|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-249 |
5.09e-142 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 398.31 E-value: 5.09e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVT-PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGV 79
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 160 PFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPGRIATRIEVPIERPRSLDLITGEVFNGL 239
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPEFAAL 244
|
250
....*....|
gi 565781182 240 KREILKQMRH 249
Cdd:COG1116 245 RAEILDLLRE 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-222 |
2.53e-124 |
|
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: 351.77 E-value: 2.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQ 82
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 163 ALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPGRIATRIEVPI 222
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
6.71e-111 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 319.50 E-value: 6.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPG-VTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGV 79
Cdd:COG4525 1 MSMLTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 160 PFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPGRIATRIEVPIER 224
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSR 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
3.39e-90 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 270.05 E-value: 3.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER--- 77
Cdd:COG3842 3 MPALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRIE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-215 |
2.61e-86 |
|
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: 255.52 E-value: 2.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---GVV 80
Cdd:cd03259 1 LELKGLSKTYGSV---RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 161 FGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRIV 210
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-226 |
9.81e-84 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 250.04 E-value: 9.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVH-ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQ 82
Cdd:NF040729 2 LKIQNISKTFINNKKENeVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:NF040729 82 NYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 163 ALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPGRIATRIEVPIERPR 226
Cdd:NF040729 162 AVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPR 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-224 |
1.12e-81 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 244.99 E-value: 1.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQE 83
Cdd:PRK11248 2 LQISHLYADYGG-KP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 AALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGA 163
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 164 LDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPGRIATRIEVPIER 224
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFAR 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-228 |
3.39e-79 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 241.97 E-value: 3.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MShISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV--ARPGPERG 78
Cdd:COG1118 1 MS-IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 V--VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:COG1118 77 VgfVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA---TRIEVpIERPRSL 228
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRIEqvgTPDEV-YDRPATP 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-228 |
7.59e-78 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 238.82 E-value: 7.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-ERGV 79
Cdd:COG3839 1 MASLELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPkDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 --VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:COG3839 78 amVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI---ATRIEVpIERPRSL 228
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRIqqvGTPEEL-YDRPANL 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-223 |
1.95e-77 |
|
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: 233.67 E-value: 1.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPERGV--V 80
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRPVntV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 161 FGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIaTRIEVPIE 223
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK--GKI-QQIGTPEE 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-244 |
3.59e-75 |
|
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: 227.73 E-value: 3.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQEAALFPWLNVWENVVFGPK 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 102 --IAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSV 179
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 180 WQTLRTTVVFVTHDIDEAILLADTIYVMSARPG-RIATRIEVPIERPRS-LDLITGEVFNGLKREIL 244
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDrLEVVEDPSYYDLRNEAL 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-214 |
2.37e-74 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 225.31 E-value: 2.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER---- 77
Cdd:COG1136 5 LELRNLTKSYGtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ----GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG1136 85 rrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDiDEAILLADTIYVMsaRPGRI 214
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL--RDGRI 222
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-215 |
1.76e-72 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 223.43 E-value: 1.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:COG1125 2 IEFENVTKRYPDGTV--AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrrriG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGL--SAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIV 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-214 |
5.78e-72 |
|
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: 218.90 E-value: 5.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ----GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAiLLADTIYVMsaRPGRI 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIEL--RDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-215 |
2.77e-69 |
|
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: 213.32 E-value: 2.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:cd03295 1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGL--SAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEIV 215
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-227 |
1.47e-64 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 204.89 E-value: 1.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER--- 77
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFT---ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKrdy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI---ATRIEVpIERPRS 227
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNH--GVIeqvGTPQEI-YRHPAT 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-214 |
5.56e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.52 E-value: 5.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE-R---GV 79
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRrriGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 160 PFGALDAQTRLTMQELLLSvwqtLR---TTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG1131 158 PTSGLDPEARRELWELLRE----LAaegKTVLLSTHYLEEAERLCDRVAIIDK--GRI 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-228 |
8.50e-63 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 200.94 E-value: 8.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE-RGV--V 80
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnRHVntV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 161 FGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIA---TRIEVpIERPRSL 228
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEqdgTPREI-YEEPKNL 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-209 |
9.99e-63 |
|
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: 194.33 E-value: 9.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:cd03229 1 LELKNVSKRYGQKT---VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVFQEAALFPWLNVWENVVFGpkiaglsrreyaaraeemleitglsafkrhlpvqLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:cd03229 78 iGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-214 |
2.12e-62 |
|
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: 194.40 E-value: 2.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-ERGV--V 80
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRDIamV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 161 FGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND--GQI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-215 |
2.45e-62 |
|
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: 194.86 E-value: 2.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:COG1122 1 IELENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQ--EAALF-PwlNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:COG1122 79 LVFQnpDDQLFaP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 156 LMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD--GRIV 213
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-214 |
2.98e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 199.94 E-value: 2.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---------GVVFQEAALFPWLN 91
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFALLPHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLT 171
Cdd:COG4175 122 VLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRRE 201
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 172 MQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:COG4175 202 MQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRI 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-214 |
3.56e-62 |
|
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: 194.87 E-value: 3.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MShISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-ERGV 79
Cdd:cd03296 1 MS-IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 --VFQEAALFPWLNVWENVVFGPKIAGLSRR----EYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:cd03296 77 gfVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK--GRI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-214 |
3.69e-62 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 202.83 E-value: 3.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP--GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---- 77
Cdd:COG1123 261 LEVRNLSKRYPvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ----GVVFQ--EAALFPWLNVWENVVFGPKIAG-LSRREYAARAEEMLEITGLSA-FKRHLPVQLSGGMRQRVGIARVLT 149
Cdd:COG1123 341 rrrvQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 150 LGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRI 483
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-214 |
1.20e-61 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 194.40 E-value: 1.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---------GVVFQEAALFPWLN 91
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLT 171
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 172 MQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRL 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-208 |
1.21e-59 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 187.29 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 5 SVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GV 79
Cdd:cd03225 1 ELKNLSFSYPD-GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:cd03225 80 VFQnpDDQFFG-PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTlRTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-214 |
3.69e-59 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 187.31 E-value: 3.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---GVV 80
Cdd:TIGR00968 1 IEIANISKRFGSFQ---ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:TIGR00968 78 FQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 161 FGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN--GKI 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-214 |
2.46e-58 |
|
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: 185.18 E-value: 2.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYpGVTPVHalDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:COG1127 6 IEVRNLTKSF-GDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFGPKI-AGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRV 154
Cdd:COG1127 83 riGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD--GKI 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-228 |
2.12e-57 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 183.34 E-value: 2.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 9 LSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQEAALFP 88
Cdd:PRK11247 18 VSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 WLNVWENVVFGpkiaglSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQT 168
Cdd:PRK11247 95 WKKVIDNVGLG------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 169 RLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTiyVMSARPGRIATRIEVPIERPRSL 228
Cdd:PRK11247 169 RIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADR--VLLIEEGKIGLDLTVDLPRPRRR 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-228 |
3.72e-57 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 185.82 E-value: 3.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-ERGV 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 --VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEE---MLEITGLSAFKrhlPVQLSGGMRQRVGIARVLTLGSRV 154
Cdd:PRK11650 79 amVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSA-RPGRIATRIEVpIERPRSL 228
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGgVAEQIGTPVEV-YEKPAST 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-215 |
1.15e-54 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 175.33 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 24 QIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-ERGV--VFQEAALFPWLNVWENVVFG- 99
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaERPVsmLFQENNLFPHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 100 -PKIAgLSRREyAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLS 178
Cdd:COG3840 97 rPGLK-LTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 565781182 179 VWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARIADRVLLVAD--GRIA 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-215 |
2.13e-54 |
|
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: 177.69 E-value: 2.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 37 LLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAAR 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 114 AEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|..
gi 565781182 194 IDEAILLADTIYVMsaRPGRIA 215
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIA 180
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
21-209 |
2.85e-54 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 178.51 E-value: 2.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---------GVVFQEAALFPWLN 91
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrkkiGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLT 171
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 565781182 172 MQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKA 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-215 |
4.38e-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: 173.25 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 24 QIDLQVaEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG-------GAVARPGPER--GVVFQEAALFPWLNVWE 94
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQRkiGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 95 NVVFGPKiaGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQE 174
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 565781182 175 LLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRLQ 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-215 |
4.83e-54 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 177.91 E-value: 4.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPERGV 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDV---VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 --VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:PRK11000 78 gmVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVA 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-208 |
5.01e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 177.58 E-value: 5.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MShISVTQLSKTYpGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER-- 77
Cdd:PRK10851 1 MS-IEIANIKKSF-GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDRkv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPWLNVWENVVFGPKIagLSRREYAARAE------EMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLG 151
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTV--LPRRERPNAAAikakvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 152 SRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-214 |
8.96e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.42 E-value: 8.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER--- 77
Cdd:COG1135 1 MIELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ----GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG1135 81 rrkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 154 VLLMDEPFGALDAQTrlTMQ--ELLLSVWQTLRTTVVFVTHDID--EAIllADTIYVMSArpGRI 214
Cdd:COG1135 161 VLLCDEATSALDPET--TRSilDLLKDINRELGLTIVLITHEMDvvRRI--CDRVAVLEN--GRI 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-214 |
6.14e-53 |
|
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: 171.22 E-value: 6.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVT-PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER---- 77
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ---GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRV 154
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK--GEV 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-208 |
1.26e-52 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 174.64 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---GVV 80
Cdd:PRK11607 20 LEIRNLTKSFDGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpiNMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 565781182 161 FGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-214 |
1.36e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 170.17 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:COG1126 2 IEIENLHKSFGDL---EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVFQEAALFPWLNVWENVVFGP-KIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:COG1126 79 vGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 156 LMDEPFGALDAqtrltmqEL---LLSVWQTLR---TTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG1126 159 LFDEPTSALDP-------ELvgeVLDVMRDLAkegMTMVVVTHEMGFAREVADRVVFMDG--GRI 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-195 |
1.46e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 169.85 E-value: 1.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:COG2884 2 IRFENVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:COG2884 80 riGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 565781182 156 LMDEPFGALDAQTRLTMQELLLSVwQTLRTTVVFVTHDID 195
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE 198
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-214 |
1.45e-51 |
|
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: 167.68 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYpGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:cd03261 1 IELRGLTKSF-GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFGPKIAG-LSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRV 154
Cdd:cd03261 78 rmGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSarPGRI 214
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLY--DGKI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-229 |
3.12e-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: 174.32 E-value: 3.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSG---GELRVGGGAVARP-----GP 75
Cdd:COG1123 5 LEVRDLSVRYPG-GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELsealrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 76 ERGVVFQE--AALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIATR--IEVPIERPRSLD 229
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVEDgpPEEILAAPQALA 238
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-207 |
4.08e-51 |
|
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: 166.57 E-value: 4.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----GV 79
Cdd:COG4555 2 IEVENLSKKYGKV---PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqiGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 565781182 160 PFGALDAQTRLTMQELLLSvWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:COG4555 159 PTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-193 |
5.99e-51 |
|
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: 166.07 E-value: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG--------GAVARPG 74
Cdd:COG4181 9 IELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldeDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 PER-GVVFQEAALFPWLNVWENVVFGPKIAGlsRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG4181 89 ARHvGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHD 193
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-214 |
6.05e-51 |
|
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: 165.76 E-value: 6.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:cd03257 2 LEVKNLSVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ---GVVFQEA--ALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGL---SAFKRHLPVQLSGGMRQRVGIARVLT 149
Cdd:cd03257 82 keiQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 150 LGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKI 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-207 |
6.71e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 169.51 E-value: 6.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA-RPGPERGV--VFQEAALFPWLNVWENVVF 98
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThRSIQQRDIcmVFQSYALFPHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 GPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLS 178
Cdd:PRK11432 102 GLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
170 180
....*....|....*....|....*....
gi 565781182 179 VWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK11432 182 LQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-214 |
2.81e-50 |
|
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: 162.18 E-value: 2.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----GV 79
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENvvfgpkiaglsrreyaaraeemleitglsafkrhlpVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:cd03230 78 LPEEPSLYENLTVREN------------------------------------LKLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 160 PFGALDAQTRLTMQELLLSvwqtLR---TTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRE----LKkegKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-220 |
4.24e-50 |
|
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: 164.21 E-value: 4.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:COG1124 2 LEVRNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQ--EAALFPWLNVWEnVVFGP-KIAGLSRREyaARAEEMLEITGL-SAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDR-ILAEPlRIHGLPDRE--ERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIATRIEV 220
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTV 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-214 |
5.62e-50 |
|
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: 163.66 E-value: 5.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---GVVFQEAALFPWLNVWENVVF 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 GPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLS 178
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 565781182 179 VWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKL 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-215 |
6.98e-50 |
|
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: 166.81 E-value: 6.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 24 QIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG-------GAVARPgPER---GVVFQEAALFPWLNVW 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIFLP-PHRrriGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 94 ENVVFGPKIAGLSRREYA-ARAEEMLEITGLsaFKRHlPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTM 172
Cdd:COG4148 96 GNLLYGRKRAPRAERRISfDEVVELLGIGHL--LDRR-PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 173 QELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ--GRVV 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-215 |
4.39e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 162.62 E-value: 4.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTP--VHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---- 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ----GVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLS-AFKRHLPVQLSGGMRQRVGIARVLTL 150
Cdd:TIGR04521 81 rkkvGLVFQfpEHQLFE-ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 151 GSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK--GKIV 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-214 |
4.81e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 161.38 E-value: 4.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:COG3638 3 LELRNLSKRYPGGTP--ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFG--------PKIAGLSRREYAARAEEMLEITGLS--AFKRhlpV-QLSGGMRQRVGI 144
Cdd:COG3638 81 riGMIFQQFNLVPRLSVLTNVLAGrlgrtstwRSLLGLFPPEDRERALEALERVGLAdkAYQR---AdQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 145 ARVLTLGSRVLLMDEPFGALDAQT-RLTMqELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTaRQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD--GRV 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-214 |
6.11e-49 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 160.00 E-value: 6.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYpgvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE----R-- 77
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVFQEAALFPWLNVWENVVFGP-KIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:cd03262 78 vGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 156 LMDEPFGALDAqtrltmqELLLSVWQTLR------TTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03262 158 LFDEPTSALDP-------ELVGEVLDVMKdlaeegMTMVVVTHEMGFAREVADRVIFMDD--GRI 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
1.14e-47 |
|
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: 158.28 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-----ERG 78
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFG-----PKIAGLSRREYAArAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGryphlGLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRIV 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-215 |
1.72e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 157.56 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 10 SKTYpGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-------ERGVVFQ 82
Cdd:PRK09493 8 SKHF-GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderlirqEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWLNVWENVVFGP-KIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:PRK09493 85 QFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 162 GALDAQTRltmQElLLSVWQTLRT---TVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:PRK09493 165 SALDPELR---HE-VLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDK--GRIA 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-214 |
4.48e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 155.80 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYpgvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGF-----EAPSGGELRVGGGAVARPGPER- 77
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ------GVVFQEAALFPwLNVWENVVFGPKIAG-LSRREYAARAEEMLEITGLSA-FKRHL-PVQLSGGMRQRVGIARVL 148
Cdd:cd03260 78 elrrrvGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDeVKDRLhALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 149 TLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQtlRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLN--GRL 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
5.63e-47 |
|
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: 156.35 E-value: 5.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER--- 77
Cdd:COG0411 2 DPLLEVRGLTKRFGGLV---AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVV--FQEAALFPWLNVWENV---------------VFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMR 139
Cdd:COG0411 79 lGIArtFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 140 QRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDeAIL-LADTIYVMSArpGRI 214
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD-LVMgLADRIVVLDF--GRV 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-197 |
8.24e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 154.56 E-value: 8.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAP---SGGELRVGGGAVARPGPER---GVVFQEAALFPWLNVWEN 95
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQrriGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 VVFG-PkiAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQE 174
Cdd:COG4136 97 LAFAlP--PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|....*.
gi 565781182 175 LllsVWQTLRTT---VVFVTHDIDEA 197
Cdd:COG4136 175 F---VFEQIRQRgipALLVTHDEEDA 197
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-193 |
9.07e-46 |
|
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: 152.18 E-value: 9.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR------PGPER 77
Cdd:cd03292 1 IEFINVTKTYPNGTA--ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraiPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:cd03292 79 kiGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 565781182 156 LMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVFVTHD 193
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-215 |
2.04e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 151.66 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 26 DLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVV---FQEAALFPWLNVWENVVFG--P 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVsmlFQENNLFSHLTVAQNIGLGlnP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 101 --KIAGLSRREYAARAEEMleitGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLS 178
Cdd:PRK10771 99 glKLNAAQREKLHAIARQM----GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 565781182 179 VWQTLRTTVVFVTHDIDEAILLAD-TIYVMSarpGRIA 215
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPrSLVVAD---GRIA 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-209 |
2.28e-45 |
|
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: 151.12 E-value: 2.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARP----GPERGV 79
Cdd:cd03263 1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDrkaaRQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 565781182 160 PFGALDAQTRLTMQELLLSVwQTLRtTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEV-RKGR-SIILTTHSMDEAEALCDRIAIMSD 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-214 |
2.55e-45 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 151.44 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGV 79
Cdd:cd03219 1 LEVRGLTKRFGGL---VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiaRLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 V--FQEAALFPWLNVWENVV----------FGPKIAGLSRREYAARAEEMLEITGLSAfKRHLPV-QLSGGMRQRVGIAR 146
Cdd:cd03219 78 GrtFQIPRLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLAD-LADRPAgELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 147 VLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQtLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQ--GRV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-207 |
3.64e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQE 83
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 AAL---FPwLNVWENVVFG--PKIAGLSR--REYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:COG1121 84 AEVdwdFP-ITVRDVVLMGryGRRGLFRRpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSvWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-193 |
5.40e-45 |
|
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: 150.09 E-value: 5.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 8 QLSKTYPGvtPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR------PGPER--GV 79
Cdd:TIGR02673 6 NVSKAYPG--GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqlPLLRRriGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:TIGR02673 84 VFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190
....*....|....*....|....*....|....
