 DDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTgpAEGVA-------MVfQTFALFPWLTVLQN 80
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--AGDIAtrrrvgyMS-QAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEagLEA--LGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:NF033858 360 LE--LHArlFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 159 TDLLDLWTQGRMPIksvLIVTHnieeavFM-----CDRIlvlsS--NPGRVIA 204
Cdd:NF033858 438 RLLIELSREDGVTI---FISTH------FMneaerCDRI----SlmHAGRVLA 477
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-204 |
2.18e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-------VAMVFQ--TFALFpWLT 76
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalrqqVATVFQdpEQQIF-YTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 157 LRTDLLDLWTQGRmpikSVLIVTHNIE------EAVFMCDRILVLSS-NPGRVIA 204
Cdd:PRK13638 175 MIAIIRRIVAQGN----HVIISSHDIDliyeisDAVYVLRQGQILTHgAPGEVFA 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-195 |
2.37e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWLTVLQ 79
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltPAKahqlGIYLVPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEAlGVGARERRERALAAIDlIGLDGFENAYPRELSGgmRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:PRK15439 106 NILFGLPK-RQASMQKMKQLLAALG-CQLDLDSSAGSLEVAD--RQIVEILRGLMRDSRILILDEPTASLTPAETERLFS 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956089794 160 DLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK15439 182 RIRELLAQG----VGIVFISHKLPEIRQLADRISVM 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-190 |
2.59e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRI---IAGLIEP--TGGEVTYLGKPLTG----PAE---GVAMVFQTF 69
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYApdvdPVEvrrRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPwLTVLQNVEAGLEALG--VGARERRERAL--AAI-----DLIGLDGFEnaypreLSGGMRQRVGFARALVVDPTIL 140
Cdd:PRK14243 101 NPFP-KSIYDNIAYGARINGykGDMDELVERSLrqAALwdevkDKLKQSGLS------LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 141 LMDEPFSALD---VLTAETLRTDLLDLWTqgrmpiksVLIVTHNIEEAVFMCD 190
Cdd:PRK14243 174 LMDEPCSALDpisTLRIEELMHELKEQYT--------IIIVTHNMQQAARVSD 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-195 |
4.43e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGlIEPTG---GEVTYLGKPLTG------PAEGVAMVFQTFALFPWLTV 77
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQAsnirdtERAGIAIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEaLGVGAR-------ERRERALAAidlIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PRK13549 100 LENIFLGNE-ITPGGImdydamyLRAQKLLAQ---LKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDLLDLWTQGrmpIKSVLIvTHNIEEAVFMCDRILVL 195
Cdd:PRK13549 176 ESETAVLLDIIRDLKAHG---IACIYI-SHKLNEVKAISDTICVI 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-203 |
4.58e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPltgP-------AEGVAMVF-QTFALFPWLTVL 78
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PfkrrkefARRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAgLEAL-GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:COG4586 115 DSFRL-LKAIyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956089794 158 RTDLLDLWTQGRMpikSVLIVTHN---IEEavfMCDRILVLssNPGRVI 203
Cdd:COG4586 194 REFLKEYNRERGT---TILLTSHDmddIEA---LCDRVIVI--DHGRII 234
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-195 |
4.67e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.50 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP----TGGEVTYLGKPLTG--PAE-------GVAMVFQ 67
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKlsPRErrkiigrEIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 68 --TFALFPWLTVLQNVEAGLEALGVGAR------ERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVD 136
Cdd:COG4170 97 epSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfkWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 137 PTILLMDEPFSALDVLT-AETLRtdLLDLWTQGR-MpikSVLIVTHNIEEAVFMCDRILVL 195
Cdd:COG4170 177 PRLLIADEPTNAMESTTqAQIFR--LLARLNQLQgT---SILLISHDLESISQWADTITVL 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-205 |
5.40e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.53 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQT-FALFPWLTVLQN 80
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvwnlRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTD 160
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD----PTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 161 LLDLWTQGRMPIK-SVLIVTHNIEEAVfMCDRILVLSSnpGRVIAE 205
Cdd:PRK13642 179 IMRVIHEIKEKYQlTVLSITHDLDEAA-SSDRILVMKA--GEIIKE 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-202 |
6.90e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTG-----GEVTYLGKP-------LTGPAEGVAMVFQTFALFP 73
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNiyerrvnLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 wLTVLQNVEAGLEALG----VGARERRERALAAIDLigLDGFENAYPR---ELSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGwrpkLEIDDIVESALKDADL--WDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 147 SALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSNPGRV 202
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSEL---TMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-199 |
9.11e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.55 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--VAMVFQTFAL---FPWLT---VL 78
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEVdwsFPVLVedvVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLR 158
Cdd:PRK15056 103 MGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 159 TDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRIL-----VLSSNP 199
Cdd:PRK15056 183 SLLRELRDEGK----TMLVSTHNLGSVTEFCDYTVmvkgtVLASGP 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-158 |
1.31e-19 |
|
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: 86.53 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYlgkpltGPAEGVAMVFQTF-ALFPWLTVLQN 80
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYVDQSRdALDPNKTVWEE 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 81 VEAGLEALGVGARERRERA-LAAIDLIGLDgfENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaETLR 158
Cdd:TIGR03719 407 ISGGLDIIKLGKREIPSRAyVGRFNFKGSD--QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV---ETLR 480
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-203 |
1.68e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 14 LREGEIVGLLGRSGSGKSTLLRIIAGLIEP---TGGEVTYLGKPLTGPAEGV--AMVFQTFALFPWLTVLqnveaglEAL 88
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVR-------EHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 89 GVGAR----------ERRERALAAIDLIGLD-------GFENAYpRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:TIGR00955 121 MFQAHlrmprrvtkkEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 152 LTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVF-MCDRILVLSSnpGRVI 203
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGK----TIICTIHQPSSELFeLFDKIILMAE--GRVA 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-205 |
1.84e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGeVTYLGKPLTGPA------------EGVAMVFQTFALFP 73
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRsifnyrdvlefrRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 wLTVLQNVEAGLEALG-VGARERRERALAAIDLIGL-DGFENAY---PRELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 149 LDVLTAETLRTDLLDLwtQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK14271 194 LDPTTTEKIEEFIRSL--ADRL---TVIIVTHNLAQAARISDRAALFFD--GRLVEE 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-211 |
3.93e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIeptggeVTYLGKPLTG----PA------------EGVAMVF 66
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIVGdyaiPAnlkkikevkrlrKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 67 Q--TFALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGL-DGFENAYPRELSGGMRQRVGFARALVVDPTILLMD 143
Cdd:PRK13645 97 QfpEYQLFQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 144 EPFSALDVLTAEtlrtDLLDLWTQ-GRMPIKSVLIVTHNIEEAVFMCDRILVLssNPGRVIaEIKVPFK 211
Cdd:PRK13645 176 EPTGGLDPKGEE----DFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVIVM--HEGKVI-SIGSPFE 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
5.23e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.93 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQT-----FA 70
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevRKFVGLVFQNpddqiFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 71 LfpwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PRK13652 94 P----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLssNPGRVIAE 205
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGM---TVIFSTHQLDLVPEMADYIYVM--DKGRIVAY 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-203 |
5.66e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKS-TLLRIIAGLIEP----TGGEVTYLGKPLTGPAEG---------VAMVFQ--TF 69
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQtlrgvrgnkIAMIFQepMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPwltvLQNVEAGL-EALGVGARERRERALAAIdLIGLD--GFENA------YPRELSGGMRQRVGFARALVVDPTIL 140
Cdd:PRK15134 104 SLNP----LHTLEKQLyEVLSLHRGMRREAARGEI-LNCLDrvGIRQAakrltdYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 141 LMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVI 203
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNM---GLLFITHNLSIVRKLADRVAVMQN--GRCV 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-196 |
1.92e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 83.01 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 17 GEIVGLLGRSGSGKSTLLRIIAGLIEP---TGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQN-VEAGLEAL--GV 90
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnfTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETlVFCSLLRLpkSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 91 GARERRERALAAIDLIGLDGFEN-----AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLW 165
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170 180 190
....*....|....*....|....*....|..