gi 565781182 160 PFGALDAQTRLTMQELLLSVWQtLRTTVVFVTHD 193
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNK-RGTTVIVATHD 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-217 |
7.85e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.72 E-value: 7.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGV 79
Cdd:COG1129 5 LEMRGISKSFGGV---KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaqAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 --VFQEAALFPWLNVWENVVFG--PKIAGL-SRREYAARAEEMLEITGLsafkrHLPV-----QLSGGMRQRVGIARVLT 149
Cdd:COG1129 82 aiIHQELNLVPNLSVAENIFLGrePRRGGLiDWRAMRRRARELLARLGL-----DIDPdtpvgDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 150 LGSRVLLMDEPFGALDAQTRltmqELLLSVWQTLR---TTVVFVTHDIDEAILLADTIYVMsaRPGR-IATR 217
Cdd:COG1129 157 RDARVLILDEPTASLTEREV----ERLFRIIRRLKaqgVAIIYISHRLDEVFEIADRVTVL--RDGRlVGTG 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-215 |
8.16e-45 |
|
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: 149.57 E-value: 8.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 8 QLSKT--YPGVTPVHaldqIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV-ARPGPERGV--VFQ 82
Cdd:cd03298 2 RLDKIrfSYGEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtAAPPADRPVsmLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWLNVWENVVFGpKIAGLSRREYAARA-EEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:cd03298 78 ENNLFAHLTVEQNVGLG-LSPGLKLTAEDRQAiEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 162 GALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDN--GRIA 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
8.17e-45 |
|
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: 152.90 E-value: 8.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAP---SGGELRVGGGAVARPGPE--- 76
Cdd:COG0444 2 LEVRNLKVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 --RG----VVFQE--AALFPWLNVWENVVFGPKI-AGLSRREYAARAEEMLEITGLSAFKRHL---PVQLSGGMRQRVGI 144
Cdd:COG0444 82 kiRGreiqMIFQDpmTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 145 ARVLTLGSRVLLMDEPFGALDAqtrlTMQ----ELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI---ATR 217
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDV----TIQaqilNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYA--GRIveeGPV 235
|
....*....
gi 565781182 218 IEVpIERPR 226
Cdd:COG0444 236 EEL-FENPR 243
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-161 |
1.09e-44 |
|
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: 147.02 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV-----ARPGPERGVVFQEAALFPWLNVWENV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 97 VFGPKIAGLSRREYAARAEEMLEITGLSAF-KRHLPV---QLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLaDRPVGErpgTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-215 |
3.93e-44 |
|
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: 148.29 E-value: 3.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG-GAVARPGPER---GV 79
Cdd:cd03265 1 IEVENLVKKYGDFE---AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRrriGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 160 PFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH--GRII 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-247 |
1.19e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 150.34 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVT-PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-----ER 77
Cdd:PRK11153 2 IELKNISKVFPQGGrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ---GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRV 154
Cdd:PRK11153 82 rqiGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIatrievpIERPRsldliTGE 234
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA--GRL-------VEQGT-----VSE 227
|
250
....*....|...
gi 565781182 235 VFNGLKREILKQM 247
Cdd:PRK11153 228 VFSHPKHPLTREF 240
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-215 |
9.21e-43 |
|
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: 146.04 E-value: 9.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPgpER------ 77
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE--ENlweirk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQE------AALfpwlnVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLT 149
Cdd:TIGR04520 78 kvGMVFQNpdnqfvGAT-----VEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 150 LGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAIlLADTIYVMSArpGRIA 215
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNK--GKIV 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-215 |
2.38e-42 |
|
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: 144.25 E-value: 2.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:cd03256 1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFG-----PKIAGLSRREYAA---RAEEMLEITGLS--AFKRhlPVQLSGGMRQRVGIA 145
Cdd:cd03256 79 qiGMIFQQFNLIERLSVLENVLSGrlgrrSTWRSLFGLFPKEekqRALAALERVGLLdkAYQR--ADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 146 RVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRIV 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-214 |
1.27e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.11 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPE--RGV--VFQEAALFPwLNVWENV 96
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwrRQVayVPQEPALWG-GTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 97 VFGPKIAGLSRREyaARAEEMLEITGLSAFKRHLPV-QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQEL 175
Cdd:COG4619 95 PFPFQLRERKFDR--ERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 565781182 176 LLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:COG4619 173 LREYLAEEGRAVLWVSHDPEQIERVADRVLTL--EAGRL 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-215 |
2.33e-41 |
|
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: 140.77 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 26 DLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---GVVFQEAALFPWLNVWENVVFG--P 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGlhP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 101 --KIAGLSRREYAARAEEMleitGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLS 178
Cdd:TIGR01277 98 glKLNAEQQEKVVDAAQQV----GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 565781182 179 VWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQ--GKIK 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-215 |
5.05e-41 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 148.83 E-value: 5.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYPGVTPvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:COG2274 473 DIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqi 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPwLNVWENVVFGpkiaglsrREYA--ARAEEMLEITGLSAFKRHLP-----------VQLSGGMRQRVGI 144
Cdd:COG2274 552 GVVLQDVFLFS-GTIRENITLG--------DPDAtdEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 145 ARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQtlRTTVVFVTHDiDEAILLADTIYVMSArpGRIA 215
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDK--GRIV 688
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-215 |
7.29e-41 |
|
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: 143.33 E-value: 7.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDqIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPG------PER---GVVFQEAALFPWL 90
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKrriGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWENVVFGPKIAGLSRREyaARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRL 170
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERR--ISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 565781182 171 TMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVA 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-193 |
8.15e-41 |
|
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: 139.15 E-value: 8.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----GV 79
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWENVVFGPKIAGLSRREyaARAEEMLEITGLSAFkRHLPV-QLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGL-ADLPVrQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 565781182 159 EPFGALDAQTRLTMQELLLSvWQTLRTTVVFVTHD 193
Cdd:COG4133 157 EPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-207 |
2.13e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.61 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 5 SVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGvvfqea 84
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 85 alfpwlnvwenvvfgpkiaglsRREYAARaeemleitglsafkrhlpVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGAL 164
Cdd:cd00267 72 ----------------------RRRIGYV------------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 165 DAQTRLTMQELLLSVWQTlRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-211 |
2.83e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 138.05 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 5 SVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQEA 84
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 85 AL---FPwLNVWENVVFG--PKIAGLSR--REYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGlyGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 158 DEPFGALDAQTRLTMQELLLSvWQTLRTTVVFVTHDIDEAILLADTIYVMSARP 211
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-207 |
1.37e-39 |
|
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: 134.82 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:cd03228 1 IEFKNVSFSYPG-RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkniA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPwLNVWENVvfgpkiaglsrreyaaraeemleitglsafkrhlpvqLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:cd03228 80 YVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 565781182 159 EPFGALDAQTRLTMQELLLSVwqTLRTTVVFVTHDIdEAILLADTIYVM 207
Cdd:cd03228 122 EATSALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-197 |
2.02e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 136.68 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MShISVTQLSKTYpGVTpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV---ARPGPER 77
Cdd:PRK11124 1 MS-IQLNGINCFY-GAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --------GVVFQEAALFPWLNVWENVVFGP-KIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVL 148
Cdd:PRK11124 77 irelrrnvGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565781182 149 TLGSRVLLMDEPFGALD----AQTRLTMQELllsvwQTLRTTVVFVTHDIDEA 197
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDpeitAQIVSIIREL-----AETGITQVIVTHEVEVA 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-228 |
3.51e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 141.70 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGV 79
Cdd:COG3845 6 LELRGITKRFGGV---VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrdaiALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 --VFQEAALFPWLNVWENVVFG---PKIAGLSRREYAARAEEMLEITGLS----AFKRHLPVqlsgGMRQRVGIARVLTL 150
Cdd:COG3845 83 gmVHQHFMLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDvdpdAKVEDLSV----GEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 151 GSRVLLMDEPFGALDAQTRltmQELLlsvwQTLR------TTVVFVTHDIDEAILLADTIYVMsaRPGRIATRIEVPIER 224
Cdd:COG3845 159 GARILILDEPTAVLTPQEA---DELF----EILRrlaaegKSIIFITHKLREVMAIADRVTVL--RRGKVVGTVDTAETS 229
|
....
gi 565781182 225 PRSL 228
Cdd:COG3845 230 EEEL 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-215 |
7.70e-39 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 132.55 E-value: 7.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGV 79
Cdd:cd03216 1 LELRGITKRFGGV---KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrdarRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VfqeaalfpwlnvwenVVFgpkiaglsrreyaaraeemleitglsafkrhlpvQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:cd03216 78 A---------------MVY----------------------------------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 160 PFGALDAQTRltmqELLLSVWQTLR---TTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:cd03216 109 PTAALTPAEV----ERLFKVIRRLRaqgVAVIFISHRLDEVFEIADRVTVL--RDGRVV 161
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-214 |
1.38e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.88 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTPVHAldqIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG------------- 67
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHG---IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 68 GAVARPGPERGVVFQEAALFPWLNVWENVVFGPKIA-GLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIAR 146
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 147 VLTLGSRVLLMDEPFGALDAqtrltmqELLLSVWQTLRT------TVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDP-------ELVGEVLNTIRQlaqekrTMVIVTHEMSFARDVADRAIFMDQ--GRI 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-194 |
1.43e-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: 133.63 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 9 LSKTY-PGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV-----ARPGPER----G 78
Cdd:TIGR02211 7 LGKRYqEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklssNERAKLRnkklG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 565781182 159 EPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDI 194
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL 202
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-207 |
1.83e-38 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.40 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP--------GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP 75
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 76 E------RGV--VFQE--AALFPWLNVWENVVFGPKIAGL-SRREYAARAEEMLEITGLSA-FKRHLPVQLSGGMRQRVG 143
Cdd:COG4608 88 RelrplrRRMqmVFQDpyASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 144 IARVLTLGSRVLLMDEPFGALD----AQTrLTmqeLLLSVWQTLRTTVVFVTHDideaiL-----LADTIYVM 207
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDvsiqAQV-LN---LLEDLQDELGLTYLFISHD-----LsvvrhISDRVAVM 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-197 |
3.38e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MShISVTQLSKTYpGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV---ARPGPER 77
Cdd:COG4161 1 MS-IQLKNINCFY-GSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --------GVVFQEAALFPWLNVWENVVFGP-KIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVL 148
Cdd:COG4161 77 irllrqkvGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 565781182 149 TLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVfVTHDIDEA 197
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFA 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-214 |
9.73e-38 |
|
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: 130.25 E-value: 9.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 5 SVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-----ERGV 79
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkelarKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQeaalfpwlnvwenvvfgpkiaglsrreyaaraeeMLEITGLSAFK-RHLPvQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:cd03214 78 VPQ----------------------------------ALELLGLAHLAdRPFN-ELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 159 EPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD--GRI 176
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
21-215 |
2.03e-37 |
|
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: 132.90 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER---GVVFQEAALFPWLNVWENV 96
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVRePRKVRrsiGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 97 VFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRltmqell 176
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR------- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 565781182 177 LSVWQTLR------TTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:TIGR01188 161 RAIWDYIRalkeegVTILLTTHYMEEADKLCDRIAII--DHGRII 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-217 |
9.84e-37 |
|
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: 136.05 E-value: 9.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:COG4987 333 SLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrrri 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFpwlN--VWENVVFGpkiaglsrREYA--ARAEEMLEITGLSAFKRHLP-----------VQLSGGMRQRV 142
Cdd:COG4987 412 AVVPQRPHLF---DttLRENLRLA--------RPDAtdEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 143 GIARVLTLGSRVLLMDEPFGALDAQTRltmQELLLSVWQTLRT-TVVFVTHDIdEAILLADTIYVMSArpGRIATR 217
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATE---QALLADLLEALAGrTVLLITHRL-AGLERMDRILVLED--GRIVEQ 550
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-215 |
4.56e-36 |
|
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: 134.12 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 2 SHISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---- 77
Cdd:COG4988 335 PSIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVFQEAALFPWlNVWENVVFGpkiaglsrREYAARAE--EMLEITGLSAFKRHLP-----------VQLSGGMRQRVG 143
Cdd:COG4988 413 iAWVPQNPYLFAG-TIRENLRLG--------RPDASDEEleAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 144 IARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTlrTTVVFVTHDIdEAILLADTIYVMSArpGRIA 215
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRL-ALLAQADRILVLDD--GRIV 550
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-207 |
4.81e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.08 E-value: 4.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPV--HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---- 77
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -----GVVFQ--EAALFPWlNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSA-FKRHLPVQLSGGMRQRVGIARVLT 149
Cdd:PRK13643 82 vrkkvGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 150 LGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLL 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
6.96e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.92 E-value: 6.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE-----RG 78
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAAL-FPWLnVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFK-RHLPvQLSGGMRQRVGIARVLT------- 149
Cdd:COG4559 79 VLPQHSSLaFPFT-VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAgRSYQ-TLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 150 LGSRVLLMDEPFGALDaqtrLTMQELLLSVWQTL---RTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:COG4559 157 GGPRWLFLDEPTSALD----LAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQ--GRLV 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-204 |
8.10e-36 |
|
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: 127.41 E-value: 8.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvtPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFG--------PKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARV 147
Cdd:TIGR02315 80 riGMIFQHYNLIERLTVLENVLHGrlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 148 LTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTI 204
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRI 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-202 |
4.08e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 4.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLL---N----LIAGFEApsGGELRVGGGAVARPG--PER-----GVVFQEAA 85
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGARV--EGEILLDGEDIYDPDvdVVElrrrvGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 86 LFPwLNVWENVVFGPKIAGL-SRREYAARAEEMLEITGL----------SAFKrhlpvqLSGGMRQRVGIARVLTLGSRV 154
Cdd:COG1117 103 PFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkdrlkkSALG------LSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSvwqtLRT--TVVFVTHDIDEAILLAD 202
Cdd:COG1117 176 LLMDEPTSALDPISTAKIEELILE----LKKdyTIVIVTHNMQQAARVSD 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-217 |
5.05e-35 |
|
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: 124.40 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTY-PGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER---G 78
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKePAEARrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 159 EPFGALDAQTRLTMQELLlsvwQTLR---TTVVFVTHDIDEAILLADTIYVMSArpGRIATR 217
Cdd:cd03266 162 EPTTGLDVMATRALREFI----RQLRalgKCILFSTHIMQEVERLCDRVVVLHR--GRVVYE 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-193 |
5.96e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 124.51 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---------GVVFQEAALFPWLNV 92
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 93 WENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTM 172
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|.
gi 565781182 173 QELLLSVWQTLRTTVVFVTHD 193
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-218 |
7.67e-35 |
|
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: 123.87 E-value: 7.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---GVV 80
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrriGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFGPKIAGLSRReyaaRAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 161 FGALDAQTRLTMQELLLSvWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIATRI 218
Cdd:cd03268 154 TNGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGII--NKGKLIEEG 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-214 |
1.54e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.85 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVArPGPER------ 77
Cdd:PRK13647 5 IEVEDLHFRYKDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKwvrskv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEA--ALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:PRK13647 82 GLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 156 LMDEPFGALDAQTRLTMQElLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE--GRV 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-207 |
2.63e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.07 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 27 LQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---------GVVFQEAALFPWLNVWENVV 97
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 98 FGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLL 177
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|
gi 565781182 178 SVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-215 |
3.05e-34 |
|
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: 122.30 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFvALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE-RGVVF- 81
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 82 --QEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:cd03264 77 lpQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 160 PFGALDAQTRLTMQELLLSVWQTlrTTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNK--GKLV 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-207 |
3.35e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.39 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MShISVTQLSKTYPGVTPVH--ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPG---- 74
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvkls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 ---PERGVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLS--AFKRHLPVQLSGGMRQRVGIARV 147
Cdd:PRK13637 80 dirKKVGLVFQypEYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 148 LTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-215 |
4.38e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 123.34 E-value: 4.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPE----RG 78
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAElarrRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAAL-FPWLnVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFK-RHLPvQLSGGMRQRVGIARVLT------L 150
Cdd:PRK13548 80 VLPQHSSLsFPFT-VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAgRDYP-QLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 151 GSRVLLMDEPFGALDaqtrLTMQELLLsvwQTLR-------TTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:PRK13548 158 PPRWLLLDEPTSALD----LAHQHHVL---RLARqlahergLAVIVVLHDLNLAARYADRIVLLHQ--GRLV 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-207 |
1.02e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 123.21 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVH--ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgAVARPG------- 74
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE-RVITAGkknkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 PER---GVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLS-AFKRHLPVQLSGGMRQRVGIARVL 148
Cdd:PRK13634 82 PLRkkvGIVFQfpEHQLFE-ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 149 TLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-193 |
1.04e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 128.30 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 9 LSKTYP-GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---------G 78
Cdd:PRK10535 10 IRRSYPsGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrehfG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 565781182 159 EPFGALDAQTrltmQELLLSVWQTLRT---TVVFVTHD 193
Cdd:PRK10535 170 EPTGALDSHS----GEEVMAILHQLRDrghTVIIVTHD 203
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-193 |
4.76e-33 |
|
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: 118.87 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---------GVVFQEAALFPWL 90
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrreklGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRL 170
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180
....*....|....*....|....*.
gi 565781182 171 TMQELLLSvwqtLR---TTVVFVTHD 193
Cdd:TIGR03608 172 EVLDLLLE----LNdegKTIIIVTHD 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-214 |
5.13e-33 |
|
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: 119.57 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYpGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER---GV 79
Cdd:cd03218 1 LRAENLSKRY-GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRarlGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VF--QEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:cd03218 78 GYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVwqTLRTTVVFVT-HDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKIL--KDRGIGVLITdHNVRETLSITDRAYIIYE--GKV 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-215 |
1.01e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.89 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 12 TYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQEAAL 86
Cdd:COG1132 348 SYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrqiGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 87 FPwLNVWENVVFGpkiaglsrREYAARAE--EMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG1132 426 FS-GTIRENIRYG--------RPDATDEEveEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVfVTHDIdEAILLADTIYVMSArpGRIA 215
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKG-RTTIV-IAHRL-STIRNADRILVLDD--GRIV 553
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-194 |
1.27e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.79 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTPVHA------LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPG 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSGKhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 PE------RGV--VFQEA--ALFPWLNVWEnVVFGP--KIAGLSRREYAARAEEMLEITGLSA-FKRHLPVQLSGGMRQR 141
Cdd:PRK10419 81 RAqrkafrRDIqmVFQDSisAVNPRKTVRE-IIREPlrHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565781182 142 VGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDI 194
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDL 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-215 |
2.45e-32 |
|
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: 117.63 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP-------------------GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELR 64
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 65 VGGGAVARPGPerGVVFQeaalfPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFkRHLPV-QLSGGMRQRVG 143
Cdd:cd03220 81 VRGRVSSLLGL--GGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDF-IDLPVkTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 144 IARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEK--GKIR 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-214 |
7.74e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.92 E-value: 7.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVH--ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---- 77
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -----GVVFQ--EAALFPWlNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSA--FKRHlPVQLSGGMRQRVGIARVL 148
Cdd:PRK13649 83 irkkvGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 149 TLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEK--GKL 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-207 |
1.16e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.42 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgavaRPGPER------ 77
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG----MVLSEEtvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ---GVVFQEA-ALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:PRK13635 81 rqvGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAiLLADTIYVM 207
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVM 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-207 |
1.17e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 121.62 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWlNVWENVVFGpkiaglsrREYAARAE--EMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIA 145
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLA--------RPDASDAEirEALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 146 RVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQtlRTTVVFVTHDiDEAILLADTIYVM 207
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-165 |
1.22e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.28 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGvTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER-- 77
Cdd:COG1137 1 MMTLEAENLVKSYGK-RTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHKRar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVF--QEAALFPWLNVWENV--VFgpKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGS 152
Cdd:COG1137 78 lGIGYlpQEASIFRKLTVEDNIlaVL--ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170
....*....|...
gi 565781182 153 RVLLMDEPFGALD 165
Cdd:COG1137 156 KFILLDEPFAGVD 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-197 |
1.62e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 115.68 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 7 TQLSKTY-PGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG------GAVARP---GPE 76
Cdd:PRK11629 9 DNLCKRYqEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAelrNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 RGVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEA 197
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-215 |
4.10e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 114.45 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 19 VHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------GVVFQEAALFPWLNV 92
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragiGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 93 WENVVFGpkIAGLSRREYAARAEEMLEI-TGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQtrlt 171
Cdd:cd03224 93 EENLLLG--AYARRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK---- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 565781182 172 MQELLLSVWQTLR---TTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:cd03224 167 IVEEIFEAIRELRdegVTILLVEQNARFALEIADRAYVLER--GRVV 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-214 |
7.83e-31 |
|
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: 119.40 E-value: 7.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPG--------VTPVHALDQIDLQVAEGEFVALLGPSGCGKSTL----LNLIagfeaPSGGELRVGGGAVA 71
Cdd:COG4172 276 LEARDLKVWFPIkrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 72 RPGPERG--------VVFQE--AALFPWLNVWENV-----VFGPkiaGLSRREYAARAEEMLEITGLSAFKRH-LPVQLS 135
Cdd:COG4172 351 GLSRRALrplrrrmqVVFQDpfGSLSPRMTVGQIIaeglrVHGP---GLSAAERRARVAEALEEVGLDPAARHrYPHEFS 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 136 GGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM--KDGKV 504
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-208 |
9.94e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 9.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV---------ARPg 74
Cdd:PRK13639 2 LETRDLKYSYPDGT--EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkslleVRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 pERGVVFQ--EAALF-PwlNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLG 151
Cdd:PRK13639 79 -TVGIVFQnpDDQLFaP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 152 SRVLLMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMS 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-207 |
1.65e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.54 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 14 PGvTPVHA--LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG---------GAVARPGPERGVVFQ 82
Cdd:PRK13641 14 PG-TPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNLKKLRKKVSLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 --EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLS-AFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:PRK13641 93 fpEAQLFE-NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 565781182 160 PFGALDAQTRLTMQELLLSvWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-208 |
1.72e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.56 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV--ARPG-----PE 76
Cdd:PRK13636 6 LKVEELNYNYSDGT--HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGlmklrES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 RGVVFQEA--ALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRV 154
Cdd:PRK13636 84 VGMVFQDPdnQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-200 |
1.95e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 113.25 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSH-ISVTQLSKTYP-------------------GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSG 60
Cdd:COG1134 1 MSSmIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 61 GELRVGGgavaRPGP--ERGVVFQeaalfPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFkRHLPVQ-LSGG 137
Cdd:COG1134 81 GRVEVNG----RVSAllELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDF-IDQPVKtYSSG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 138 MRQRVGIARVLTLGSRVLLMDEPFGALDA--QTRLT--MQELLLSvwqtlRTTVVFVTHDI-------DEAILL 200
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDEVLAVGDAafQKKCLarIRELRES-----GRTVIFVSHSMgavrrlcDRAIWL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-220 |
1.84e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 111.44 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERG--------VVFQEA--ALFPWLN 91
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRrafrrdvqLVFQDSpsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VwENVVFGP--KIAGLSRREYAARAEEMLEITGL-SAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQT 168
Cdd:TIGR02769 107 V-RQIIGEPlrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 169 RLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIATRIEV 220
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQIVEECDV 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-214 |
2.96e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirkkiG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEA-ALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:PRK13632 87 IIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAIlLADTIYVMSArpGRI 214
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSE--GKL 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-207 |
3.83e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.95 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG------GAVARPGPERGVVFQE------AALfp 88
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQNpdnqivATI-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 wlnVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQT 168
Cdd:PRK13633 103 ---VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 565781182 169 RLTMQELLLSVWQTLRTTVVFVTHDIDEAIlLADTIYVM 207
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVM 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-214 |
4.15e-29 |
|
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: 109.79 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAP-SGGELRVGGgavARPGPER--------GVVFQEAALF--PWL 90
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFG---ERRGGEDvwelrkriGLVSPALQLRfpRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWENVV---FGpkIAGLSRR---EYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGAL 164
Cdd:COG1119 96 TVLDVVLsgfFD--SIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 165 DaqtrLTMQELLLSVWQTL----RTTVVFVTHDIDEAIllaDTIY-VMSARPGRI 214
Cdd:COG1119 174 D----LGARELLLALLDKLaaegAPTLVLVTHHVEEIP---PGIThVLLLKDGRV 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-197 |
5.31e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.09 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 13 YPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAvaRPG--PERGVVfqeAALFPwL 90
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--RVAyvPQRSEV---PDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWENVVFG--PKIAGLSR--REYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDA 166
Cdd:NF040873 73 TVRDLVAMGrwARRGLWRRltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|.
gi 565781182 167 QTRLTMQElLLSVWQTLRTTVVFVTHDIDEA 197
Cdd:NF040873 153 ESRERIIA-LLAEEHARGATVVVVTHDLELV 182
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-207 |
7.09e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.21 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 8 QLSKTYP-------GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE---- 76
Cdd:PRK11308 10 DLKKHYPvkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 --RGV--VFQE--AALFPWLNVwENVVFGPKI--AGLSRREYAARAEEMLEITGLSA--FKRHlPVQLSGGMRQRVGIAR 146
Cdd:PRK11308 90 lrQKIqiVFQNpyGSLNPRKKV-GQILEEPLLinTSLSAAERREKALAMMAKVGLRPehYDRY-PHMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 147 VLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-214 |
7.32e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.72 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVHAldqIDLQVAEGEFVALLGPSGCGKSTLL----NLIAGFEAPsGGELRVGGGAVARPG----- 74
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHA---VDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSA-GSHIELLGRTVQREGrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 -----PERGVVFQEAALFPWLNVWENVVFG-----PKIAGLSR---REYAARAEEMLEITGLSAFKRHLPVQLSGGMRQR 141
Cdd:PRK09984 81 irksrANTGYIFQQFNLVNRLSVLENVLIGalgstPFWRTCFSwftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 142 VGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHV 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-207 |
1.24e-28 |
|
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: 107.75 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-GVVFQ 82
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 565781182 163 ALDAQTrltmQELLLSVWQTLR---TTVVFVTHDIDEAILLADTIYVM 207
Cdd:cd03269 158 GLDPVN----VELLKDVIRELAragKTVILSTHQMELVEELCDRVLLL 201
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-207 |
1.66e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.05 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPG-----PERG 78
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEA-ALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEaILLADTIYVM 207
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-207 |
3.43e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.33 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVH--ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA--------RP 73
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEhqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 74 GPER-GVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGlsaFKRHL----PVQLSGGMRQRVGIAR 146
Cdd:PRK13646 83 VRKRiGMVFQfpESQLFE-DTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLG---FSRDVmsqsPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 147 VLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
3.95e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 6 VTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVArpgperGVVFQEAA 85
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRI------GYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 86 LFPWLNVWENV--VFGPKIAGLSRREYA------------------------------ARAEEMLEITGLSAFKRHLPV- 132
Cdd:COG0488 72 LDDDLTVLDTVldGDAELRALEAELEELeaklaepdedlerlaelqeefealggweaeARAEEILSGLGFPEEDLDRPVs 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 133 QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLlsvwQTLRTTVVFVTHD 193
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-194 |
4.53e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 106.50 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR------PGPER 77
Cdd:PRK10908 2 IRFEHVSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:PRK10908 80 qiGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565781182 156 LMDEPFGALDAQtrltMQELLLSVWQTLR---TTVVFVTHDI 194
Cdd:PRK10908 160 LADEPTGNLDDA----LSEGILRLFEEFNrvgVTVLMATHDI 197
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-204 |
5.68e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.24 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLN-----LIAGFEAPSGGELRVGGGAVARPG-------PERGVVFQEAALF 87
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDvdpievrREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 88 PWLNVWENVVFGPKIAGL--SRREYAARAEEMLEITGL-SAFKRHL---PVQLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 162 GALDAQTRLTMQELLLSVWQTLrtTVVFVTHDIDEAILLADTI 204
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYV 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-214 |
6.89e-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: 111.05 E-value: 6.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTP--VHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGEL--RVGGGAV--ARPGPER 77
Cdd:TIGR03269 280 IKVRNVSKRYISVDRgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVdmTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --------GVVFQEAALFPWLNVWENV-----------------VFGPKIAGLSRREyaarAEEMLEitglsafkrHLPV 132
Cdd:TIGR03269 360 rgrakryiGILHQEYDLYPHRTVLDNLteaiglelpdelarmkaVITLKMVGFDEEK----AEEILD---------KYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 133 QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPG 212
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDG 504
|
..
gi 565781182 213 RI 214
Cdd:TIGR03269 505 KI 506
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-207 |
7.84e-28 |
|
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: 105.24 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAgfeapsgGELRVGGGAVARPGPErGVVFQEaalfPWL---NVWENVV 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELEKLSGSVSVPGSI-AYVSQE----PWIqngTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 98 FGpkiaglsRREYAARAEEMLEITGLSA-FKRhLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALD 165
Cdd:cd03250 88 FG-------KPFDEERYEKVIKACALEPdLEI-LPdgdlteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 166 AQT-RLTMQELLLSVWQTLRtTVVFVTHDIdEAILLADTIYVM 207
Cdd:cd03250 160 AHVgRHIFENCILGLLLNNK-TRILVTHQL-QLLPHADQIVVL 200
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-217 |
9.73e-28 |
|
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: 105.78 E-value: 9.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 12 TYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA-------RpgPERGVVFQEA 84
Cdd:cd03251 9 RYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdytlaslR--RQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 85 ALFPWlNVWENVVFGPKIAGLSRREYAARAEEMLEitglsaFKRHLP-----------VQLSGGMRQRVGIARVLTLGSR 153
Cdd:cd03251 86 FLFND-TVAENIAYGRPGATREEVEEAARAANAHE------FIMELPegydtvigergVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVfVTHDIdEAILLADTIYVMSArpGRIATR 217
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRL-STIENADRIVVLED--GKIVER 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-215 |
1.36e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.14 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERG----- 78
Cdd:PRK15439 12 LCARSISKQYSGV-EV--LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 -VVFQEAALFPWLNVWENVVFgpkiaGLSRREYAARAEEMLeitgLSAFKRHLPVQLSGGM-----RQRVGIARVLTLGS 152
Cdd:PRK15439 89 yLVPQEPLLFPNLSVKENILF-----GLPKRQASMQKMKQL----LAALGCQLDLDSSAGSlevadRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 153 RVLLMDEPFGALD-AQTrltmqELLLSVWQTLRTT---VVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:PRK15439 160 RILILDEPTASLTpAET-----ERLFSRIRELLAQgvgIVFISHKLPEIRQLADRISVM--RDGTIA 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-207 |
1.69e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGvtPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER--- 77
Cdd:PRK13652 1 MHLIETRDLCYSYSG--SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:PRK13652 79 fvGLVFQnpDDQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-215 |
1.69e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.55 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYpGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER----G 78
Cdd:COG4604 2 IEIKNVSKRY-GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELakrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFG--PKIAGLSRREYAARAEEMLEITGLSAFK-RHLPvQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFGrfPYSKGRLTAEDREIIDEAIAYLDLEDLAdRYLD-ELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 156 LMDEPFGALD-AQTRLTMQeLLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:COG4604 158 LLDEPLNNLDmKHSVQMMK-LLRRLADELGKTVVIVLHDINFASCYADHIVAM--KDGRVV 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-208 |
1.80e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.00 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 23 DQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVarPGPERG----------VVFQEAALFPWLNV 92
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--PAMSRSrlytvrkrmsMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 93 WENVVFgpkiaglSRREYAARAEEM--------LEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGAL 164
Cdd:PRK11831 102 FDNVAY-------PLREHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 565781182 165 DAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVA 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-209 |
1.93e-27 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 104.82 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYP----GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRV--GGGAV--ARPGP 75
Cdd:COG4778 5 LEVENLSKTFTlhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 76 ER---------GVVFQeaalFpwLNVW-----ENVVFGPKIA-GLSRREYAARAEEMLEITGLsafKRHL----PVQLSG 136
Cdd:COG4778 85 REilalrrrtiGYVSQ----F--LRVIprvsaLDVVAEPLLErGVDREEARARARELLARLNL---PERLwdlpPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 137 GMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLlsvwQTLR---TTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI----EEAKargTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-214 |
2.45e-27 |
|
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: 105.11 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTY------PGVTP------------VHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRV 65
Cdd:cd03267 1 IEVSNLSKSYrvyskePGLIGslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 66 GGgavARPGPER-------GVVFQEAALFPW-LNVWENVVFGPKIAGLSRREYAARAE---EMLEITGLsafkRHLPV-Q 133
Cdd:cd03267 81 AG---LVPWKRRkkflrriGVVFGQKTQLWWdLPVIDSFYLLAAIYDLPPARFKKRLDelsELLDLEEL----LDTPVrQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 134 LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGR 213
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK--GR 231
|
.