gi 1956089794 166 TQGrmpiKSVLIVTHNIEEAVF-MCDRILVLS 196
Cdd:PLN03211 254 QKG----KTIVTSMHQPSSRVYqMFDSVLVLS 281
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-217 |
2.12e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.51 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 8 DDANLSLREGEIVGLLGRSGSGKS----TLLRIIAGLIEPTGGEVTYLGKPLTG---PAEGVAMVFQT--FALFPWLTVL 78
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPcalRGRKIATIMQNprSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALGVGARERRerALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLtAE 155
Cdd:PRK10418 100 THARETCLALGKPADDAT--LTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV-AQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 156 TLRTDLLDLWTQGRMPikSVLIVTHNIEEAVFMCDRILVLSSnpGRVI--AEIKVPFKHPRNRL 217
Cdd:PRK10418 177 ARILDLLESIVQKRAL--GMLLVTHDMGVVARLADDVAVMSH--GRIVeqGDVETLFNAPKHAV 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-180 |
3.84e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLieptggevtYLGKPLTGPAEgvamvfqtfalFPWLTVLQNVeAGL 85
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA---------LKGTPVAGCVD-----------VPDNQFGREA-SLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 EALGvgareRRERALAAIDLIGLDGFENAY-----PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTD 160
Cdd:COG2401 104 DAIG-----RKGDFKDAVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170 180
....*....|....*....|
gi 1956089794 161 LLDLWTQGRmpiKSVLIVTH 180
Cdd:COG2401 179 LQKLARRAG---ITLVVATH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-208 |
4.25e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAE----GVAMVFQTFALFPWLTVLQN 80
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSsqeaGIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLE---ALG-VGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 156
Cdd:PRK10762 100 IFLGREfvnRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETES 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 157 LRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEIKV 208
Cdd:PRK10762 180 LFRVIRELKSQGR----GIVYISHRLKEIFEICDDVTVFRD--GQFIAEREV 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-154 |
4.58e-18 |
|
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: 78.84 E-value: 4.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTG---GEVTYLGKPLTGPAE----GVAMVFQTFALFPWL 75
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEkypgEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 76 TVLQNVEAGLEALGvgarerreralaaidligldgfeNAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 154
Cdd:cd03233 99 TVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-205 |
4.64e-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: 78.72 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGL--IEPTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWLTV 77
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDlpPEErarlGIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 ---LQNVEAGlealgvgarerreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDV--- 151
Cdd:cd03217 95 adfLRYVNEG----------------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdal 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 152 -LTAETLRTdLLDlwtqgrmPIKSVLIVTHNIEEAVFM-CDRILVLSSnpGRVIAE 205
Cdd:cd03217 141 rLVAEVINK-LRE-------EGKSVLIITHYQRLLDYIkPDRVHVLYD--GRIVKS 186
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-202 |
6.61e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.80 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP-----AEGVAMVFQTFA-LFPWLT 76
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnfeklRKHIGIVFQNPDnQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaET 156
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD----PD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 157 LRTDLLDLWTQGRMPiKSVLI--VTHNIEEAVfMCDRILVLssNPGRV 202
Cdd:PRK13648 177 ARQNLLDLVRKVKSE-HNITIisITHDLSEAM-EADHVIVM--NKGTV 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-194 |
7.55e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.22 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK-----PLTGPAEGVAMVFQTFALFPwLTV 77
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVALVSQNVHLFN-DTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEalGVGARERRERA--LA-AIDLI-----GLDGF--ENAYprELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:PRK11176 434 ANNIAYART--EQYSREQIEEAarMAyAMDFInkmdnGLDTVigENGV--LLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 148 ALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTH---NIEEAvfmcDRILV 194
Cdd:PRK11176 510 ALDTESERAIQAALDELQKN-----RTSLVIAHrlsTIEKA----DEILV 550
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-203 |
1.19e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK-----PLTGPAEGVAMVFQTFALFPwLTVLQNV 81
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvTRASLRRNIAVVFQDAGLFN-RSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLE-ALGVGARERRERAlAAIDLI-----GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAE 155
Cdd:PRK13657 430 RVGRPdATDEEMRAAAERA-QAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 156 TLRtDLLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILVLSSnpGRVI 203
Cdd:PRK13657 509 KVK-AALDELMKGR----TTFIIAHrlsTVRNA----DRILVFDN--GRVV 548
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-200 |
1.79e-17 |
|
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: 78.22 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 13 SLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVtylGKPLtgpaEGVAMVFQTF-ALFPwLTVLQNVEAGLEALGVG 91
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIEL----DTVSYKPQYIkADYE-GTVRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 92 ARERREralaAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRTDLLDlwTQ 167
Cdd:cd03237 93 PYFKTE----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAEN--NE 166
|
170 180 190
....*....|....*....|....*....|...
gi 1956089794 168 grmpiKSVLIVTHNIEEAVFMCDRILVLSSNPG 200
Cdd:cd03237 167 -----KTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-209 |
3.70e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.08 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVlDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYlgkPltgPAEGVAMVFQTfALFPWLTVLqn 80
Cdd:COG4178 374 DGRPLL-EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P---AGARVLFLPQR-PYLPLGTLR-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 veaglEALGVGARERR---ERALAAIDLIGLDGF------ENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:COG4178 444 -----EALLYPATAEAfsdAELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 152 LTAETLRTDLLDlwtqgRMPIKSVLIVTHNIEEAVFmCDRILVLSSNPGRVIAEIKVP 209
Cdd:COG4178 519 ENEAALYQLLRE-----ELPGTTVISVGHRSTLAAF-HDRVLELTGDGSWQLLPAEAP 570
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-200 |
3.82e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.22 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLG------------KPLTGP-----AEGVAMVFQTF 69
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEGTvydfvAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 70 ALFPWLTV-------------LQNVEAGLEALGVGARERRERALaaIDLIGLDGfeNAYPRELSGGMRQRVGFARALVVD 136
Cdd:PRK11147 99 KRYHDISHlvetdpseknlneLAKLQEQLDHHNLWQLENRINEV--LAQLGLDP--DAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 137 PTILLMDEPFSALDVLTAETLRTDLLDLwtQGrmpikSVLIVTHNIEEAVFMCDRIL-----VLSSNPG 200
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-----SIIFISHDRSFIRNMATRIVdldrgKLVSYPG 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-207 |
4.14e-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: 79.29 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTgpaEGVAMVFQTFALFPWLTVLQNVEAGLE 86
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 AL-------GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 159
Cdd:TIGR01257 2032 HLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 160 DLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSNPGRVIAEIK 207
Cdd:TIGR01257 2112 TIVSIIREGR----AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-204 |
4.86e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.01 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAmVFQTFA---------LF 72
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA-VCPRIAympqglgknLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVE--AGLeaLGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:NF033858 91 PTLSVFENLDffGRL--FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 151 VLT-------AETLRTdlldlwtqgRMPIKSVLIVTHNIEEAV-FmcDRILVLssNPGRVIA 204
Cdd:NF033858 169 PLSrrqfwelIDRIRA---------ERPGMSVLVATAYMEEAErF--DWLVAM--DAGRVLA 217
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-195 |
5.03e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 78.78 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTylgkpLTGPAEGVAMvfqTFALFPWLTVLQNVEAGLE 86
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD-----IKGSAALIAI---SSGLNGQLTGIENIELKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 87 ALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWT 166
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD----QTFTKKCLDKMN 187
|
170 180
....*....|....*....|....*....