gi 565781182 214 I 214
Cdd:cd03267 232 L 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-198 |
4.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.94 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVH--ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGG------------------EL 63
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 64 RVGGGAVARPGPER-----------GVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGL--SAFKR 128
Cdd:PRK13651 83 VLEKLVIQKTRFKKikkikeirrrvGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdeSYLQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 129 HlPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAI 198
Cdd:PRK13651 162 S-PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVL 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-214 |
4.99e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 104.62 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 5 SVTQLSKTYpgvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGEL--RVGGGAV----ARPGPER- 77
Cdd:PRK11701 8 SVRGLTKLY---GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLrdlyALSEAERr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -------GVVFQEAA--LFPWLNVWENVvfGPKIAGLSRREYA---ARAEEMLEITGLSAfKR--HLPVQLSGGMRQRVG 143
Cdd:PRK11701 85 rllrtewGFVHQHPRdgLRMQVSAGGNI--GERLMAVGARHYGdirATAGDWLERVEIDA-ARidDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 144 IARVLTLGSRVLLMDEPFGALD--AQTRLTmqELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDvsVQARLL--DLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQGRV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-215 |
9.65e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.14 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 18 PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE----RGVVF--QEAALFPWLN 91
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarLGIGYvpEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVFGPKIAGlSRREYAARAEEMLEI-TGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPfgaldaqtrl 170
Cdd:COG0410 95 VEENLLLGAYARR-DRAEVRADLERVYELfPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP---------- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 171 TM-------QElllsVWQTLR------TTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:COG0410 164 SLglaplivEE----IFEIIRrlnregVTILLVEQNARFALEIADRAYVLER--GRIV 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-207 |
1.43e-26 |
|
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: 101.14 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWlNVWENVvfgpkiaglsrreyaaraeemleitglsafkrhlpvqLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:cd03246 80 YLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 159 EPFGALDAQTrltmQELLLSVWQTLR---TTVVFVTHDIdEAILLADTIYVM 207
Cdd:cd03246 122 EPNSHLDVEG----ERALNQAIAALKaagATRIVIAHRP-ETLASADRILVL 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-214 |
2.06e-26 |
|
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: 106.69 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 15 GVTPVHALDQIDLQVAEGEFVALLGPSGCGKS----TLLNLIAGFEAPSGGELRVGGGAVARPGPER---------GVVF 81
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgnriAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 82 QE--AALFPWLNVwenvvfGPKIA-------GLSRREYAARAEEMLEITGLSAFKRHL---PVQLSGGMRQRVGIARVLT 149
Cdd:COG4172 99 QEpmTSLNPLHTI------GKQIAevlrlhrGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAMALA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 150 LGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIdeAIL--LADTIYVMsaRPGRI 214
Cdd:COG4172 173 NEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL--GVVrrFADRVAVM--RQGEI 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-216 |
2.14e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.53 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 10 SKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV----ARPGPERGV--VFQE 83
Cdd:PRK11288 11 GKTFPGV---KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAAGVaiIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 AALFPWLNVWENVVFG--PKIAGL-SRREYAARAEEMLEITGLSaFKRHLPVQ-LSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:PRK11288 88 LHLVPEMTVAENLYLGqlPHKGGIvNRRLLNYEAREQLEHLGVD-IDPDTPLKyLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 160 PFGALDAqtRLTmqELLLSVWQTLR---TTVVFVTHDIDEAILLADTIYVMsaRPGR-IAT 216
Cdd:PRK11288 167 PTSSLSA--REI--EQLFRVIRELRaegRVILYVSHRMEEIFALCDAITVF--KDGRyVAT 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-193 |
3.06e-26 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 106.29 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 9 LSKTYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQE 83
Cdd:TIGR02868 340 LSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrrvSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 AALFPwLNVWENVVFGpkiaglsrREYAARAE--EMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTL 150
Cdd:TIGR02868 418 AHLFD-TTVRENLRLA--------RPDATDEElwAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 151 GSRVLLMDEPFGALDAQTRLTMQELLLSVwqTLRTTVVFVTHD 193
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-242 |
4.43e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.17 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLL-------NLIAGFEAPsgGELRVGGGAVARPGPER-------GVVFQEAAL 86
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVE--GKVTFHGKNLYAPDVDPvevrrriGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 87 FPwLNVWENVVFGPKIAGL----------SRREYAARAE--EMLEITGLSafkrhlpvqLSGGMRQRVGIARVLTLGSRV 154
Cdd:PRK14243 103 FP-KSIYDNIAYGARINGYkgdmdelverSLRQAALWDEvkDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQtlRTTVVFVTHDIDEAILLADTIYVMSARPGRIATRIEVPIERPRsldliTGE 234
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDR-----TEK 245
|
....*...
gi 565781182 235 VFNGLKRE 242
Cdd:PRK14243 246 IFNSPQQQ 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-231 |
5.61e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.78 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVH--ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGA----------VA 71
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanlkkikeVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 72 RPGPERGVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGL-SAFKRHLPVQLSGGMRQRVGIARVL 148
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 149 TLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMS-------ARPGRIATRIE-- 219
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHegkvisiGSPFEIFSNQEll 245
|
250
....*....|....
gi 565781182 220 --VPIERPRSLDLI 231
Cdd:PRK13645 246 tkIEIDPPKLYQLM 259
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-210 |
9.59e-26 |
|
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: 100.31 E-value: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 27 LQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQEAAlFPW---LNVWENVVFG-PKI 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHE-FAWdfpISVAHTVMSGrTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 103 AGLSRR----EYAARAEEmLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTrltmQELLLS 178
Cdd:TIGR03771 80 IGWLRRpcvaDFAAVRDA-LRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT----QELLTE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 565781182 179 VWQTLR---TTVVFVTHDIDEAILLADTIYVMSAR 210
Cdd:TIGR03771 155 LFIELAgagTAILMTTHDLAQAMATCDRVVLLNGR 189
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-214 |
9.91e-26 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 99.04 E-value: 9.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGVVF-----QEAALFPWLN 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdaiRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVfgpkiaglsrreyaaraeemleitglsafkrhLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLT 171
Cdd:cd03215 95 VAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 565781182 172 MQELLLSvwqtLR---TTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:cd03215 143 IYRLIRE----LAdagKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
1.36e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP-------- 75
Cdd:COG4152 2 LELKGLTKRFGDKT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 76 ERGvvfqeaaLFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAfKRHLPVQ-LSGGMRQRVGIArvLTLGSR- 153
Cdd:COG4152 79 ERG-------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGD-RANKKVEeLSKGNQQKVQLI--AALLHDp 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 154 -VLLMDEPFGALDAQTRLTMQELLLSvwqtLR---TTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG4152 149 eLLILDEPFSGLDPVNVELLKDVIRE----LAakgTTVIFSSHQMELVEELCDRIVIINK--GRK 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-207 |
1.47e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.83 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPE---RGVV--FQEAALFPWLNVWE 94
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQiarMGVVrtFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 95 NVVFGPK-------IAGL--------SRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:PRK11300 100 NLLVAQHqqlktglFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 565781182 160 PFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-202 |
1.88e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGF-----EAPSGGELRVGGGAVARPG-------PERGVVFQEAALFP 88
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRtdtvdlrKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 wLNVWENVVFGPKIAGLSRREYAARAEEMlEITGLSAF---KRHL---PVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:PRK14239 100 -MSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWdevKDRLhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 565781182 163 ALDAQTRLTMQELLLSVWQtlRTTVVFVTHDIDEAILLAD 202
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISD 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-207 |
2.51e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.87 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 24 QIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG-------GAVARPgPER---GVVFQEAALFPWLNVW 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLP-PEKrriGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 94 ENVVFGPKiagLSRREYAARAEEMLEITGLsaFKRhLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRltmQ 173
Cdd:PRK11144 95 GNLRYGMA---KSMVAQFDKIVALLGIEPL--LDR-YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK---R 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 565781182 174 ELL-----LSvwQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK11144 166 ELLpylerLA--REINIPILYVSHSLDEILRLADRVVVL 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
2.60e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 101.32 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTY------PGV------------TPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRV 65
Cdd:COG4586 2 IEVENLSKTYrvyekePGLkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 66 GGgavARPGPER-------GVVF-QEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKrHLPV-QLSG 136
Cdd:COG4586 82 LG---YVPFKRRkefarriGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL-DTPVrQLSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 137 GMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH--GRI 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-214 |
2.77e-25 |
|
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: 99.54 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 12 TYPGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQEAAL 86
Cdd:cd03249 9 RYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrsqiGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 87 FPwLNVWENVVFGPKIAGLSRREYAARAEEMLEitglsaFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:cd03249 89 FD-GTIAENIRYGKPDATDEEVEEAAKKANIHD------FIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 156 LMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVfVTHDIdEAILLADTIYVMSarPGRI 214
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKG-RTTIV-IAHRL-STIRNADLIAVLQ--NGQV 215
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-215 |
5.26e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 103.11 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG--------GAVARpgp 75
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlagldvQAVRR--- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 76 ERGVVFQEAALFPWlNVWENVVFGpkiAGLSRREyaarAEEMLEITGLSAFKRHLPVQ-----------LSGGMRQRVGI 144
Cdd:TIGR03797 528 QLGVVLQNGRLMSG-SIFENIAGG---APLTLDE----AWEAARMAGLAEDIRAMPMGmhtvisegggtLSGGQRQRLLI 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 145 ARVLTLGSRVLLMDEPFGALDAQTRLTMQELLlsvwQTLRTTVVFVTHDIdEAILLADTIYVMSArpGRIA 215
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRL-STIRNADRIYVLDA--GRVV 663
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-214 |
6.03e-25 |
|
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: 98.05 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:cd03245 3 IEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrrniG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFpWLNVWENVVFGPKIAGlsrreyAARAEEMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARV 147
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 148 LTLGSRVLLMDEPFGALDAQTRLTMQELLLsvwQTLRT-TVVFVTHDIdeAIL-LADTIYVMSArpGRI 214
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLR---QLLGDkTLIIITHRP--SLLdLVDRIIVMDS--GRI 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
7.10e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.00 E-value: 7.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKT-YPG-VTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPER--- 77
Cdd:COG1101 2 LELKNLSKTfNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRaky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVFQEAAL--FPWLNVWENVVfgpkIA-------GLSR---REYAARAEEMLEITGLSAFKR-HLPV-QLSGGMRQrv 142
Cdd:COG1101 82 iGRVFQDPMMgtAPSMTIEENLA----LAyrrgkrrGLRRgltKKRRELFRELLATLGLGLENRlDTKVgLLSGGQRQ-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 143 giarVLTL------GSRVLLMDEPFGALDAQT-----RLTMQelllsVWQTLRTTVVFVTHDIDEAILLADTIYVMSArp 211
Cdd:COG1101 156 ----ALSLlmatltKPKLLLLDEHTAALDPKTaalvlELTEK-----IVEENNLTTLMVTHNMEQALDYGNRLIMMHE-- 224
|
...
gi 565781182 212 GRI 214
Cdd:COG1101 225 GRI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-207 |
8.58e-25 |
|
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: 96.61 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----GV 79
Cdd:cd03247 1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFpwlnvwenvvfgpkiaglsrreyaarAEEMLEITGLsafkrhlpvQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:cd03247 80 LNQRPYLF--------------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 565781182 160 PFGALDaqtRLTMQELLLSVWQTLR-TTVVFVTHDIdEAILLADTIYVM 207
Cdd:cd03247 125 PTVGLD---PITERQLLSLIFEVLKdKTLIWITHHL-TGIEHMDKILFL 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-208 |
1.45e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVHALDqidLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR----------- 72
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLS---LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrqlarrla 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 73 ------PGPErGVVFQEAALF---PWLNVWenvvfgpkiAGLSRREYaARAEEMLEITGLSAFKRHLPVQLSGGMRQRVG 143
Cdd:PRK11231 80 llpqhhLTPE-GITVRELVAYgrsPWLSLW---------GRLSAEDN-ARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 144 IARVLTLGSRVLLMDEPFGALDaqtrLTMQELLLSVWQTLRT---TVVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLD----INHQVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-214 |
1.70e-24 |
|
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: 102.01 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTY-PGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARP----GPERG 78
Cdd:TIGR01257 929 VCVKNLVKIFePSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 159 EPFGALDAQTRLTMQELLLSvWQTLRtTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLK-YRSGR-TIIMSTHHMDEADLLGDRIAIISQ--GRL 1138
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-214 |
2.30e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.92 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV----ARPGPE 76
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTT---VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 R-GVVFQEAALFPWLNVWENVVFG--PKIAGLSRREYAARA--EEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLG 151
Cdd:PRK09536 78 RvASVPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWTETDRAavERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 152 SRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLAD--GRV 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-207 |
2.35e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 97.59 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRV---GGGAV---ARPGPER 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGK---GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELelyQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --------GVVFQEAALFPWLNVWENVVFGPKIAGLSRREYA---ARAEEMLEITGLSAFK-RHLPVQLSGGMRQRVGIA 145
Cdd:TIGR02323 81 rrlmrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGnirATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 146 RVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-217 |
3.14e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.39 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISvtqlsKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFeAPSG---GELRVGGGAVA----RP 73
Cdd:PRK13549 8 MKNIT-----KTFGGVK---ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQasniRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 74 GPERGVV--FQEAALFPWLNVWENVVFGPKIAGLSRREYAA---RAEEMLEITGLsAFKRHLPV-QLSGGMRQRVGIARV 147
Cdd:PRK13549 79 TERAGIAiiHQELALVKELSVLENIFLGNEITPGGIMDYDAmylRAQKLLAQLKL-DINPATPVgNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 148 LTLGSRVLLMDEPFGALDAQTrltmQELLLSVWQTLR---TTVVFVTHDIDEAILLADTIYVMsaRPGR-IATR 217
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESE----TAVLLDIIRDLKahgIACIYISHKLNEVKAISDTICVI--RDGRhIGTR 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-167 |
3.45e-24 |
|
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: 95.50 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA--RPGPERGVVF--QEAALFPWLNVWENV 96
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeqRDEPHENILYlgHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 97 VFGPKIAGLSRREyaarAEEMLEITGLSAFKrHLPV-QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQ 167
Cdd:TIGR01189 95 HFWAAIHGGAQRT----IEDALAAVGLTGFE-DLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-246 |
4.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 18 PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVG----------GGAVARPGPER---------- 77
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVFQ--EAALFPwLNVWENVVFGPKIAGLSRREYAARAEEMLEITGL-SAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:PRK13631 118 vSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDI-------DEAILLADTIYVMSARPGRIATRIEV----PI 222
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMehvlevaDEVIVMDKGKILKTGTPYEIFTDQHIinstSI 275
|
250 260
....*....|....*....|....