gi 1956089794 167 QGRMPIKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK13545 188 EFKEQGKTIFFISHSLSQVKSFCTKALWL 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-205 |
1.25e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLI--EPTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWLTV 77
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILElsPDEraraGIFLAFQYPVEIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALG---VGARERRERALAAIDLIGLDgfENAYPREL----SGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:COG0396 95 SNFLRTALNARRgeeLSAREFLKLLKEKMKELGLD--EDFLDRYVnegfSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 151 VltaetlrtDLLDLWTQG----RMPIKSVLIVTHN---IEEAVfmCDRILVLSSnpGRVIAE 205
Cdd:COG0396 173 I--------DALRIVAEGvnklRSPDRGILIITHYqriLDYIK--PDFVHVLVD--GRIVKS 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-180 |
1.41e-16 |
|
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: 77.67 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTylgkpltgPAEG--VAMVFQTFALFPWLTVLQNVEA 83
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPGikVGYLPQEPQLDPTKTVRENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 84 GL-EALGVGAR-------------------ERRERALAAIDLIGLDGFEN---------------AYPRELSGGMRQRVG 128
Cdd:TIGR03719 92 GVaEIKDALDRfneisakyaepdadfdklaAEQAELQEIIDAADAWDLDSqleiamdalrcppwdADVTKLSGGERRRVA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 129 FARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGrmpikSVLIVTH 180
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-----TVVAVTH 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-195 |
1.44e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGV------------------ 62
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVielseqsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 63 -AMVFQ--TFALFPWLTVLQNVEaglEALGVGARERRERALAA----IDLIGLDGFE---NAYPRELSGGMRQRVGFARA 132
Cdd:PRK10261 106 mAMIFQepMTSLNPVFTVGEQIA---ESIRLHQGASREEAMVEakrmLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 133 LVVDPTILLMDEPFSALDVltaeTLRTDLLDLWT--QGRMPIkSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDV----TIQAQILQLIKvlQKEMSM-GVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-158 |
1.45e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.47 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYlgkpltGPAEGVAMVFQTF-ALFPWLTVLQN 80
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYVDQSRdALDPNKTVWEE 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 81 VEAGLEALGVGARERRERA-LAAIDLIGLDgfENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaETLR 158
Cdd:PRK11819 409 ISGGLDIIKVGNREIPSRAyVGRFNFKGGD--QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV---ETLR 482
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-205 |
1.63e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.02 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAG-LIEPTG-------GEVTYLGKPLTG-PAEGVAMVFQTFA-----L 71
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAiDAPRLARLRAVLPqaaqpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLT---VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARAL---------VVDPTI 139
Cdd:PRK13547 96 FAFSAreiVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 140 LLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNL---GVLAIVHDPNLAARHADRIAMLAD--GAIVAH 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-205 |
1.89e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG------PAEGVAMVFQTFALFPWL 75
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGlealgvGARERRERALAAIDLIgLDGFENAYPRE------LSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:PRK11614 96 TVEENLAMG------GFFAERDQFQERIKWV-YELFPRLHERRiqragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 150 dvltAETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK11614 169 ----APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLEN--GHVVLE 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-204 |
2.24e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.17 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAE-----GVAMVFQTFALFP-- 73
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEaalrqAISVVSQRVHLFSat 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 ----------------WLTVLQNVeaGLEALgvgarerreralaAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDP 137
Cdd:PRK11160 430 lrdnlllaapnasdeaLIEVLQQV--GLEKL-------------LEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 138 TILLMDEPFSALDvltAETLRT--DLLDLWTQGrmpiKSVLIVTHNIEEAVFMcDRILVLSSnpGRVIA 204
Cdd:PRK11160 495 PLLLLDEPTEGLD---AETERQilELLAEHAQN----KTVLMITHRLTGLEQF-DRICVMDN--GQIIE 553
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
11-204 |
2.87e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLREGEIVGLLGRSGSGKSTLLRIIAGLIePTGGEVTYLGKPLTG-PAEGVA----MVFQTFALFPWLTVLQNVEAGL 85
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELArhraYLSQQQSPPFAMPVFQYLALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 EAlgVGARERRERALAAI-DLIGLdgfENAYPR---ELSGGMRQRVGFARALV-VDPTI------LLMDEPFSALDVLTA 154
Cdd:COG4138 95 PA--GASSEAVEQLLAQLaEALGL---EDKLSRpltQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 155 ETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:COG4138 170 AALDRLLRELCQQGI----TVVMSSHDLNHTLRHADRVWLLKQ--GKLVA 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
6-195 |
3.20e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.67 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPwLTVLQN 80
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldswrSRLAVVSQTPFLFS-DTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VeagleALGV--GARERRERA--LAAI--DLIGL-DGFENAYPRE---LSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PRK10789 409 I-----ALGRpdATQQEIEHVarLASVhdDILRLpQGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDlLDLWTQGRmpikSVLIVTHNIeEAVFMCDRILVL 195
Cdd:PRK10789 484 GRTEHQILHN-LRQWGEGR----TVIISAHRL-SALTEASEILVM 522
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-195 |
4.37e-16 |
|
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: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAegvamvfqtfalFPWL---TVLQNVe 82
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWImpgTIKDNI- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 agleALGVGARERRERALaaIDLIGLDGFENAYPRE-----------LSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:TIGR01271 508 ----IFGLSYDEYRYTSV--IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 152 LT-AETLRTDLLDLwtqgrMPIKSVLIVTHNIEEaVFMCDRILVL 195
Cdd:TIGR01271 582 VTeKEIFESCLCKL-----MSNKTRILVTSKLEH-LKKADKILLL 620
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-195 |
4.46e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.92 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA------EGVAMVFQTFALFPWLTVLQN 80
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSskealeNGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAG---LEALGVGARERRERALAAIDLIGLDgfenAYPRE----LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:PRK10982 94 MWLGrypTKGMFVDQDKMYRDTKAIFDELDID----IDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956089794 154 AETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK10982 170 VNHLFTIIRKLKERG----CGIVYISHKMEEIFQLCDEITIL 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
6-195 |
4.98e-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: 74.51 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKpltgpaegVAMVFQTFALFPWlTVLQNVeagl 85
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQFSWIMPG-TIKENI---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 eALGVGARERRERALAAI-----DLIGLDGFENAYPRE----LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAEt 156
Cdd:cd03291 119 -IFGVSYDEYRYKSVVKAcqleeDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK- 196
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956089794 157 lrtDLLDLWTQGRMPIKSVLIVTHNIEEaVFMCDRILVL 195
Cdd:cd03291 197 ---EIFESCVCKLMANKTRILVTSKMEH-LKKADKILIL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-205 |
5.16e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAEGVA--MVF-----QTFALFPWLTV 77
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrSPQDGLAngIVYisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEagLEAL------GVGARERRERaLAAIDLIGLdgFENAYP------RELSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:PRK10762 348 KENMS--LTALryfsraGGSLKHADEQ-QAVSDFIRL--FNIKTPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 146 FSALDVlTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK10762 423 TRGVDV-GAKKEIYQLINQFKAEGL---SIILVSSEMPEVLGMSDRILVMHE--GRISGE 476
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-195 |
8.14e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGpaegvaMVFQTFALFPWLTVLQNV 81
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIG------YVPQKLYLDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEAlGVgareRRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDL 161
Cdd:PRK09544 89 FLRLRP-GT----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV----NGQVAL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1956089794 162 LDLWTQGRMPIK-SVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK09544 160 YDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-205 |
1.13e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.66 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLG---------KPLTGPAEGVAMVFQtfalFP 73
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WL-----TVLQNVEAGLEALGVGARERRERALaaiDLIGLDGFE----NAYPRELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:PRK13646 95 ESqlfedTVEREIIFGPKNFKMNLDEVKNYAH---RLLMDLGFSrdvmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 145 PFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLssNPGRVIAE 205
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDEN---KTIILVSHDMNEVARYADEVIVM--KEGSIVSQ 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-182 |
3.28e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 3 ELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG--------VAMVFQT--FALF 72
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrdIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVEAGLEALGVG-ARERRERALAAIDLIGLDGfENA--YPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLpGKAAAARVAWLLERVGLLP-EHAwrYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190
....*....|....*....|....*....|...
gi 1956089794 150 DVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNI 182
Cdd:PRK10261 495 DVSIRGQIINLLLDL--QRDFGI-AYLFISHDM 524
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-206 |
4.64e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 9 DANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK------PLTGPAEGVAMVFQT---FALFPWLTVLQ 79
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKKGMAYITESrrdNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NV-------EAGLE-ALG-VGARERRERALAAIDLIGLDGFE-NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:PRK09700 361 NMaisrslkDGGYKgAMGlFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 150 DVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEI 206
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADDG----KVILMVSSELPEIITVCDRIAVFCE--GRLTQIL 491
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-180 |
1.10e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTylgkpltgPAEG--VAMVFQTFALFPWLTVLQNVEA 83
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PAPGikVGYLPQEPQLDPEKTVRENVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 84 GLEALgVGARERRER-------------ALAA--------IDLIGLDGFEN---------------AYPRELSGGMRQRV 127
Cdd:PRK11819 94 GVAEV-KAALDRFNEiyaayaepdadfdALAAeqgelqeiIDAADAWDLDSqleiamdalrcppwdAKVTKLSGGERRRV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 128 GFARALVVDPTILLMDEPFSALDvltAETLrtdlldLWTQG---RMPiKSVLIVTH 180
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLD---AESV------AWLEQflhDYP-GTVVAVTH 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-157 |
2.06e-14 |
|
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: 67.95 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKpltgpaEGVAMVFQTfalfPWLTvlqnveAG 84
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG------EDLLFLPQR----PYLP------LG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 85 L--EALgvgarerreralaaidligldgfenAYP--RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:cd03223 79 TlrEQL-------------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-195 |
2.20e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGlIEPTG---GEVTYLGKPLT------GPAEGVAMVFQTFALFPWLTV 77
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFDGEVCRfkdirdSEALGIVIIHQELALIPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALGVGA---RERRERALAAIDLIGLDgfENayPRELSG----GMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:NF040905 96 AENIFLGNERAKRGVidwNETNRRARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 151 VLTAETLRTDLLDLWTQGrmpIKSVLIvTHNIEEAVFMCDRILVL 195
Cdd:NF040905 172 EEDSAALLDLLLELKAQG---ITSIII-SHKLNEIRRVADSITVL 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-198 |
2.69e-14 |
|
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: 68.42 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIA-----GLIEptgGEVTYLGKPLTGP-AEGVAMVFQTFALFPW 74
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVIT---GEILINGRPLDKNfQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVlqnveaglealgvgaRErreralaAIDLigldgfeNAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 154
Cdd:cd03232 94 LTV---------------RE-------ALRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 155 ETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVF-MCDRILVLSSN 198
Cdd:cd03232 145 YNIVRFLKKLADSGQ----AILCTIHQPSASIFeKFDRLLLLKRG 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-183 |
3.68e-14 |
|
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: 68.51 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 4 LLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAMVFQTFALF-----PWL--- 75
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWLlna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEaglealgVGARERRERALAAIDLIGLDGFENAYPR-----------ELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:cd03290 94 TVEENIT-------FGSPFNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956089794 145 PFSALDV-LTAETLRTDLLDLWTQGRmpiKSVLIVTHNIE 183
Cdd:cd03290 167 PFSALDIhLSDHLMQEGILKFLQDDK---RTLVLVTHKLQ 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
11-204 |
3.70e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLREGEIVGLLGRSGSGKSTLLRIIAGLIePTGGEVTYLGKPLTG-PAEGVAM----------------VFQTFALF- 72
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwSAAELARhraylsqqqtppfampVFQYLTLHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 73 PWLTVLQNVEAGLEALgvgarerreralaaIDLIGLDGFENAYPRELSGGMRQRVGFARA-LVVDPTI------LLMDEP 145
Cdd:PRK03695 95 PDKTRTEAVASALNEV--------------AEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 146 FSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIA 204
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGI----AVVMSSHDLNHTLRHADRVWLLKQ--GKLLA 213
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-203 |
5.96e-14 |
|
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: 69.85 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPwLTVLQN 80
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTqaslrAAIGIVPQDTVLFN-DTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAG-LEAlgvgareRRERALAAIDLIGLDGFENAYPR-----------ELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:COG5265 452 IAYGrPDA-------SEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 149 LDVLT-AETLRTdlLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILVLSSnpGRVI 203
Cdd:COG5265 525 LDSRTeRAIQAA--LREVARGR----TTLVIAHrlsTIVDA----DEILVLEA--GRIV 571
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-213 |
7.73e-14 |
|
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: 67.44 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK-----PLTGPAEGVAMVFQTFALFPWlTVLQN 80
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 veagleaLGVGARERRERALAAIDLIGldGFENaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT----AET 156
Cdd:cd03369 102 -------LDPFDEYSDEEIYGALRVSE--GGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdaliQKT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956089794 157 LRTDLLDlwtqgrmpiKSVLIVTHNIeEAVFMCDRILVLSSnpGRVIAeikvpFKHP 213
Cdd:cd03369 168 IREEFTN---------STILTIAHRL-RTIIDYDKILVMDA--GEVKE-----YDHP 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-201 |
1.14e-13 |
|
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: 69.04 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 13 SLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVT------YlgKP--LTGPAEGvamvfqtfalfpwltvlqNVEag 84
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisY--KPqyISPDYDG------------------TVE-- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 85 lEALGVGARERRERALAAIDLI---GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETL 157
Cdd:COG1245 420 -EFLRSANTDDFGSSYYKTEIIkplGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 158 RTdlldlWTQGRMpiKSVLIVTHNIEEAVFMCDRILVLSSNPGR 201
Cdd:COG1245 499 RR-----FAENRG--KTAMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-199 |
1.28e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 17 GEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGP--AEGVAMVFQTFALFPWLTVLQNVEAgleALGVGARE 94
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrSRFMAYLGHLPGLKADLSTLENLHF---LCGLHGRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 95 RRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvLTAETLRTDLLD--LWTQGrmpi 172
Cdd:PRK13543 114 AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMISahLRGGG---- 188
|
170 180
....*....|....*....|....*..