gi 565781182 223 ERPRSLDLITGEVFNGLKREILKQ 246
Cdd:PRK13631 276 QVPRVIQVINDLIKKDPKYKKLYQ 299
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-207 |
4.64e-24 |
|
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: 95.40 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 9 LSKTYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgaVARPGPER----GVVFQEA 84
Cdd:cd03226 5 ISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG--KPIKAKERrksiGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 85 --ALFPwLNVWENVVFGPKIAGlsrrEYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:cd03226 81 dyQLFT-DSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 565781182 163 ALDAQTRLTMQELLLSVwQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:cd03226 156 GLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-207 |
4.87e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.18 E-value: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAP---SGGELRVGGGAVARPG----PE 76
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTvwdiRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 R-GVVFQEA-ALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRV 154
Cdd:PRK13640 85 KvGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAIlLADTIYVM 207
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVL 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-207 |
4.94e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVhalDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgavaRPGPER------ 77
Cdd:PRK13537 8 IDFRNVEKRYGDKLVV---DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG----EPVPSRarharq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 --GVVFQEAALFPWLNVWENV-VFGpKIAGLSRREYAARAEEMLEITGLSAfKRHLPV-QLSGGMRQRVGIARVLTLGSR 153
Cdd:PRK13537 81 rvGVVPQFDNLDPDFTVRENLlVFG-RYFGLSAAAARALVPPLLEFAKLEN-KADAKVgELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVI 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-213 |
5.51e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQEAALFPwLNVWENV 96
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrqqvSYCAQTPTLFG-DTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 97 VFGPKI-----------AGLSRREYaarAEEMLE--ITglsafkrhlpvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGA 163
Cdd:PRK10247 102 IFPWQIrnqqpdpaiflDDLERFAL---PDTILTknIA-----------ELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 565781182 164 LDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEaILLADTIYVMSARPGR 213
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGE 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-209 |
1.17e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVhalDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV---ARPGPER-GV 79
Cdd:PRK13536 42 IDLAGVSKSYGDKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparARLARARiGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAALFPWLNVWEN-VVFGpKIAGLSRREYAARAEEMLEITGLSAfKRHLPV-QLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:PRK13536 119 VPQFDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLES-KADARVsDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWqTLRTTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-207 |
1.28e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.70 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPgvtPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------ 77
Cdd:PRK09700 6 ISMAGIGKSFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaaqlgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPWLNVWENVVFG----PKIAGLSRREYA---ARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTL 150
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGrhltKKVCGVNIIDWRemrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 151 GSRVLLMDEPfgaldaQTRLTMQEL--LLSVWQTLR---TTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK09700 163 DAKVIIMDEP------TSSLTNKEVdyLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVM 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-214 |
1.52e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.82 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG---GAVAR-PGPER-- 77
Cdd:PRK13644 2 IRLENVSYSYPDGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKlQGIRKlv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAAL-FPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEaILLADTIYVMSArpGRI 214
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMDR--GKI 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-197 |
2.07e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.04 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYpGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERG----- 78
Cdd:PRK10619 6 LNVIDLHKRY-GEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 -------------VVFQEAALFPWLNVWENVVFGP-KIAGLSRREYAARAEEMLEITGLSAFKR-HLPVQLSGGMRQRVG 143
Cdd:PRK10619 83 dknqlrllrtrltMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 144 IARVLTLGSRVLLMDEPFGALDAQtrltMQELLLSVWQTLR---TTVVFVTHDIDEA 197
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQQLAeegKTMVVVTHEMGFA 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-215 |
2.42e-23 |
|
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: 94.48 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQEAALFPwLNVWEN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlrrqvGVVLQENVLFN-RSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 VVFGPKIAGLSRREYAARaeemleITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGAL 164
Cdd:cd03252 96 IALADPGMSMERVIEAAK------LAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 565781182 165 DAQTRLTMQELLLSVWQTlrTTVVFVTHDIdEAILLADTIYVMSArpGRIA 215
Cdd:cd03252 170 DYESEHAIMRNMHDICAG--RTVIIIAHRL-STVKNADRIIVMEK--GRIV 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-214 |
9.13e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 19 VHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGF-----EAPSGGELRVGGGAVAR-PGPE--RGV--VFQEAALFP 88
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKmDVIElrRRVqmVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 WLNVWENVVFGPKIAGL--SRREYAARAEEMLEITGL-SAFKRHLPV---QLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:PRK14247 96 NLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 163 ALDAQTRLTMQELLLSVWQTLrtTVVFVTHDIDEAILLADtiYVMSARPGRI 214
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISD--YVAFLYKGQI 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-209 |
9.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPG-----PERG 78
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEA-ALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAIlLADTIYVMSA 209
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKA 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-219 |
9.96e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 9.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTL---LNLIAGFEapsgGELRVGGGA-------------VARPGPERGVVFQEAA 85
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELE----SEVRVEGRVeffnqniyerrvnLNRLRRQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 86 LFPwLNVWENVVFGPKIAGLSRR-------EYAARAEEMLEITGLSAFKRHLpvQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 159 EPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPGRIATRIE 219
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVE 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-217 |
1.27e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 96.32 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA-------RPgpE 76
Cdd:TIGR02203 331 VEFRNVTFRYPG-RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdytlaslRR--Q 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 RGVVFQEAALFPwLNVWENVVFG-PKIAGLSRREYAARAEEMLEITGLSAFKRHLPV-----QLSGGMRQRVGIARVLTL 150
Cdd:TIGR02203 408 VALVSQDVVLFN-DTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIgengvLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 151 GSRVLLMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVfVTHDIdEAILLADTIYVMSArpGRIATR 217
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQG-RTTLV-IAHRL-STIEKADRIVVMDD--GRIVER 548
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-214 |
1.68e-22 |
|
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: 91.90 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgavaRPGPER---------GVVFQEAALFPWl 90
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG----IDIRDIsrkslrsmiGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWENVVFGpkiaglsrREYAARAEEM--LEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:cd03254 92 TIMENIRLG--------RPNATDEEVIeaAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTlRTTVVfVTHDIDeAILLADTIYVMsaRPGRI 214
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKG-RTSII-IAHRLS-TIKNADKILVL--DDGKI 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
2.03e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAvarpgpERGVVFQE 83
Cdd:COG0488 316 LELEGLSKSYGD-KTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 -AALFPWLNVWENVV-FGPKIAGLSRREYAARaeeMLeITGLSAFKrhlPV-QLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:COG0488 387 qEELDPDKTVLDELRdGAPGGTEQEVRGYLGR---FL-FSGDDAFK---PVgVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 161 FGALDAQTRLTMQELLLSvWQtlrTTVVFVTHD---IDEailLADTIYVMsaRPGRI 214
Cdd:COG0488 460 TNHLDIETLEALEEALDD-FP---GTVLLVSHDryfLDR---VATRILEF--EDGGV 507
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-208 |
3.58e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYPGVTPVhalDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA-RPGPER-- 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVV---EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISlLPLHARar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ---GVVFQEAALFPWLNVWENVVFGPKI-AGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR 153
Cdd:PRK10895 78 rgiGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLlsvwQTLRTT---VVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRII----EHLRDSglgVLITDHNVRETLAVCERAYIVS 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-215 |
4.10e-22 |
|
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: 89.92 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 2 SHISVTQLSKTYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSG--GELRVGGgavaRPGPER-- 77
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING----RPLDKRsf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ----GVVFQEAALFPWLNVWENVVFGPKIAGLSrreyaaraeemleitglsafkrhlpvqlsGGMRQRVGIARVLTLGSR 153
Cdd:cd03213 81 rkiiGYVPQDDILHPTLTVRETLMFAAKLRGLS-----------------------------GGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDI-DEAILLADTIYVMSarPGRIA 215
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPsSEIFELFDKLLLLS--QGRVI 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-207 |
4.86e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARpgpergvvFQE 83
Cdd:PRK11160 339 LTLNNVSFTYPD-QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD--------YSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 AALFPWLNVwenvvfgpkiagLSRREY---------------AARAEEMLEI-------------TGLSAFKRHLPVQLS 135
Cdd:PRK11160 410 AALRQAISV------------VSQRVHlfsatlrdnlllaapNASDEALIEVlqqvgleklleddKGLNAWLGEGGRQLS 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 136 GGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTlrTTVVFVTHdidEAILLA--DTIYVM 207
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITH---RLTGLEqfDRICVM 546
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-220 |
4.92e-22 |
|
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: 90.89 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAP----SGGELRVGG---GAVARPGPERGVVFQE--AALFPWLN 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGrplLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHL---PVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQT 168
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 169 RLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRIATRIEV 220
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIVERGTV 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-207 |
9.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTPVhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----G 78
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkhiG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAA-LFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAiLLADTIYVM 207
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVM 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-214 |
9.95e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 12 TYPGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGVVF-----Q 82
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerrRLGVAYipedrL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWLNVWENVVFG----PKIAG---LSRREYAARAEEMLEitglsAFK-----RHLPV-QLSGGMRQRVGIARVLT 149
Cdd:COG3845 344 GRGLVPDMSVAENLILGryrrPPFSRggfLDRKAIRAFAEELIE-----EFDvrtpgPDTPArSLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 150 LGSRVLLMDEPFGALDAQTRLTMQELLLSvwqtLR---TTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGAIEFIHQRLLE----LRdagAAVLLISEDLDEILALSDRIAVMYE--GRI 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-233 |
1.55e-21 |
|
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: 92.97 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISvtqlsKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEaPSG---GELRVGGGAVA----RP 73
Cdd:TIGR02633 4 MKGIV-----KTFGGVK---ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKasniRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 74 GPERGVVF--QEAALFPWLNVWENVVFGPKIA-GLSRREYAA---RAEEMLEITGLSAFKRHLPV-QLSGGMRQRVGIAR 146
Cdd:TIGR02633 75 TERAGIVIihQELTLVPELSVAENIFLGNEITlPGGRMAYNAmylRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 147 VLTLGSRVLLMDEPFGALDAQTrltmQELLLSVWQTLR---TTVVFVTHDIDEAILLADTIYVMsaRPGR-IATRIEVPI 222
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKE----TEILLDIIRDLKahgVACVYISHKLNEVKAVCDTICVI--RDGQhVATKDMSTM 228
|
250
....*....|.
gi 565781182 223 ERPRSLDLITG 233
Cdd:TIGR02633 229 SEDDIITMMVG 239
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-192 |
1.73e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.71 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 23 DQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPErgvvFQEAALF--------PWLNVWE 94
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQDLLYlghqpgikTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 95 NVVFGPKIAGLSRREYAARAeemLEITGLSAFKrHLPV-QLSGGMRQRVGIARvLTLGSRVL-LMDEPFGALDAQTRLTM 172
Cdd:PRK13538 94 NLRFYQRLHGPGDDEALWEA---LAQVGLAGFE-DVPVrQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAIDKQGVARL 168
|
170 180
....*....|....*....|..
gi 565781182 173 QELLLsvwQTLRT--TVVFVTH 192
Cdd:PRK13538 169 EALLA---QHAEQggMVILTTH 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-207 |
2.42e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.37 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 11 KTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------GVVFQEA 84
Cdd:PRK10762 12 KAFPGV---KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagiGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 85 ALFPWLNVWENVVFG----PKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:PRK10762 89 NLIPQLTIAENIFLGrefvNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 565781182 161 FGAL-DAQTrltmqELLLSVWQTLRTT---VVFVTHDIDEAILLADTIYVM 207
Cdd:PRK10762 169 TDALtDTET-----ESLFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVF 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-143 |
2.85e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.49 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGpERGVVFQE 83
Cdd:NF033858 2 ARLEGVSHRYGKTV---ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR-HRRAVCPR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 84 AA---------LFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVG 143
Cdd:NF033858 78 IAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-217 |
3.34e-21 |
|
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: 88.83 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG---GAVARPGPER--GVVFQEAALFpwlN--VWE 94
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRaiGVVPQDTVLF---NdtIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 95 NVVFGPKIAGLSRREYAARAEEMLE-ITGLSaFK-------RHLpvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDA 166
Cdd:cd03253 94 NIRYGRPDATDEEVIEAAKAAQIHDkIMRFP-DGydtivgeRGL--KLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 565781182 167 QTRLTMQELLLSVWQtlRTTVVFVTHDIDEaILLADTIYVMSArpGRIATR 217
Cdd:cd03253 171 HTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKD--GRIVER 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-215 |
5.20e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 15 GVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGVVF-----QEAA 85
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdaiRAGIAYvpedrKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 86 LFPWLNVWENVVFG--PKIAG---LSRREYAARAEEMLEITGLSAFKRHLPVQ-LSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:COG1129 341 LVLDLSIRENITLAslDRLSRgglLDRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 160 PFGALDAQTRLTMQELLlsvwQTLR---TTVVFVTHDIDEAILLADTIYVMSArpGRIA 215
Cdd:COG1129 421 PTRGIDVGAKAEIYRLI----RELAaegKAVIVISSELPELLGLSDRILVMRE--GRIV 473
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-217 |
9.71e-21 |
|
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: 90.65 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG------------GAVarpgperGVVFQEAALFpw 89
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslrAAI-------GIVPQDTVLF-- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 90 lN--VWENVVFGPkiAGLSRRE--YAARAEEmleitgLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRV 154
Cdd:COG5265 445 -NdtIAYNIAYGR--PDASEEEveAAARAAQ------IHDFIESLPdgydtrvgergLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTlRTTVVF------VTHdideaillADTIYVMSArpGRIATR 217
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVARG-RTTLVIahrlstIVD--------ADEILVLEA--GRIVER 573
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-208 |
1.01e-20 |
|
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: 84.81 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAvarpgpergvvfqe 83
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 aalfpwlnvwenvvfgpKIAglsrreyaaraeemleitglsafkrHLPvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGA 163
Cdd:cd03221 64 -----------------KIG-------------------------YFE-QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 565781182 164 LDAQTRLTMQELLlsvwQTLRTTVVFVTHD---IDEailLADTIYVMS 208
Cdd:cd03221 101 LDLESIEALEEAL----KEYPGTVILVSHDryfLDQ---VATKIIELE 141
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-204 |
1.23e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 6 VTQLSKTYPGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV-----------ARPG 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidaIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 PERGVVFQEAALFPWLNVWENVVFGPKIAGLS-RREYAARAEEMLEITGL--SAFKR-HLPV-QLSGGMRQRVGIARVLT 149
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkEVYDRlNSPAsQLSGGQQQRLTIARALA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 150 LGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLrtTVVFVTHDIDEAILLADTI 204
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-224 |
1.38e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPgpERGV---------VFQ--EAALFpWL 90
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS--KRGLlalrqqvatVFQdpEQQIF-YT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWENVVFGPKIAGLSRREYAARAEEMLEITGLSAFkRHLPVQ-LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTR 169
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 170 LTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVM-------SARPGRIATRIEVpIER 224
Cdd:PRK13638 173 TQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLrqgqiltHGAPGEVFACTEA-MEQ 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-214 |
5.73e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 85.27 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER------GVVFQEAALFPWLNVW 93
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHEraragiAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 94 ENVVFGpkIAGLSRREyAARAEEMLEI-TGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTM 172
Cdd:TIGR03410 94 ENLLTG--LAALPRRS-RKIPDEIYELfPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565781182 173 QELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:TIGR03410 171 GRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMER--GRV 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-207 |
6.35e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.07 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER--------GVVFQE--AALFPWL 90
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwravrsdiQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWENV-----VFGPKiagLSRREYAARAEEMLEITGL--SAFKRHlPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGA 163
Cdd:PRK15079 116 TIGEIIaeplrTYHPK---LSRQEVKDRVKAMMLKVGLlpNLINRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 565781182 164 LDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-167 |
1.63e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.31 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE--RGVVF--QEAALFPWLNVWENVV 97
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYlgHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 98 FGPKIAGlsrreyAARAEEMLEITGLSAFKrHLPV-QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQ 167
Cdd:cd03231 96 FWHADHS------DEQVEEALARVGLNGFE-DRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-194 |
4.81e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 6 VTQLSKTYPG--------VTPVHALDQIDLQVAEGEFVALLGPSGCGKST----LLNLIAgfeapSGGELRVGGGAVARP 73
Cdd:PRK15134 278 VEQLQVAFPIrkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 74 GPER--------GVVFQE--AALFPWLNVWENVVFGPKI--AGLSRREYAARAEEMLEITGLSAFKRH-LPVQLSGGMRQ 140
Cdd:PRK15134 353 NRRQllpvrhriQVVFQDpnSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQ 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 141 RVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDI 194
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDL 486
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-193 |
8.07e-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: 84.99 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 9 LSKTYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGElrvgggAVARPGPERGVVFQEAALFP 88
Cdd:TIGR03719 10 VSKVVPPKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE------ARPQPGIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 WLNVWENVVFG-PKIAGLSRR-------------EYAARAEEMLEI------TGLSAFKRHL--------------PVQ- 133
Cdd:TIGR03719 82 TKTVRENVEEGvAEIKDALDRfneisakyaepdaDFDKLAAEQAELqeiidaADAWDLDSQLeiamdalrcppwdaDVTk 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 134 LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLlsvwQTLRTTVVFVTHD 193
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-209 |
1.17e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 83.25 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTY-PGVTPVHALDQIDLQVAEGEFVALLGPSGCGKS----TLLNLIAGFEAPSGGELRVGGGAVAR--- 72
Cdd:PRK11022 1 MALLNVDKLSVHFgDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRise 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 73 ------PGPERGVVFQEA--ALFPWLNVWENVVFGPKI-AGLSRREYAARAEEMLEITGLSAFKRHL---PVQLSGGMRQ 140
Cdd:PRK11022 81 kerrnlVGAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 141 RVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-192 |
1.79e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVF--QEAALFPWLNVWENVVFG 99
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlgHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 100 PKIAGlsrrEYAARAEEMLEITGLSAFKrHLPVQ-LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTrltmQELLLS 178
Cdd:PRK13539 98 AAFLG----GEELDIAAALEAVGLAPLA-HLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA----VALFAE 168
|
170
....*....|....*..
gi 565781182 179 VWQTLRT---TVVFVTH 192
Cdd:PRK13539 169 LIRAHLAqggIVIAATH 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-233 |
2.19e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 5 SVTQLSKTYPGVTPVHALDqidLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE---RGVVF 81
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLS---LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 82 --QEAALFPWLNVWENVVFG--PKIAGLSR--REYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVL 155
Cdd:PRK10575 90 lpQQLPAAEGMTVRELVAIGryPWHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 156 LMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADtiYVMSARPGR-IATRIEVPIERPRSLDLITG 233
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCD--YLVALRGGEmIAQGTPAELMRGETLEQIYG 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-214 |
2.56e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 8 QLSKTYPGVTPVHALDqidLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQ 82
Cdd:PRK10253 12 QLTLGYGKYTVAENLT---VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWLNVWENVVFG--PKIAGLSR--REYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:PRK10253 89 NATTPGDITVQELVARGryPHQPLFTRwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 159 EPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLAdtIYVMSARPGRI 214
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYA--SHLIALREGKI 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-207 |
4.13e-18 |
|
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: 80.07 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAG-FEAPSG-----GELRVGGGAVARPGPERGVVfQEAALFPWL---NV 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGkvhwsNKNESEPSFEATRSRNRYSV-AYAAQKPWLlnaTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 93 WENVVFGpkiAGLSRREYAAraeeMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:cd03290 96 EENITFG---SPFNKQRYKA----VTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 565781182 162 GALDAQ-TRLTMQELLLSVWQTLRTTVVFVTHDIdEAILLADTIYVM 207
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAM 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-207 |
4.39e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 18 PVHALDQIDLQVAEGEFVALLGPSGCGKS-TLLNLIAGFEApSGGELRVGGGAVARP-------------------GPER 77
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRRsrqvielseqsaaqmrhvrGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQE--AALFPWLNVWENVVFGPKI-AGLSRREYAARAEEMLE---ITGLSAFKRHLPVQLSGGMRQRVGIARVLTLG 151
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDqvrIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 152 SRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-202 |
4.64e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLL-------NLIAGFEapSGGELRVGGGA------V 70
Cdd:PRK14271 22 MAAVNLTLGFAGKT---VLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYR--YSGDVLLGGRSifnyrdV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 71 ARPGPERGVVFQEAALFPwLNVWENVVFGPKIAGL-SRREYAARAEEMLEITGL-SAFKRHL---PVQLSGGMRQRVGIA 145
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 146 RVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQtlRTTVVFVTHDIDEAILLAD 202
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISD 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-217 |
6.20e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.59 E-value: 6.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFeAPSGGELRVGGGAVARPGPER-----GVVFQEAALFPWlNVWENV 96
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrkhlSWVGQNPQLPHG-TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 97 VFGPKIAGlsrreyAARAEEMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALD 165
Cdd:PRK11174 444 LLGNPDAS------DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565781182 166 AQT-RLTMQElLLSVWQtlRTTVVFVTHDIDEaILLADTIYVMsaRPGRIATR 217
Cdd:PRK11174 518 AHSeQLVMQA-LNAASR--RQTTLMVTHQLED-LAQWDQIWVM--QDGQIVQQ 564
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-215 |
7.13e-18 |
|
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: 82.10 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:COG4618 330 RLSVENLTVVPPG-SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgrhi 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPWlNVWENvvfgpkIAGLSrreyAARAEEMLE---ITGLSAFKRHLP-----------VQLSGGMRQRVG 143
Cdd:COG4618 409 GYLPQDVELFDG-TIAEN------IARFG----DADPEKVVAaakLAGVHEMILRLPdgydtrigeggARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 144 IARVLTLGSRVLLMDEPFGALDAQTRLTMQELLlsvwQTLR---TTVVFVTHDIdEAILLADTIYVMsaRPGRIA 215
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAI----RALKargATVVVITHRP-SLLAAVDKLLVL--RDGRVQ 545
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-208 |
1.07e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.85 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 32 GEFVALLGPSGCGKSTLLNLIAGFEAPSG--GELRVGGGAVARPGPER-GVVFQEAALFPWLNVWENVVFG-----PKia 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETLVFCsllrlPK-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 104 GLSRREYAARAEEMLEITGLS---------AFKRhlpvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQE 174
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTkcentiignSFIR----GISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190
....*....|....*....|....*....|....