gi 1956089794 173 kSVLIVTHNIEEAVFMCDRILVLSSNP 199
Cdd:PRK13543 189 -AALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-195 |
2.26e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 9 DANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEGVAM----VF-----QTFALFPWLTVLQ 79
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLarglVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGL-EALGVGARERRERAL-----AAIDlIGLDGFENAYpRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVlt 153
Cdd:PRK15439 361 NVCALThNRRGFWIKPARENAVleryrRALN-IKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV-- 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956089794 154 aeTLRTDLLDLwtqgrmpIKS-------VLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK15439 437 --SARNDIYQL-------IRSiaaqnvaVLFISSDLEEIEQMADRVLVM 476
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-200 |
2.98e-13 |
|
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: 67.89 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 14 LREGEIVGLLGRSGSGKSTLLRIIAGLIEPTggevtyLGKPLTGPA-EGVAMVFQTFALFPWLTVL-----------QNV 81
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPN------LGDYDEEPSwDEVLKRFRGTELQDYFKKLangeikvahkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEALGVGARE------RRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV---L 152
Cdd:COG1245 170 DLIPKVFKGTVREllekvdERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrL 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 153 TAETLRTDLLDlwtqgrmPIKSVLIVTHNIeeAV--FMCDRILVLSSNPG 200
Cdd:COG1245 250 NVARLIRELAE-------EGKYVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-203 |
4.58e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIE----PTGGEVTYLGkplTGPAE-------GVAMVFQTFALFPW 74
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDG---ITPEEikkhyrgDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 75 LTVLQNVEAGLEALGVGAR----ERRERALAAIDLI----GLDGFENA-----YPRELSGGMRQRVGFARALVVDPTILL 141
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRpdgvSREEYAKHIADVYmatyGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 142 MDEPFSALDVLTA-ETLRTdlldLWTQGRMPIKSVLIVTHNIEEAVF-MCDRILVLSSnpGRVI 203
Cdd:TIGR00956 233 WDNATRGLDSATAlEFIRA----LKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYE--GYQI 290
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-180 |
6.24e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLG----KPLTGPAEGVAMVFQTFALFPWLTVLQN 80
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEAlgvgarerRERALAAIDLIGLDGFENA--YP-RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:PRK13540 95 CLYDIHF--------SPGAVGITELCRLFSLEHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|...
gi 1956089794 158 RTDLLDLWTQGrmpiKSVLIVTH 180
Cdd:PRK13540 167 ITKIQEHRAKG----GAVLLTSH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-201 |
8.04e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 14 LREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVT------YlgKP--LTGPAEGvamvfqtfalfpwlTVLQNVEAGL 85
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkisY--KPqyIKPDYDG--------------TVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 EALGvGARERREralaAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRtdl 161
Cdd:PRK13409 426 DDLG-SSYYKSE----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIR--- 497
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956089794 162 ldlwtqgRMPI---KSVLIVTHNIEEAVFMCDRILVLSSNPGR 201
Cdd:PRK13409 498 -------RIAEereATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-163 |
9.71e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.35 E-value: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVtylgkpltGPAEGVAMVFqtFALFPwLTVLQNV 81
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLAKGIKLGY--FAQHQ-LEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEALGVGARERRERALAaiDLIGLDGFE----NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 157
Cdd:PRK10636 392 ESPLQHLARLAPQELEQKLR--DYLGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
....*.
gi 1956089794 158 RTDLLD 163
Cdd:PRK10636 470 TEALID 475
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-205 |
1.93e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG-----PAEGVAMVFQTFALFPWLT 76
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaskeVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEAGL---EALGVGARERRERALA-AIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVl 152
Cdd:PRK10253 98 VQELVARGRyphQPLFTRWRKEDEEAVTkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956089794 153 taeTLRTDLLDLWTQ-GRMPIKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK10253 177 ---SHQIDLLELLSElNREKGYTLAAVLHDLNQACRYASHLIALRE--GKIVAQ 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-195 |
1.98e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLREGEIVGLLGRSGSGKSTLLRIIAGLIePTGGEVTYLGKPLTGPAEG-----VAMVFQTFALFPWlTVLQNVeagl 85
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswrkhLSWVGQNPQLPHG-TLRDNV---- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 eALG-VGARErrERALAAIDLIGLDGFENAYPR-----------ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:PRK11174 444 -LLGnPDASD--EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956089794 154 AETLRTDLLDLWTQgrmpiKSVLIVTHNIEEaVFMCDRILVL 195
Cdd:PRK11174 521 EQLVMQALNAASRR-----QTTLMVTHQLED-LAQWDQIWVM 556
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-206 |
2.86e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 10 ANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLT--GPAEGVA--MVF-----QTFALFPWLTVLQN 80
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIRagIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 veagleaLGVGAR-----------ERRERALAAiDLIGLDGFENAYPRE----LSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:PRK11288 352 -------INISARrhhlragclinNRWEAENAD-RFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 146 FSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAEI 206
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGV----AVLFVSSDLPEVLGVADRIVVMRE--GRIAGEL 478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-203 |
1.00e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP-----LTGPAEGVAMVFQTFALFPWlTVLQN 80
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfgLTDLRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAiDLI-----GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltae 155
Cdd:PLN03232 1330 IDPFSEHNDADLWEALERAHIK-DVIdrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV---- 1404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 156 tlRTDLLDLWTQgRMPIKS--VLIVTHNIeEAVFMCDRILVLSSnpGRVI 203
Cdd:PLN03232 1405 --RTDSLIQRTI-REEFKSctMLVIAHRL-NTIIDCDKILVLSS--GQVL 1448
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-150 |
2.13e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTgpAEGVAMVFQTFALFPWLTVL------ 78
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG--AYGLRELRRQFSMIPQDPVLfdgtvr 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAGLEALG---------VGARERRERALAAIDLIGLDGFENaypreLSGGMRQRVGFARALVV-DPTILLMDEPFSA 148
Cdd:PTZ00243 1402 QNVDPFLEASSaevwaalelVGLRERVASESEGIDSRVLEGGSN-----YSVGQRQLMCMARALLKkGSGFILMDEATAN 1476
|
..
gi 1956089794 149 LD 150
Cdd:PTZ00243 1477 ID 1478
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-195 |
2.51e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.43 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPwLTVLQ 79
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsvlrQGVAMVQQDPVVLA-DTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLEAlgvgARERRERALAAIDLIGL-----DGFENAYPRE---LSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:PRK10790 434 NVTLGRDI----SEEQVWQALETVQLAELarslpDGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 152 LTAETLRTDLLDLWTQgrmpiKSVLIVTH---NIEEAvfmcDRILVL 195
Cdd:PRK10790 510 GTEQAIQQALAAVREH-----TTLVVIAHrlsTIVEA----DTILVL 547
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-200 |
3.44e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 14 LREGEIVGLLGRSGSGKSTLLRIIAGLIEPTggevtyLGKPLTGPA-EGVAMVFQTFALFPWLTVL-----------QNV 81
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPSwDEVLKRFRGTELQNYFKKLyngeikvvhkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 EAGLEALGVGARE------RRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV---L 152
Cdd:PRK13409 170 DLIPKVFKGKVREllkkvdERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrL 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956089794 153 TAETLRTDLldlwTQGrmpiKSVLIVTHNIeeAV--FMCDRILVLSSNPG 200
Cdd:PRK13409 250 NVARLIREL----AEG----KYVLVVEHDL--AVldYLADNVHIAYGEPG 289
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-200 |
3.49e-11 |
|
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: 60.84 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 15 REGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVT-------------------YLGKPLTGPAEgVAMVFQTFALFPwL 75
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnYFTKLLEGDVK-VIVKPQYVDLIP-K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGLEAlgvgaRERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV---L 152
Cdd:cd03236 102 AVKGKVGELLKK-----KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 153 TAETLRTDLLDlwtqgrmPIKSVLIVTHNIEEAVFMCDRILVLSSNPG 200
Cdd:cd03236 177 NAARLIRELAE-------DDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
14-200 |
4.33e-11 |
|
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: 59.51 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 14 LREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYlgkpltgpaEGVAMVFQTfalfpwltvlQNVEaglealgvgar 93
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---------DGITPVYKP----------QYID----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 94 erreralaaidligldgfenaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiK 173
Cdd:cd03222 72 -------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK---K 123
|
170 180
....*....|....*....|....*..
gi 1956089794 174 SVLIVTHNIEEAVFMCDRILVLSSNPG 200
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-209 |
6.81e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKP-----LTGPAEGVAMVFQTFALFPWlTVLQN 80
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfgLMDLRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 VEAGLEALGVGARERRERALAAiDLI-----GLD-----GFENaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PLN03130 1333 LDPFNEHNDADLWESLERAHLK-DVIrrnslGLDaevseAGEN-----FSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956089794 151 VltaetlRTDLLDLWTQgRMPIKS--VLIVTHNIeEAVFMCDRILVLSSnpGRVIaEIKVP 209
Cdd:PLN03130 1407 V------RTDALIQKTI-REEFKSctMLIIAHRL-NTIIDCDRILVLDA--GRVV-EFDTP 1456
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-195 |
6.93e-11 |
|
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: 60.99 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPT-GGEVTYLGKPLT--GPAE----GVAMV---FQTFALFPWLT 76
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirNPAQairaGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 77 VLQNVEagLEALGVGARERRERALAAIDLIGLD----GFENAYP----RELSGGMRQRVGFARALVVDPTILLMDEPFSA 148
Cdd:TIGR02633 356 VGKNIT--LSVLKSFCFKMRIDAAAELQIIGSAiqrlKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 149 LDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEG----VAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-205 |
7.92e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEptG---GEVTYLGKPLT--GPAE----GVAMVFQ---TFALFP 73
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKirNPQQaiaqGIAMVPEdrkRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 WLTVLQNVE-AGLEALGVGARERRERALAAID-LIGLDGFENAYPR----ELSGGMRQRVGFARALVVDPTILLMDEPFS 147
Cdd:PRK13549 355 VMGVGKNITlAALDRFTGGSRIDDAAELKTILeSIQRLKVKTASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 148 ALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRVIAE 205
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQG----VAIIVISSELPEVLGLSDRVLVMHE--GKLKGD 486
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-198 |
8.85e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.87 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEpTGGE-----VTYLGKPLTGPAEGVAMVFQTFALFPWlTVLQN 80
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDiqidgVSWNSVPLQKWRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 V---------EAGLEALGVGARERRERALAAIDLIGLDGfenAYPreLSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:cd03289 97 LdpygkwsdeEIWKVAEEVGLKSVIEQFPGQLDFVLVDG---GCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 152 LTAETLRTDLLDLWTQGrmpikSVLIVTHNIeEAVFMCDRILVLSSN 198
Cdd:cd03289 172 ITYQVIRKTLKQAFADC-----TVILSEHRI-EAMLECQRFLVIEEN 212
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-180 |
1.22e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGliEP----TGGEVTYLGKPLTG--PAE----GVAMVFQTFAL 71
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDlePEErahlGIFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVEAGLEAlgvgarERRERALAAID-------------LIGLD-GFENAYPRE-LSGGMRQRVGFARALVVD 136
Cdd:CHL00131 96 IPGVSNADFLRLAYNS------KRKFQGLPELDplefleiineklkLVGMDpSFLSRNVNEgFSGGEKKRNEILQMALLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 137 PTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTH 180
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSE----NSIILITH 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-196 |
1.27e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.34 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKpltgpaegVAMVFQTfalfPWL---TV 77
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ----AWIqndSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGlEALGVGARERRERALAAI-DLIGLDGFENAYPRE----LSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:TIGR00957 716 RENILFG-KALNEKYYQQVLEACALLpDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956089794 153 TAETLRTDLLDlwTQGRMPIKSVLIVTHNIeEAVFMCDRILVLS 196
Cdd:TIGR00957 795 VGKHIFEHVIG--PEGVLKNKTRILVTHGI-SYLPQVDVIIVMS 835
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
63-201 |
1.78e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 63 AMVFQTFALFPwLTVLQNVEAGLEAlgvGARERRERA--LAAIDLIgLDGFENAYP-------RELSGGMRQRVGFARAL 133
Cdd:PTZ00265 1299 SIVSQEPMLFN-MSIYENIKFGKED---ATREDVKRAckFAAIDEF-IESLPNKYDtnvgpygKSLSGGQKQRIAIARAL 1373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956089794 134 VVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIeEAVFMCDRILVLsSNPGR 201
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD---KTIITIAHRI-ASIKRSDKIVVF-NNPDR 1436
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-209 |
2.76e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGkpLTGPAEGVAMVFQTFALFPWLTVL--QNVE 82
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIGLHDLRFKITIIPQDPVLfsGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 AGLEALGvgaRERRERALAAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:TIGR00957 1378 MNLDPFS---QYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 152 ----LTAETLRTDLLDLwtqgrmpikSVLIVTHNIeEAVFMCDRILVLSSNpgrVIAEIKVP 209
Cdd:TIGR00957 1455 etdnLIQSTIRTQFEDC---------TVLTIAHRL-NTIMDYTRVIVLDKG---EVAEFGAP 1503
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
17-181 |
4.42e-10 |
|
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: 56.23 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 17 GEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKpltgpaegvamvfqtfalfpwltvlqnveaglealgvgarerr 96
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 97 ERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPIKSVL 176
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
|
....*
gi 1956089794 177 IVTHN 181
Cdd:smart00382 119 VILTT 123
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-198 |
4.46e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEpTGGE-----VTYLGKPLTGPAEGVAMVFQTFALFPWlTVLQN 80
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEiqidgVSWNSVTLQTWRKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 81 V---------EAGLEALGVGARERRERALAAIDLIGLDGfenAYPreLSGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:TIGR01271 1312 LdpyeqwsdeEIWKVAEEVGLKSVIEQFPDKLDFVLVDG---GYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956089794 152 LTAETLRTDLLDLWTQGrmpikSVLIVTHNIeEAVFMCDRILVLSSN 198
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNC-----TVILSEHRV-EALLECQQFLVIEGS 1427
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-151 |
1.09e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKpltgpaEGVAMVFQ-TFALFpwLTVLQ 79
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN------WQLAWVNQeTPALP--QPALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAG------LEALGVGARERRE-------------------RALAAIDLIGLdGFEN---AYP-RELSGGMRQRVGFA 130
Cdd:PRK10636 83 YVIDGdreyrqLEAQLHDANERNDghaiatihgkldaidawtiRSRAASLLHGL-GFSNeqlERPvSDFSGGWRMRLNLA 161
|
170 180
....*....|....*....|.