gi 565781182 175 LLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLS 281
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-188 |
1.78e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 13 YPGVTPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG---GAVARPGPER--GVVFQEAALF 87
Cdd:PRK13657 344 YDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRniAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 88 PwLNVWENVVFGPKIAGLSRREYAARAEEMLE-----ITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:PRK13657 422 N-RSIEDNIRVGRPDATDEEMRAAAERAQAHDfierkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180
....*....|....*....|....*.
gi 565781182 163 ALDAQTRLTMQELLLSVWQTlRTTVV 188
Cdd:PRK13657 501 ALDVETEAKVKAALDELMKG-RTTFI 525
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-216 |
2.14e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.60 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISvtqlsKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEaPSG---GELRVGGGAVA----RP 73
Cdd:NF040905 4 MRGIT-----KTFPGV---KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRfkdiRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 74 GPERGVVF--QEAALFPWLNVWENVVFGPKIA--GL-SRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVL 148
Cdd:NF040905 75 SEALGIVIihQELALIPYLSIAENIFLGNERAkrGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 149 TLGSRVLLMDEPFGAL---DAQTRLtmqELLLSvwqtLRT---TVVFVTHDIDEAILLADTIYVMsaRPGR-IAT 216
Cdd:NF040905 155 SKDVKLLILDEPTAALneeDSAALL---DLLLE----LKAqgiTSIIISHKLNEIRRVADSITVL--RDGRtIET 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-193 |
3.11e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.55 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 9 LSKTYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGElrvgggAVARPGPERGVVFQEAALFP 88
Cdd:PRK11819 12 VSKVVPPKKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE------ARPAPGIKVGYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 WLNVWENVV--FGPKIAGLSRRE--YAARAEEMLEITGLSAFKRHL------------------------------PV-Q 133
Cdd:PRK11819 84 EKTVRENVEegVAEVKAALDRFNeiYAAYAEPDADFDALAAEQGELqeiidaadawdldsqleiamdalrcppwdaKVtK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 134 LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQtrltmqelllSV-W--QTLRT---TVVFVTHD 193
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE----------SVaWleQFLHDypgTVVAVTHD 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-193 |
7.68e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.21 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGggavarPGPERGVVFQE-AALFPWLNVWENVVFGP 100
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------ETVKLAYVDQSrDALDPNKTVWEEISGGL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 101 KIAGLSRREYAARAEemleitgLSAF--------KRhlpV-QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLT 171
Cdd:TIGR03719 412 DIIKLGKREIPSRAY-------VGRFnfkgsdqqKK---VgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
170 180
....*....|....*....|..
gi 565781182 172 MQELLLSvwqtLRTTVVFVTHD 193
Cdd:TIGR03719 482 LEEALLN----FAGCAVVISHD 499
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-215 |
8.40e-17 |
|
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: 79.31 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYP-GVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-----PGPE 76
Cdd:TIGR01842 316 HLSVENVTIVPPgGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwdretFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 77 RGVVFQEAALFPWlNVWENVvfgpkiaglSRREYAARAEEMLE---ITGLSAFKRHLP-----------VQLSGGMRQRV 142
Cdd:TIGR01842 394 IGYLPQDVELFPG-TVAENI---------ARFGENADPEKIIEaakLAGVHELILRLPdgydtvigpggATLSGGQRQRI 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 143 GIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVwQTLRTTVVFVTHDIdEAILLADTIYVMSArpGRIA 215
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRP-SLLGCVDKILVLQD--GRIA 532
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-213 |
8.87e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 23 DQIDLQVAEGEFVALLGPSGCGKS-TLLNLIAGFEAPS----GGELRVGGGAV--ARPGPERGV-------VFQE--AAL 86
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhASEQTLRGVrgnkiamIFQEpmVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 87 FPWLNVWENVVfgpKIAGLSR--REYAARAEEM--LEITGLSAFKRHL---PVQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:PRK15134 106 NPLHTLEKQLY---EVLSLHRgmRREAARGEILncLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 160 PFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMsaRPGR 213
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QNGR 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-217 |
9.82e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.08 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVtpvHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEA--PSGGEL--RVG----GGAVARPG- 74
Cdd:TIGR03269 1 IEVKNLTKKFDGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyHVAlcekCGYVERPSk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 ------------------------PER-------GVVFQEA-ALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEITG 122
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfwnlsdKLRrrirkriAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 123 LSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTH------DI-D 195
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLsD 237
|
250 260
....*....|....*....|..
gi 565781182 196 EAILLADTIYVMSARPGRIATR 217
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-214 |
9.97e-17 |
|
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: 76.36 E-value: 9.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYPGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlhskv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPwLNVWENVVFGPKIAGLSRREYAARAeemleiTGLSAFKRHLP-----------VQLSGGMRQRVGIAR 146
Cdd:cd03248 91 SLVGQEPVLFA-RSLQDNIAYGLQSCSFECVKEAAQK------AHAHSFISELAsgydtevgekgSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 147 VLTLGSRVLLMDEPFGALDAQTRLTMQElLLSVWQTlRTTVVFVTHDIdEAILLADTIYVMSArpGRI 214
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQ-ALYDWPE-RRTVLVIAHRL-STVERADQILVLDG--GRI 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-212 |
9.44e-16 |
|
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: 73.98 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 13 YPGVTPVHALDQIDLQVAEGEF-----VALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA---------RPGPERG 78
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikadYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPWLNVWENVVFGPkiaglsrreyaaraeemLEITGLsaFKRHLPvQLSGGMRQRVGIARVLTLGSRVLLMD 158
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKP-----------------LQIEQI--LDREVP-ELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 159 EPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPG 212
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-192 |
1.05e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.00 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAG---FeapsggelrvGGGAVARPGPERgVVF--Q----------EAAL 86
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpY----------GSGRIARPAGAR-VLFlpQrpylplgtlrEALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 87 FPwlnvwenvvfgpkiagLSRREYA-ARAEEMLEITGLSAFKRHLPVQ------LSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:COG4178 448 YP----------------ATAEAFSdAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|....
gi 565781182 160 PFGALDAQTRLTMQELLLsvwQTLR-TTVVFVTH 192
Cdd:COG4178 512 ATSALDEENEAALYQLLR---EELPgTTVISVGH 542
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-207 |
1.06e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYPGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE---RGV 79
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlrQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 --VFQEAALFPwLNVWENVVFGPKIAglsrreyAARAEEMLEITGLSAFKRHLPV-----------QLSGGMRQRVGIAR 146
Cdd:PRK10790 418 amVQQDPVVLA-DTFLANVTLGRDIS-------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 147 VLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQtlRTTVVFVTHDIdEAILLADTIYVM 207
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRL-STIVEADTILVL 547
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-214 |
1.24e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 17 TPVHALDQIDLQVAEGEFVALLGPSGCGKS-----TLLNLIAGFEApSGGELRVGGGAVArPGPERG----VVFQ--EAA 85
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVA-PCALRGrkiaTIMQnpRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 86 LFPWLNVWENVVFGPKIAGLSRREyaARAEEMLEITGLSAFKRHL---PVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 163 ALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGRI 214
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRI 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-192 |
3.41e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 12 TYPGVTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgavaRPGPER---------GVVFQ 82
Cdd:TIGR00958 487 SYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG----VPLVQYdhhylhrqvALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPWlNVWENVVFGPKIAGLSRREYAARAeemleiTGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLG 151
Cdd:TIGR00958 563 EPVLFSG-SVRENIAYGLTDTPDEEIMAAAKA------ANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565781182 152 SRVLLMDEPFGALDAQTRLTMQElllsvWQTLRT-TVVFVTH 192
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQE-----SRSRASrTVLLIAH 672
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-231 |
4.04e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.28 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTYPGV-TPvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG------------GA 69
Cdd:PRK11176 341 DIEFRNVTFTYPGKeVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 70 VArpgpergVVFQEAALFpwlnvweNVVFGPKIAGLSRREY-------AARAEEMLEitglsaFKRHLP----------- 131
Cdd:PRK11176 419 VA-------LVSQNVHLF-------NDTIANNIAYARTEQYsreqieeAARMAYAMD------FINKMDngldtvigeng 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 132 VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVwQTLRTTVVfVTHDIdEAILLADTIYVMSArp 211
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLV-IAHRL-STIEKADEILVVED-- 553
|
250 260
....*....|....*....|
gi 565781182 212 GRIatrievpIERPRSLDLI 231
Cdd:PRK11176 554 GEI-------VERGTHAELL 566
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-194 |
6.14e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 19 VHALDQIDLQVAEGEFVALLGPSGCGKST----LLNLIAGfeapSGGELRVGGGAVARPGPER--------GVVFQE--A 84
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVES----QGGEIIFNGQRIDTLSPGKlqalrrdiQFIFQDpyA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 85 ALFPWLNVWENVVFGPKIAGLSRREYAA-RAEEMLEITGL-SAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFG 162
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|..
gi 565781182 163 ALDAQTRLTMQELLLSVWQTLRTTVVFVTHDI 194
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
22-200 |
7.38e-15 |
|
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: 73.44 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQEAALFPW-----LN 91
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlansvAMVDQDIFLFEGtvrdnLT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVfgpKIAGLSRreyAARAEEMLEITGLSAFKRHLPV-----QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDA 166
Cdd:TIGR03796 575 LWDPTI---PDADLVR---ACKDAAIHDVITSRPGGYDAELaeggaNLSGGQRQRLEIARALVRNPSILILDEATSALDP 648
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 167 QTRltmqellLSVWQTLR---TTVVFVTH------DIDEAILL 200
Cdd:TIGR03796 649 ETE-------KIIDDNLRrrgCTCIIVAHrlstirDCDEIIVL 684
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-176 |
7.74e-15 |
|
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: 71.15 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 27 LQVAEGEFVALLGPSGCGKSTLLNLIAGfEAPSGGELRvggGAVARPGPER---------GVVFQEAALFPWLNVWENVV 97
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTS---GQILFNGQPRkpdqfqkcvAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 98 FGPKIAgLSRREYAARAEEMLEITGLSAFK----RH-LPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTM 172
Cdd:cd03234 104 YTAILR-LPRKSSDAIRKKRVEDVLLRDLAltriGGnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
....
gi 565781182 173 QELL 176
Cdd:cd03234 183 VSTL 186
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-194 |
1.27e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.39 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgavarpgpERGVVFQEAALFPWLNVWENVVFG 99
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVIAISAGLSGQLTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 100 PKIAGLSRREYAARAEEMLEITGLSAFKrHLPVQ-LSGGMRQRVGIARVLTLGSRVLLMDEpfgALDAQTRLTMQELLLS 178
Cdd:PRK13546 110 MLCMGFKRKEIKAMTPKIIEFSELGEFI-YQPVKkYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDK 185
|
170
....*....|....*...
gi 565781182 179 VWQ--TLRTTVVFVTHDI 194
Cdd:PRK13546 186 IYEfkEQNKTIFFVSHNL 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-209 |
1.34e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFeAPSGGELRVGGGAVAR-PGPE----RGVVFQEAALFPWLNVWENV 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwSAAElarhRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 97 -VFGPkiAGLSRREYAARAEEMLEITGLSAfKRHLPV-QLSGGMRQRVGIARVL-------TLGSRVLLMDEPFGALD-A 166
Cdd:COG4138 91 aLHQP--AGASSEAVEQLLAQLAEALGLED-KLSRPLtQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDEPMNSLDvA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 565781182 167 QtrltmQELLLSVWQTLRT---TVVFVTHDIDEAILLADTIYVMSA 209
Cdd:COG4138 168 Q-----QAALDRLLRELCQqgiTVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-208 |
1.35e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAG----FEAPSG----GELRVGGGAVARPGPE-----RGVVFQEA-ALF 87
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAIDAPrlarlRAVLPQAAqPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 88 PWlNVWENVVFG----PKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVL---------TLGSRV 154
Cdd:PRK13547 97 AF-SAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 155 LLMDEPFGALDaqtrLTMQELLLSVWQTL----RTTVVFVTHDIDEAILLADTIYVMS 208
Cdd:PRK13547 176 LLLDEPTAALD----LAHQHRLLDTVRRLardwNLGVLAIVHDPNLAARHADRIAMLA 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-207 |
2.19e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPErgvVFQE 83
Cdd:TIGR01257 1938 LRLNELTKVYSG-TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 AALFPWLNVWENVVFGPKIAGLSRREYAARAEEMLEIT-------GLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLL 156
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVAnwsiqslGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 565781182 157 MDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVM 207
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIM 2143
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-195 |
2.65e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGfeapsggelrvgggaVARPGPERGVVfqeaaLFPWLNVWENVvfg 99
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---------------ALKGTPVAGCV-----DVPDNQFGREA--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 100 PKIAGLSRREYAARAEEMLEITGLS--AFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLL 177
Cdd:COG2401 101 SLIDAIGRKGDFKDAVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*...
gi 565781182 178 SVWQTLRTTVVFVTHDID 195
Cdd:COG2401 181 KLARRAGITLVVATHHYD 198
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-213 |
4.10e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 17 TP---VHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGgelRVGGGAVARPG-----PER----------G 78
Cdd:PRK09473 24 TPdgdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSATFNGReilnlPEKelnklraeqiS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQE--AALFPWLNVWEN---VVFGPKiaGLSRREYAARAEEMLEITGL-SAFKR--HLPVQLSGGMRQRVGIARVLTL 150
Cdd:PRK09473 101 MIFQDpmTSLNPYMRVGEQlmeVLMLHK--GMSKAEAFEESVRMLDAVKMpEARKRmkMYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 151 GSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSArpGR 213
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA--GR 239
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-208 |
5.07e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.13 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPgpergvvfQEAalfpWL---NVWENVVF 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVP--------QQA----WIqndSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 GpkiAGLSRREYaaraEEMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQ 167
Cdd:TIGR00957 722 G---KALNEKYY----QQVLEACALLPDLEILPsgdrteigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565781182 168 TRLTMQELLLSVWQTLRT-TVVFVTHDIdEAILLADTIYVMS 208
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKNkTRILVTHGI-SYLPQVDVIIVMS 835
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-168 |
6.28e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 35 VALLGPSGCGKSTLLNLIAGFEAPSGGELRVGggavarPGPERGVVFQE-AALFPWLNVWENVVFGPKIAGLSRREYAAR 113
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG------ETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKVGNREIPSR 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565781182 114 AEemleitgLSAF--------KRhlpV-QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQT 168
Cdd:PRK11819 427 AY-------VGRFnfkggdqqKK---VgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-168 |
6.49e-14 |
|
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: 71.09 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 16 VTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGpergvvfqeaalFPWL---NV 92
Cdd:TIGR01271 438 VTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWImpgTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 93 WENVVFGpkiagLSRREYAAR----AEEMLEITGLSAFKRHLP-----VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGA 163
Cdd:TIGR01271 504 KDNIIFG-----LSYDEYRYTsvikACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
....*
gi 565781182 164 LDAQT 168
Cdd:TIGR01271 579 LDVVT 583
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-215 |
1.89e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 25 IDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGVVF-----QEAALFPWLNVWEN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdaiRAGIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 V---------VFGPKIAGLSRREYAARAEEMLEITGLSAfkRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDA 166
Cdd:PRK11288 352 InisarrhhlRAGCLINNRWEAENADRFIRSLNIKTPSR--EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 565781182 167 QTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVMsaRPGRIA 215
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVM--REGRIA 475
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-217 |
2.38e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 12 TYPGVTPVhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE--RG---VVFQEAAL 86
Cdd:PRK10789 322 TYPQTDHP-ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSrlaVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 87 FPwLNVWENVVFGPKIAGLSRREYAARA----EEMLEI-TGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:PRK10789 401 FS-DTVANNIALGRPDATQQEIEHVARLasvhDDILRLpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 162 GALDAQTRltmQELL--LSVWQTLRtTVVFVTHDIdEAILLADTIYVMSArpGRIATR 217
Cdd:PRK10789 480 SAVDGRTE---HQILhnLRQWGEGR-TVIISAHRL-SALTEASEILVMQH--GHIAQR 530
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-207 |
3.52e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYpgvTPVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER--- 77
Cdd:PRK11614 3 KVMLSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ---GVVFQEAALFPWLNVWENVVFGPKIAglSRREYAARAEEMLEITGLSAFKRHLPV-QLSGGMRQRVGIARVLTLGSR 153
Cdd:PRK11614 80 eavAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 154 VLLMDEPfgALDAQTRLTMQelLLSVWQTLRT---TVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK11614 158 LLLLDEP--SLGLAPIIIQQ--IFDTIEQLREqgmTIFLVEQNANQALKLADRGYVL 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-192 |
5.50e-13 |
|
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: 64.87 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGfeapsggeL-RVGGGAVARPGPErGVVF------------QEAALFP 88
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--------LwPWGSGRIGMPEGE-DLLFlpqrpylplgtlREQLIYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 WLNVwenvvfgpkiaglsrreyaaraeemleitglsafkrhlpvqLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQT 168
Cdd:cd03223 88 WDDV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....
gi 565781182 169 RLTMQELLlsvwQTLRTTVVFVTH 192
Cdd:cd03223 127 EDRLYQLL----KELGITVISVGH 146
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-217 |
6.94e-13 |
|
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: 65.24 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEA--PSGGELRVGGGAVARPGP-ER-----GVVFQEaalfPwlnvw 93
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeERarlgiFLAFQY----P----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 94 envvfgPKIAGLSrreyaaraeemleitgLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAqTRLTMQ 173
Cdd:cd03217 87 ------PEIPGVK----------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 565781182 174 ELLLSVWQTLRTTVVFVTH--DIDEAIlLADTIYVMSArpGRIATR 217
Cdd:cd03217 144 AEVINKLREEGKSVLIITHyqRLLDYI-KPDRVHVLYD--GRIVKS 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-193 |
7.34e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 28 QVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGG-AVARPGPERgvvfqeAALFPWLNVWENVVFGPK---IA 103
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQHR------AELDPEKTVMDNLAEGKQevmVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 104 GLSRreyaaraeemlEITG-LSAF----KRHL-PVQ-LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTrLTMQELL 176
Cdd:PRK11147 415 GRPR-----------HVLGyLQDFlfhpKRAMtPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-LELLEEL 482
|
170
....*....|....*..
gi 565781182 177 LSVWQtlrTTVVFVTHD 193
Cdd:PRK11147 483 LDSYQ---GTVLLVSHD 496
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-207 |
8.36e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.85 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 18 PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPS----GGELRVGGGAVAR-PGPER--------GVVFQE- 83
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKlSPRERrkiigreiAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 -AALFPWLNVWENVVFG-PKIAGLSR-----REYAARAEEMLEITGLSAFKRHL---PVQLSGGMRQRVGIARVLTLGSR 153
Cdd:COG4170 99 sSCLDPSAKIGDQLIEAiPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-215 |
1.32e-12 |
|
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: 64.82 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 3 HISVTQLSKTY-PGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER---- 77
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 -GVVFQEAALFPWlNVWENV-VFGpkiaglsrrEYA-ARAEEMLEITGLSAFKRHLPVQL-----------SGGMRQRVG 143
Cdd:cd03244 80 iSIIPQDPVLFSG-TIRSNLdPFG---------EYSdEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565781182 144 IARVLTLGSRVLLMDEPFGALDAQTRLTMQelllsvwQTLRT-----TVVFVTHDIDeAILLADTIYVMSArpGRIA 215
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQ-------KTIREafkdcTVLTIAHRLD-TIIDSDRILVLDK--GRVV 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-209 |
2.75e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVT------PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGG-----GAVAR 72
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 73 PGPERGVVFQEA--ALFPWLNVWENVVFGPKI-AGLSRREYAARAEEMLEITGLSA-FKRHLPVQLSGGMRQRVGIARVL 148
Cdd:PRK15112 85 RSQRIRMIFQDPstSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565781182 149 TLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-165 |
8.33e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 25 IDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVF--QEAALFPWLNVWENVVFgpkI 102
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYlgHLPGLKADLSTLENLHF---L 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565781182 103 AGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALD 165
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-168 |
8.69e-12 |
|
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: 63.34 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 16 VTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPgpergvvfQEAALFPWlNVWEN 95
Cdd:cd03291 49 GAPV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS--------QFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 VVFGpkiagLSRREY-------AARAEEmleitGLSAF--KRHLP-----VQLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:cd03291 118 IIFG-----VSYDEYryksvvkACQLEE-----DITKFpeKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
....*..
gi 565781182 162 GALDAQT 168
Cdd:cd03291 188 GYLDVFT 194
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-172 |
9.93e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVA--RPGPERGVVF--QEAALFPWLNVWENVV 97
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdLCTYQKQLCFvgHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 98 FgpkiaGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTM 172
Cdd:PRK13540 97 Y-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-168 |
1.17e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAvarpgperGVVFQEAALFPWLNVWENVVFG 99
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--------ALIAISSGLNGQLTGIENIELK 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 100 PKIAGLSRREYAARAEEMLEITGLSAFKrHLPVQ-LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDaQT 168
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADIGKFI-YQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGD-QT 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-194 |
1.50e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTY-PGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVF- 81
Cdd:PRK15056 7 IVVNDVTVTWrNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 82 -QEAAL---FPWLnvWENVVFGPKIA--GLSRREYA---ARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGS 152
Cdd:PRK15056 84 pQSEEVdwsFPVL--VEDVVMMGRYGhmGWLRRAKKrdrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565781182 153 RVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVfVTHDI 194
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNL 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-193 |
1.61e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 1 MSHISVTQLSKTYpGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGG-AVAR-----PG 74
Cdd:PRK11147 1 MSLISIHGAWLSF-SDAPL--LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARlqqdpPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 75 PERGVVF-------QEAA--LFPWLNVWENVVFGPKIAGLSRreyAARAEEMLEITGLSAF---------KRHLP----- 131
Cdd:PRK11147 78 NVEGTVYdfvaegiEEQAeyLKRYHDISHLVETDPSEKNLNE---LAKLQEQLDHHNLWQLenrinevlaQLGLDpdaal 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 132 VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSvwqtLRTTVVFVTHD 193
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHD 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-217 |
2.27e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 7 TQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV----ARPGPERGV--V 80
Cdd:PRK10982 2 SNISKSFPGVK---ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGIsmV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 FQEAALFPWLNVWENVVFG--PKIAGLSRREYAAR-AEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLM 157
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 158 DEPfgaldaQTRLTMQEL--LLSVWQTLRTT---VVFVTHDIDEAILLADTIYVMsaRPGR-IATR 217
Cdd:PRK10982 159 DEP------TSSLTEKEVnhLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITIL--RDGQwIATQ 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-215 |
3.75e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.37 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 31 EGEFVALLGPSGCGKSTLLNLIAGFEAPS---GGELRVGGGAVARPGPER--GVVFQEAALFPWLNVWENVVFGPKI--- 102
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHLMFQAHLrmp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 103 AGLSRREYAARAEEMLEITGLSAfKRHLPVQ-------LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAqtrlTMQEL 175
Cdd:TIGR00955 130 RRVTKKEKRERVDEVLQALGLRK-CANTRIGvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS----FMAYS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 565781182 176 LLSVWQTL---RTTVVFVTHDIDEAIL-LADTIYVMSArpGRIA 215
Cdd:TIGR00955 205 VVQVLKGLaqkGKTIICTIHQPSSELFeLFDKIILMAE--GRVA 246
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
19-207 |
3.80e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.06 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 19 VHALDQIDLQVAEGEFVALLGPSGCGKSTLLnLIAGFEAPSGGE--LRVGGGAVARPGPERGVVFQEAALFPWLNVW--- 93
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrpWRF*TWCANRRALRRTIG*HRPVR*GRRESFsgr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 94 ENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRltmq 173
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR---- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 565781182 174 ellLSVWQTLRT------TVVFVTHDIDEAILLADTIYVM 207
Cdd:NF000106 181 ---NEVWDEVRSmvrdgaTVLLTTQYMEEAEQLAHELTVI 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-189 |
5.28e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAG----FEAPSgGELRVGG--GAVARPGPERGVVF--QEAALFPWLNVW 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGipYKEFAEKYPGEIIYvsEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 94 ENVVFGPKIAGlsrreyaaraeemleitglSAFKRhlpvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQ 173
Cdd:cd03233 102 ETLDFALRCKG-------------------NEFVR----GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170
....*....|....*.
gi 565781182 174 ELLLSVWQTLRTTVVF 189
Cdd:cd03233 159 KCIRTMADVLKTTTFV 174
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-194 |
6.41e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRvgggavaRPGPER-GVVFQEAALFPWLNVwenvvfgp 100
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRiGYVPQKLYLDTTLPL-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 101 KIAGLSRREYAARAEEMLeitglSAFKR----HL---PVQ-LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTM 172
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDIL-----PALKRvqagHLidaPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|..
gi 565781182 173 QELLLSVWQTLRTTVVFVTHDI 194
Cdd:PRK09544 160 YDLIDQLRRELDCAVLMVSHDL 181
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-167 |
7.61e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVArpgpergVVFQEAALFPwLNVWENVVFG 99
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVA-------YVPQVSWIFN-ATVRDNILFG 702
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 100 PKIAglsrreyAARAEEMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQ 167
Cdd:PLN03130 703 SPFD-------PERYERAIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-212 |
1.28e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 29 VAEGEFVALLGPSGCGKSTLLNLIAGFEAPS------------------GGEL-----RVGGG---AVARPgpergvvfQ 82
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwdeildefrGSELqnyftKLLEGdvkVIVKP--------Q 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALFPwlnvweNVVFGPKIAGLSRREYAARAEEMLEITGLS-AFKRHLPvQLSGGMRQRVGIARVLTLGSRVLLMDEPF 161
Cdd:cd03236 95 YVDLIP------KAVKGKVGELLKKKDERGKLDELVDQLELRhVLDRNID-QLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565781182 162 GALDAQTRLTMQELLLSVWQTLRTTVVfVTHDIdeAIL--LADTIYVMSARPG 212
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLV-VEHDL--AVLdyLSDYIHCLYGEPG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-209 |
1.95e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 28 QVAEGEFVALLGPSGCGKSTLLNLIAGFeAPSGGELRVGGGAVAR-PGPE----RGVVFQEAALFPWLNVWENV-VFGPk 101
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwSAAElarhRAYLSQQQTPPFAMPVFQYLtLHQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 102 iAGLSRREYAARAEEMLEITGLSAfKRHLPV-QLSGGMRQRVGIA-------RVLTLGSRVLLMDEPFGALD-AQTRLTM 172
Cdd:PRK03695 96 -DKTRTEAVASALNEVAEALGLDD-KLGRSVnQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDvAQQAALD 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 565781182 173 QelLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSA 209
Cdd:PRK03695 174 R--LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-207 |
2.20e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.82 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 18 PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAP----SGGELRVGGGAVARPGP-ER--------GVVFQE- 83
Cdd:PRK15093 19 WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPrERrklvghnvSMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 -AALFPWLNVWENVVfgPKIAGLS-----------RREyaaRAEEMLEITGLSAFK---RHLPVQLSGGMRQRVGIARVL 148
Cdd:PRK15093 99 qSCLDPSERVGRQLM--QNIPGWTykgrwwqrfgwRKR---RAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 149 TLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-170 |
3.75e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 10 SKTYPGVTPVHALdqidlqVAEGEFVALLGPSGCGKSTLLNLIA----GFEAPSGGELRVGGgavarPGPE------RGV 79
Cdd:TIGR00956 71 TKTFDILKPMDGL------IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG-----ITPEeikkhyRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 80 VFQEAAL---FPWLNVWENVVF-------GPKIAGLSRREYAAR-AEEMLEITGLS---------AFKRhlpvQLSGGMR 139
Cdd:TIGR00956 140 VVYNAETdvhFPHLTVGETLDFaarcktpQNRPDGVSREEYAKHiADVYMATYGLShtrntkvgnDFVR----GVSGGER 215
|
170 180 190
....*....|....*....|....*....|.
gi 565781182 140 QRVGIARVLTLGSRVLLMDEPFGALDAQTRL 170
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-176 |
1.11e-09 |
|
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: 56.10 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPS--GGELRVGGgavaRPGPER-----GVVFQEAALFPWLNVWE 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING----RPLDKNfqrstGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 95 NVVFGPKIAGLSRREyaaraeemleitglsafkrhlpvqlsggmRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQE 174
Cdd:cd03232 99 ALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
..
gi 565781182 175 LL 176
Cdd:cd03232 150 FL 151
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-212 |
1.35e-09 |
|
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: 55.66 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 29 VAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGgavarpgpergvvfqeaalfpwlnvwENVVFGPKIaglsrr 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG--------------------------ITPVYKPQY------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 109 eyaaraeemleitglsafkrhlpVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVV 188
Cdd:cd03222 70 -----------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170 180
....*....|....*....|....
gi 565781182 189 FVTHDIDEAILLADTIYVMSARPG 212
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-160 |
1.82e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAV------ARpgpeRGVVF--QEAALFPWLNV 92
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagdiaTR----RRVGYmsQAFSLYGELTV 356
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565781182 93 WENVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-219 |
2.53e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 79 VVFQEAALFPwLNVWENVVFGPKIAglsRREYAARAEEMLEItglSAFKRHLPVQ-----------LSGGMRQRVGIARV 147
Cdd:PTZ00265 1300 IVSQEPMLFN-MSIYENIKFGKEDA---TREDVKRACKFAAI---DEFIESLPNKydtnvgpygksLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 148 LTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIdEAILLADTIYVMSaRPGRIATRIE 219
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFN-NPDRTGSFVQ 1442
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-219 |
3.52e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 25 IDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGVVF-----QEAALFPWLNVWEN 95
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavKKGMAYitesrRDNGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 VVFGP--KIAGL----------SRREYAARAEEMLEITgLSAFKRHLpVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGA 163
Cdd:PRK09700 362 MAISRslKDGGYkgamglfhevDEQRTAENQRELLALK-CHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 164 LDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVMsaRPGRIATRIE 219
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVF--CEGRLTQILT 492
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-198 |
3.96e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.92 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 32 GEFVALLGPSGCGKSTLLNLIAGFEAPSGGelrvgggavarpgperGVVFQEAALFPWLNVWENVVFGPKIAGLSrreya 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGG----------------GVIYIDGEDILEEVLDQLLLIIVGGKKAS----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 112 araeemleitglsafkrhlpvqLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQEL-----LLSVWQTLRTT 186
Cdd:smart00382 61 ----------------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLT 118
|
170
....*....|..
gi 565781182 187 VVFVTHDIDEAI 198
Cdd:smart00382 119 VILTTNDEKDLG 130
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-167 |
4.21e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARpgpergvvfqeAALFPWL---NVWENVVF 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAY-----------VPQVSWIfnaTVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 GPKIAglSRREYAAraeemLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQ 167
Cdd:PLN03232 702 GSDFE--SERYWRA-----IDVTALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-213 |
7.94e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRvGGGAVA------RPGPER 77
Cdd:COG1245 342 VEYPDLTKSYGGFS----LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISykpqyiSPDYDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVV-FQEAALFPWL--NVWENVVFGPkiAGLsrreyaaraEEMLEitglsafkRHLPvQLSGGMRQRVGIARVLTLGSRV 154
Cdd:COG1245 417 TVEeFLRSANTDDFgsSYYKTEIIKP--LGL---------EKLLD--------KNVK-DLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDI---DeaiLLADTIYVMSARPGR 213
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIyliD---YISDRLMVFEGEPGV 535
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-215 |
8.26e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLL-NLIAGFEAPSGgelrvgggavaRPGPERGVVF--QEAalfpWL---NVWEN 95
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEISEG-----------RVWAERSIAYvpQQA----WImnaTVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 VVFGPKiaglsrrEYAARAEEMLEITGLSAFKRHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGAL 164
Cdd:PTZ00243 741 ILFFDE-------EDAARLADAVRVSQLEADLAQLGggleteigekgVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565781182 165 DAQT-RLTMQELLLSvwqTLR-TTVVFVTHDIdEAILLADtiYVMSARPGRIA 215
Cdd:PTZ00243 814 DAHVgERVVEECFLG---ALAgKTRVLATHQV-HVVPRAD--YVVALGDGRVE 860
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-207 |
9.02e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 25 IDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGP----ERGVVF-----QEAALF-----PWl 90
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLYldaplAW- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 91 NVWeNVVFGPKIAGLSRREYAARAEEMLEITGLSAFKRHLPVQ-LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTR 169
Cdd:PRK15439 361 NVC-ALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190
....*....|....*....|....*....|....*...