gi 1956089794 131 RALVVDPTILLMDEPFSALDV 151
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDL 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-180 |
1.47e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVtYLGKPLTgpaegVAMVFQTFA-LFPWLTVLQNVEAGL 85
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLE-----VAYFDQHRAeLDPEKTVMDNLAEGK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 86 EALGVGARERR------------ERALAAIdligldgfenaypRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 153
Cdd:PRK11147 409 QEVMVNGRPRHvlgylqdflfhpKRAMTPV-------------KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
170 180
....*....|....*....|....*..
gi 1956089794 154 AETLRtDLLDLWtQGrmpikSVLIVTH 180
Cdd:PRK11147 476 LELLE-ELLDSY-QG-----TVLLVSH 495
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-202 |
1.59e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK------PLTGPAEGVAMVFQ---TFALFPWLTV 77
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnANEAINHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 -----LQNVEAGLEALGVGARERRERALAAIdligLDGFENAYPRE------LSGGMRQRVGFARALVVDPTILLMDEPF 146
Cdd:PRK10982 344 gfnslISNIRNYKNKVGLLDNSRMKSDTQWV----IDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 147 SALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSnpGRV 202
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKKD----KGIIIISSEMPELLGITDRILVMSN--GLV 469
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-180 |
1.69e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGL--IEPTGGEVTYLGKPLTG------PAEGVAMVFQTFALFPWLTV 77
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLElspedrAGEGIFMAFQYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 78 LQNVEAGLEALgvgareRRERALAAIDLIGLDGFENA------YPREL---------SGGMRQRVGFARALVVDPTILLM 142
Cdd:PRK09580 96 QFFLQTALNAV------RSYRGQEPLDRFDFQDLMEEkiallkMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956089794 143 DEPFSALDVltaetlrtDLLDLWTQG----RMPIKSVLIVTH 180
Cdd:PRK09580 170 DESDSGLDI--------DALKIVADGvnslRDGKRSFIIVTH 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-196 |
2.07e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPT-GGEVTYLGKpltgpaegVAMVFQTfalfPWL---TVLQNVE 82
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGS--------VAYVPQV----SWIfnaTVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 aglealgVGARERRERALAAIDLIGLDGFENAYP-REL----------SGGMRQRVGFARALVVDPTILLMDEPFSALDV 151
Cdd:PLN03232 701 -------FGSDFESERYWRAIDVTALQHDLDLLPgRDLteigergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956089794 152 LTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMcDRILVLS 196
Cdd:PLN03232 774 HVAHQVFDSCMKDELKG----KTRVLVTNQLHFLPLM-DRIILVS 813
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-195 |
2.32e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.96 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP----TGGEVTYLGKPL--TGPAE-------GVAMVFQ 67
Cdd:PRK15093 17 DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLlrLSPRErrklvghNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 68 --TFALFPWLTV----LQNVEA----GLEALGVGARERReralaAIDLIGLDGFEN------AYPRELSGGMRQRVGFAR 131
Cdd:PRK15093 97 epQSCLDPSERVgrqlMQNIPGwtykGRWWQRFGWRKRR-----AIELLHRVGIKDhkdamrSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 132 ALVVDPTILLMDEPFSALDVLT-AETLRtdLLDLWTQGRMpiKSVLIVTHNIEEAVFMCDRILVL 195
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTqAQIFR--LLTRLNQNNN--TTILLISHDLQMLSQWADKINVL 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-144 |
2.36e-09 |
|
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: 56.34 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTgpAEGVA-------MVFQTFALFPwltvlqnvea 83
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--ADNREayrqlfsAVFSDFHLFD---------- 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 84 glEALGVGARERRERALAAIDLIGLDG---FENAY--PRELSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:COG4615 420 --RLLGLDGEADPARARELLERLELDHkvsVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-144 |
2.85e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTGPAEG-----VAMVFQTFALFPWLTVLQN----- 80
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyrklFSAVFTDFHLFDQLLGPEGkpanp 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956089794 81 --VEAGLEALGVGarerreralaaiDLIGLDGFENAYPReLSGGMRQRVGFARALVVDPTILLMDE 144
Cdd:PRK10522 423 alVEKWLERLKMA------------HKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-202 |
3.13e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTylgkpltgPAEGVAMVFQTfalfPWL---TVLQNV- 81
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------AERSIAYVPQQ----AWImnaTVRGNIl 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 82 -------------------EAGLEALGVGARERreralaaidlIGLDGFEnaypreLSGGMRQRVGFARALVVDPTILLM 142
Cdd:PTZ00243 743 ffdeedaarladavrvsqlEADLAQLGGGLETE----------IGEKGVN------LSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 143 DEPFSALDVLTAETLRTDLLdlwtQGRMPIKSVLIVTHNIeEAVFMCDRILVLSSnpGRV 202
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECF----LGALAGKTRVLATHQV-HVVPRADYVVALGD--GRV 859
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-150 |
5.16e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEP-TGGEVTYLGKpltgpaegVAMVFQTFALFPwLTVLQ 79
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT--------VAYVPQVSWIFN-ATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLE--------ALGVGARERRERALAAIDL--IGLDGFEnaypreLSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:PLN03130 698 NILFGSPfdperyerAIDVTALQHDLDLLPGGDLteIGERGVN------ISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
.
gi 1956089794 150 D 150
Cdd:PLN03130 772 D 772
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-208 |
1.35e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSG--KSTLLRIIAGliePTGGEVTYlgKPLTGPAEGVAMVFQTFALFPWLTVLQ 79
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANRRALRRTIG*HRPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 80 NVEAGLE-------ALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:NF000106 99 ESFSGREnlymigr*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956089794 153 TAEtlrtdllDLWTQGRMPIK---SVLIVTHNIEEAVFMCDRILVLssNPGRVIAEIKV 208
Cdd:NF000106 179 TRN-------EVWDEVRSMVRdgaTVLLTTQYMEEAEQLAHELTVI--DRGRVIADGKV 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-181 |
1.38e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 20 VGLLGRSGSGKSTLLRIIAGLIEPTGGEVtylgkpLTGPAEGVAMVFQ------TFALFPWLTVLQNVEaglealgvGAR 93
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVRMAVFSQhhvdglDLSSNPLLYMMRCFP--------GVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 94 ERRERA-LAAIDLIGLDGFENAYprELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGrmpi 172
Cdd:PLN03073 604 EQKLRAhLGSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--QG---- 675
|
....*....
gi 1956089794 173 kSVLIVTHN 181
Cdd:PLN03073 676 -GVLMVSHD 683
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
6-150 |
1.60e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTY-------LGKPLTGpaegvaMVFQTFALFPWLTVL 78
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYkncninnIAKPYCT------YIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 79 QNVEAGLEALgvgarERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PRK13541 89 ENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-207 |
1.68e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGKPLTG--PAEGVAMVFQTFALFPWLTVL- 78
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyAQDHAYDFENDLTLFDWMSQWr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 ------QNVEAgleALGvgarerreRALAAIDLIgldgfeNAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVL 152
Cdd:PRK15064 410 qegddeQAVRG---TLG--------RLLFSQDDI------KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 153 TAETLRTDLLDLwtQGrmpikSVLIVTHnieeavfmcDRILVlSSNPGRVIaEIK 207
Cdd:PRK15064 473 SIESLNMALEKY--EG-----TLIFVSH---------DREFV-SSLATRII-EIT 509
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-153 |
2.23e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 11 NLSLR--EGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYlgkpltGPAEGVAMVFQ-TFAlFPWLTVLQNVEAGLEA 87
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL------DPNERLGKLRQdQFA-FEEFTVLDTVIMGHTE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 88 LGVGARER----------RERALAAIDLIG----LDGFeNAYPR--EL-----------SGGMRQ-------RVGFARAL 133
Cdd:PRK15064 92 LWEVKQERdriyalpemsEEDGMKVADLEVkfaeMDGY-TAEARagELllgvgipeeqhYGLMSEvapgwklRVLLAQAL 170
|
170 180
....*....|....*....|
gi 1956089794 134 VVDPTILLMDEPFSALDVLT 153
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINT 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-180 |
7.17e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIA-----GLI----------EPTGGEVTYLGKPLTGPAEGVAMVFQTFA 70
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPkncqilhveqEVVGDDTTALQCVLNTDIERTQLLEEEAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 71 L--------FPWLTVLQNVE--AGLEALGVGAR-ERRERALAAID-----------LIGLD---GFENAYPRELSGGMRQ 125
Cdd:PLN03073 272 LvaqqreleFETETGKGKGAnkDGVDKDAVSQRlEEIYKRLELIDaytaearaasiLAGLSftpEMQVKATKTFSGGWRM 351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956089794 126 RVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDlWTqgrmpiKSVLIVTH 180
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WP------KTFIVVSH 399
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-150 |
3.22e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTYLGK------PLTGPAEGVAMVFQTFALFP------ 73
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdiNLKWWRSKIGVVSQDPLLFSnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 74 ---WLTVLQNVEAGLEALGVGARERRE--------RALAAIDL---------------------------------IGLD 109
Cdd:PTZ00265 480 ikySLYSLKDLEALSNYYNEDGNDSQEnknkrnscRAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkVLIH 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956089794 110 GFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALD 150
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-197 |
5.49e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 48.75 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTL-------LRIIAGLIEPTGGEVTYLgkPLTGPAEGVAMVFQTFALFPWlTVL 78
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKL--PLHTLRSRLSIILQDPILFSG-SIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 79 QNVEAG--------LEALGVGARERRERAL-AAIDLIGLDGFENaypreLSGGMRQRVGFARALVVDPTILLMDEPFSAL 149
Cdd:cd03288 113 FNLDPEckctddrlWEALEIAQLKNMVKSLpGGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956089794 150 DVLTAETLRTDLLDLWTQgrmpiKSVLIVTHNIeEAVFMCDRILVLSS 197
Cdd:cd03288 188 DMATENILQKVVMTAFAD-----RTVVTIAHRV-STILDADLVLVLSR 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-206 |
7.27e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 6 VLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGL-----IeptGGEVTYLGKPLTGP------AEGVAMVFQ---TFAL 71
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnI---SGTVFKDGKEVDVStvsdaiDAGLAYVTEdrkGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNVE-AGLEAL---GVgARERRERALAaidligldgfeNAYPRE--------------LSGGMRQRVGFARAL 133
Cdd:NF040905 352 NLIDDIKRNITlANLGKVsrrGV-IDENEEIKVA-----------EEYRKKmniktpsvfqkvgnLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956089794 134 VVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLssNPGRVIAEI 206
Cdd:NF040905 420 FTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEG----KGVIVISSELPELLGMCDRIYVM--NEGRITGEL 486
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4-154 |
1.03e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 4 LLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGliEPTGG----EVTYLGKP--------LTGPAEgvamvfQTFAL 71
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyiegDIRISGFPkkqetfarISGYCE------QNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 72 FPWLTVLQNV--EAGLE-ALGVGARERRERALAAIDLIGLDGFENA---YP--RELSGGMRQRVGFARALVVDPTILLMD 143
Cdd:PLN03140 965 SPQVTVRESLiySAFLRlPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170
....*....|.
gi 1956089794 144 EPFSALDVLTA 154
Cdd:PLN03140 1045 EPTSGLDARAA 1055
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-154 |
2.00e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 2 GELLVLDDANLSLREGEIVGLLGRSGSGKSTLL-----RIIAGLIepTGGEVTYLGKPL-TGPAEGVAMVFQTFALFPWL 75
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGRPLdSSFQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVlqnveagLEALGVGARERRERAL----------AAIDLIGLDGFENAY---PRE-LSGGMRQRVGFARALVVDPTILL 141
Cdd:TIGR00956 852 TV-------RESLRFSAYLRQPKSVsksekmeyveEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLL 924
|
170
....*....|....
gi 1956089794 142 -MDEPFSALDVLTA 154
Cdd:TIGR00956 925 fLDEPTSGLDSQTA 938
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
96-185 |
2.57e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 96 RERALAA--IDLIGLDGFENAYP-RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpi 172
Cdd:PRK10938 376 RQQKLAQqwLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGE--- 452
|
90
....*....|...
gi 1956089794 173 KSVLIVTHNIEEA 185
Cdd:PRK10938 453 TQLLFVSHHAEDA 465
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-153 |
5.47e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 1 QGELLVLDDANLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPT---GGEVTYLGKPLTG--PAEGVAMVFQTFALFPWL 75
Cdd:PLN03140 175 KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEfvPRKTSAYISQNDVHVGVM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 76 TVLQNVEAGLEALGVGAR-------ERRE---------------RALAA------------IDLIGLDGFENA-----YP 116
Cdd:PLN03140 255 TVKETLDFSARCQGVGTRydllselARREkdagifpeaevdlfmKATAMegvksslitdytLKILGLDICKDTivgdeMI 334
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956089794 117 RELSGGMRQRVGFARaLVVDPT-ILLMDEPFSALDVLT 153
Cdd:PLN03140 335 RGISGGQKKRVTTGE-MIVGPTkTLFMDEISTGLDSST 371
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
7-206 |
2.83e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 7 LDDANLSLREGEIVGLLGRSGSGKSTLLR-IIAgliepTGGEVTYLGKPLTGPAEGVAMVFQtfalfpwltvLQN-VEAG 84
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLY-----ASGKARLISFLPKFSRNKLIFIDQ----------LQFlIDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 85 LEALGVGarerreRALAAidligldgfenaypreLSGGMRQRVGFARALVVDP--TILLMDEPFSALDVLTAETLRTDLL 162
Cdd:cd03238 76 LGYLTLG------QKLST----------------LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956089794 163 DLWTQGrmpiKSVLIVTHNIEeavFMC--DRILVLSSNPGRVIAEI 206
Cdd:cd03238 134 GLIDLG----NTVILIEHNLD---VLSsaDWIIDFGPGSGKSGGKV 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-179 |
1.75e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 5 LVLDDanLSLREGEIVGLLGRSGSGKSTLLRIIAGLIEPTGGEVTylgkpltgpaegvaMVFQTFALFPWLTVLQNVE-- 82
Cdd:PRK10938 19 LQLPS--LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ--------------SQFSHITRLSFEQLQKLVSde 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 83 ----------AGLEALGVGARE-------RRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEP 145
Cdd:PRK10938 83 wqrnntdmlsPGEDDTGRTTAEiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190
....*....|....*....|....*....|....
gi 1956089794 146 FSALDVLTAETLRTDLLDLWTQGrmpIKSVLIVT 179
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSG---ITLVLVLN 193
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-200 |
4.64e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956089794 119 LSGGMRQRVGFARAL---VVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIeEAVFMCDRILVL 195
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH----TVVIIEHNM-HVVKVADYVLEL 884
|
....*
gi 1956089794 196 SSNPG 200
Cdd:PRK00635 885 GPEGG 889
|
|
| |