gi 565781182 170 LTMQELLLSVWQTlRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:PRK15439 440 NDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-212 |
3.34e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 31 EGEFVALLGPSGCGKSTLLNLIAG------------------------------FEAPSGGELRVgggaVARPgpergvv 80
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrfrgtelqnyFKKLYNGEIKV----VHKP------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 81 fQEAALFPwlnvweNVVFGPKIAGLSRREYAARAEEMLEITGLSAF-KRHLPvQLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:PRK13409 167 -QYVDLIP------KVFKGKVRELLKKVDERGKLDEVVERLGLENIlDRDIS-ELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 160 PFGALDAQTRLTM----QELllsvwqTLRTTVVFVTHDIdeAIL--LADTIYVMSARPG 212
Cdd:PRK13409 239 PTSYLDIRQRLNVarliREL------AEGKYVLVVEHDL--AVLdyLADNVHIAYGEPG 289
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-214 |
3.49e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.44 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 21 ALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-----GVVFQEAALFPWLnvwen 95
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklfSAVFTDFHLFDQL----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 vvFGPKiaGLSRREyaARAEEMLEITGLSAFKRH-----LPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRL 170
Cdd:PRK10522 413 --LGPE--GKPANP--ALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 565781182 171 TMQELLLSVWQTLRTTVVFVTHDiDEAILLADTIYVMsaRPGRI 214
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEM--RNGQL 527
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-212 |
4.16e-08 |
|
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: 53.25 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 31 EGEFVALLGPSGCGKSTLLNLIAGfeapsggELRVGGGAVARPGPERGVV--FQEAALFPWL-NVWEN---VVFGP---- 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG-------ELKPNLGDYDEEPSWDEVLkrFRGTELQDYFkKLANGeikVAHKPqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 101 KIAG---------LSRREYAARAEEMLEITGLSAF-KRHLPvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRL 170
Cdd:COG1245 171 LIPKvfkgtvrelLEKVDERGKLDELAEKLGLENIlDRDIS-ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 565781182 171 TMQELLLSVWQTLRTTVVfVTHDIdeAIL--LADTIYVMSARPG 212
Cdd:COG1245 250 NVARLIRELAEEGKYVLV-VEHDL--AILdyLADYVHILYGEPG 290
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-213 |
4.61e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTYPGVTpvhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGElrvgggavarpgpergvvfqe 83
Cdd:PRK13409 341 VEYPDLTKKLGDFS----LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--------------------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 84 aalfpwlnvwenVVFGPKIA---GLSRREYAARAEEML----EITGLSAFKRHL--PVQ-----------LSGGMRQRVG 143
Cdd:PRK13409 396 ------------VDPELKISykpQYIKPDYDGTVEDLLrsitDDLGSSYYKSEIikPLQlerlldknvkdLSGGELQRVA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 144 IARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEAILLADTIYVMSARPGR 213
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-209 |
5.32e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAP---SGGELRVGGGAVARPGPER-GVVFQEAALFPWLNVWENVV 97
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRSiGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 98 FGPKI---AGLSRREYAARAEEMLEITGLSAFKRHLpVQLSG-GM----RQRVGIARVLTLGSRVLL-MDEPFGALDAQT 168
Cdd:TIGR00956 859 FSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAV-VGVPGeGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 565781182 169 RltmqellLSVWQTLRTTVvfvthDIDEAILLadTIYVMSA 209
Cdd:TIGR00956 938 A-------WSICKLMRKLA-----DHGQAILC--TIHQPSA 964
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-195 |
5.98e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGfeapsggELRVGGGAVARPGP-ERGVVFQEAalfPWLNV--WENVVF 98
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKN-------EISADGGSYTFPGNwQLAWVNQET---PALPQpaLEYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 GPK--------------------IAGLSRREYA-------ARAEEMLEITGLSAFKRHLPVQ-LSGGMRQRVGIARVLTL 150
Cdd:PRK10636 87 GDReyrqleaqlhdanerndghaIATIHGKLDAidawtirSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALIC 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 565781182 151 GSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLrttvVFVTHDID 195
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRD 207
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-176 |
7.41e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 39 GPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVAR-PGPERGVVFQEAALFPWLNVWENVVFGPKIAGLSRREYAAraeem 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAA----- 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 118 LEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELL 176
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-225 |
8.68e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 25 IDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARP------GPERGVVFQEAALFPwLNVWENVVF 98
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwwRSKIGVVSQDPLLFS-NSIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 G--------------------------------PKIAGL---------------SRREYAA-RAEEMLEITG---LSAFK 127
Cdd:PTZ00265 483 SlyslkdlealsnyynedgndsqenknkrnscrAKCAGDlndmsnttdsnelieMRKNYQTiKDSEVVDVSKkvlIHDFV 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 128 RHLP-----------VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIdE 196
Cdd:PTZ00265 563 SALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL-S 641
|
250 260
....*....|....*....|....*....
gi 565781182 197 AILLADTIYVMSARPGRIATRIEVPIERP 225
Cdd:PTZ00265 642 TIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-215 |
1.00e-07 |
|
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: 50.87 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 4 ISVTQLSKTY-PGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER----- 77
Cdd:cd03369 7 IEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrssl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 GVVFQEAALFPWlNVWENV-VFGpkiaglsrrEYA-ARAEEMLEIT--GLSafkrhlpvqLSGGMRQRVGIARVLTLGSR 153
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNLdPFD---------EYSdEEIYGALRVSegGLN---------LSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565781182 154 VLLMDEPFGALDAQTRLTMQELLLSVWQtlRTTVVFVTHDIdEAILLADTIYVMSArpGRIA 215
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRL-RTIIDYDKILVMDA--GEVK 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-226 |
1.68e-07 |
|
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: 51.34 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 2 SHISVTQLSKTYPGVT--PVHALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER-- 77
Cdd:COG4615 326 QTLELRGVTYRYPGEDgdEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyr 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 78 ---GVVFQEAALFpwlnvwenvvfgPKIAGLSRREYAARAEEMLEITGLS---AFK--RHLPVQLSGGMRQRVgiARVLT 149
Cdd:COG4615 406 qlfSAVFSDFHLF------------DRLLGLDGEADPARARELLERLELDhkvSVEdgRFSTTDLSQGQRKRL--ALLVA 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 150 L--GSRVLLMDE-------PFgaldaqTRLTMQELLlsvwQTLRT---TVVFVTHDiDEAILLADTIYVMSArpGRIATR 217
Cdd:COG4615 472 LleDRPILVFDEwaadqdpEF------RRVFYTELL----PELKArgkTVIAISHD-DRYFDLADRVLKMDY--GKLVEL 538
|
....*....
gi 565781182 218 IEVPIERPR 226
Cdd:COG4615 539 TGPAALAAS 547
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-193 |
2.41e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPERGVVFQEAALFPWLNVwenVVFGPK 101
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHL---ARLAPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 102 IAGLSRREYAA----RAEEMLEITGlsafkrhlpvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLL 177
Cdd:PRK10636 405 ELEQKLRDYLGgfgfQGDKVTEETR----------RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
170
....*....|....*.
gi 565781182 178 SVWQTLrttvVFVTHD 193
Cdd:PRK10636 475 DFEGAL----VVVSHD 486
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-195 |
1.48e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTL-LNLIAGFEApSGGELRVGGGAVARPG-----PERGVVFQEAALFpwlnvwen 95
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINES-AEGEIIIDGLNIAKIGlhdlrFKITIIPQDPVLF-------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 96 vvfgpkiAGLSRRE---YAARAEE----MLEITGLSAFKRHLPVQL-----------SGGMRQRVGIARVLTLGSRVLLM 157
Cdd:TIGR00957 1373 -------SGSLRMNldpFSQYSDEevwwALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190
....*....|....*....|....*....|....*...
gi 565781182 158 DEPFGALDAQTRLTMQELLLSVWQTlrTTVVFVTHDID 195
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLN 1481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-207 |
2.37e-06 |
|
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: 47.90 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAG-FEAPSGGELRVGGGAVARPGP----ERGVVF-----QEAALFPWLN 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPaqaiRAGIAMvpedrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 92 VWENVVFG--PKIAGLSRREYAARAEEMLE-ITGLS--AFKRHLPV-QLSGGMRQRVGIARVLTLGSRVLLMDEPFGALD 165
Cdd:TIGR02633 356 VGKNITLSvlKSFCFKMRIDAAAELQIIGSaIQRLKvkTASPFLPIgRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565781182 166 AQTRLTMQELLLSVWQTlRTTVVFVTHDIDEAILLADTIYVM 207
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-210 |
2.43e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 20 HALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAgfeapsggelrvgggavarpgpergvvfqeaalfpwlnvwenVVFG 99
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG------------------------------------------LALG 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 100 PKIAGLSRREYAARAEEmleITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSR----VLLMDEPFGALDAQTRL----T 171
Cdd:cd03227 47 GAQSATRRRSGVKAGCI---VAAVSAELIFTRLQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQalaeA 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 565781182 172 MQELLLSvwqtlRTTVVFVTHDiDEAILLADTIYVMSAR 210
Cdd:cd03227 124 ILEHLVK-----GAQVIVITHL-PELAELADKLIHIKKV 156
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-213 |
2.88e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 19 VHALDQIDLQVAEGEFVALLGPSGCGKSTLLNliAGFEAPsgGELRVGGGavaRPGPERgvvfqeaalfpwlnvwENVVF 98
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS--GKARLISF---LPKFSR----------------NKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 gpkIAGLSRreyaaraeeMLEItGLSAFKRHLPVQ-LSGGMRQRVGIARVL--TLGSRVLLMDEPFGALDAQTRLTmqel 175
Cdd:cd03238 65 ---IDQLQF---------LIDV-GLGYLTLGQKLStLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQ---- 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 565781182 176 LLSVWQTLRT---TVVFVTHDiDEAILLADTIYVMSARPGR 213
Cdd:cd03238 128 LLEVIKGLIDlgnTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-193 |
3.24e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 6 VTQLSKTYPGVTpvhALDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAvarpgpERGVVFQEAA 85
Cdd:PRK15064 322 VENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA------NIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 86 --------LFPWLNVWENvvfgPKIAGLSRREYAARaeeMLeitgLSA--FKRHLPVqLSGGMRQRVGIARVLTLGSRVL 155
Cdd:PRK15064 393 ydfendltLFDWMSQWRQ----EGDDEQAVRGTLGR---LL----FSQddIKKSVKV-LSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 565781182 156 LMDEPFGALDaqtrltMQ--ELLLSVWQTLRTTVVFVTHD 193
Cdd:PRK15064 461 VMDEPTNHMD------MEsiESLNMALEKYEGTLIFVSHD 494
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-197 |
1.01e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 32 GEFVALLGPSGCGKSTLLNLIAGFEAPS--GGELRVGGGAVARPGPER--GVVFQEAALFPWLNVWENVVFG-----PKi 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFARisGYCEQNDIHSPQVTVRESLIYSaflrlPK- 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 103 aGLSRREYAARAEEMLEITGLSAFKRH---LP--VQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLL 177
Cdd:PLN03140 985 -EVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
170 180
....*....|....*....|....
gi 565781182 178 SVWQTLRtTVVFVTH----DIDEA 197
Cdd:PLN03140 1064 NTVDTGR-TVVCTIHqpsiDIFEA 1086
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-193 |
1.14e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 35 VALLGPSGCGKSTLLNLIAgfeapsgGELRVGGGAVARPGPERGVVFQEAALfPWLNVWENVVFgpkiagLSRREYAARA 114
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLIS-------GELQPSSGTVFRSAKVRMAVFSQHHV-DGLDLSSNPLL------YMMRCFPGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 115 EEMLEiTGLSAF--KRHLPVQ----LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDaqtrLTMQELLLSVWQTLRTTVV 188
Cdd:PLN03073 604 EQKLR-AHLGSFgvTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQGLVLFQGGVL 678
|
....*
gi 565781182 189 FVTHD 193
Cdd:PLN03073 679 MVSHD 683
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-165 |
1.16e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.40 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPS--GGELRVGGGAVARPGPE----RGV--VFQEAALFPWLNvw 93
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEerahLGIflAFQYPIEIPGVS-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 94 eNVVFgPKIAGLSRREYAARAE-----------EMLEITGLSA--FKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEP 160
Cdd:CHL00131 101 -NADF-LRLAYNSKRKFQGLPEldplefleiinEKLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQMALLDSELAILDET 178
|
....*
gi 565781182 161 FGALD 165
Cdd:CHL00131 179 DSGLD 183
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
6-64 |
1.80e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.92 E-value: 1.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565781182 6 VTQLSKTYPGVT--PVHALDQIDLQV-----AEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELR 64
Cdd:PRK01889 162 IAEVEALAPGVPvlAVSALDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-209 |
2.46e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 14 PGVTPVhaLDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPG-----------PERGVVFQ 82
Cdd:PLN03232 1246 PGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGltdlrrvlsiiPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 83 EAALF---PW-----LNVWENVVFGPKIAGLSRREYAARAEEMleiTGLSAFkrhlpvqlSGGMRQRVGIARVLTLGSRV 154
Cdd:PLN03232 1324 GTVRFnidPFsehndADLWEALERAHIKDVIDRNPFGLDAEVS---EGGENF--------SVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTlrTTVVFVTHDIDeAILLADTIYVMSA 209
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLN-TIIDCDKILVLSS 1444
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-165 |
3.49e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFE--APSGGELRVGGGAVARPGPE----RGV--VFQEAALFP----- 88
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEdragEGIfmAFQYPVEIPgvsnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 89 -WLNVWENVVFGPK-IAGLSRREYAARAEEMLEITGLSA--FKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGAL 164
Cdd:PRK09580 97 fFLQTALNAVRSYRgQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGL 176
|
.
gi 565781182 165 D 165
Cdd:PRK09580 177 D 177
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-159 |
1.92e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.43 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 28 QVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVgggavarpgPERGVVF---QEaalfPWLNVW---ENVVFGPK 101
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFyvpQR----PYMTLGtlrDQIIYPDS 540
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565781182 102 IAGLSRREYA-ARAEEMLEIT----------GLSAFKRHLPVqLSGGMRQRVGIARVLTLGSRVLLMDE 159
Cdd:TIGR00954 541 SEDMKRRGLSdKDLEQILDNVqlthileregGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
22-193 |
4.09e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.43 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELrVGGGAVARPgpergvVFQEAALFPWLNVWENVVFGPK 101
Cdd:PRK15177 3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDF-IGLRGDALP------LGANSFILPGLTGEENARMMAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 102 IAGLSRREYaarAEEMLEITGLSAFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSvwQ 181
Cdd:PRK15177 76 LYGLDGDEF---SHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALAC--Q 150
|
170
....*....|..
gi 565781182 182 TLRTTVVFVTHD 193
Cdd:PRK15177 151 LQQKGLIVLTHN 162
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
15-205 |
4.63e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.28 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 15 GVTPVHALDQIDLqvaEGEFVALLGPSGCGKSTLLNLI--AGF-EAPSGGELRVGGGAVARPGPERGVV---FQEAA--- 85
Cdd:cd03240 8 NIRSFHERSEIEF---FSPLTLIVGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIREGEVRAQVklaFENANgkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 86 --LFPWLNVWENVVFgpkiagLSRREYAARAEEMLEitglsafkrhlpvQLSGGMRQ------RVGIARVLTLGSRVLLM 157
Cdd:cd03240 85 ytITRSLAILENVIF------CHQGESNWPLLDMRG-------------RCSGGEKVlasliiRLALAETFGSNCGILAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 565781182 158 DEPFGALDAQTRltmQELLLSVWQTLRTTVVF----VTHDiDEAILLADTIY 205
Cdd:cd03240 146 DEPTTNLDEENI---EESLAEIIEERKSQKNFqlivITHD-EELVDAADHIY 193
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-197 |
4.78e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGfEAPSG--------GELRVGG----------GAVARP--------GP 75
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGetiwdikkhiGYVSSSlhldyrvsTS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 76 ERGVVFqeAALFPWLNVWENVvfgpkiaglSRREyAARAEEMLEITGLSAFKRHLPVQ-LSGGMRQRVGIARVLTLGSRV 154
Cdd:PRK10938 355 VRNVIL--SGFFDSIGIYQAV---------SDRQ-QKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 565781182 155 LLMDEPFGALDAQTRLTMQELLLSVWQTLRTTVVFVTHDIDEA 197
Cdd:PRK10938 423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
116-208 |
5.53e-04 |
|
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: 40.28 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 116 EMLEITGLSAFKRHLPVQL-----------SGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTlr 184
Cdd:cd03288 128 EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-- 205
|
90 100
....*....|....*....|....
gi 565781182 185 TTVVFVTHDIdEAILLADTIYVMS 208
Cdd:cd03288 206 RTVVTIAHRV-STILDADLVLVLS 228
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
111-194 |
7.87e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 111 AARAEEMLEITGLSAFKrhlpvQLSGGMRQRVGIARVLTlgsrvLLMDepFGALDAQTRLTMQELLLSvwqtlrttVVFV 190
Cdd:COG0419 141 KLKQEILAQLSGLDPIE-----TLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE--------LAII 200
|
....
gi 565781182 191 THDI 194
Cdd:COG0419 201 THVI 204
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
31-64 |
8.60e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 8.60e-04
10 20 30
....*....|....*....|....*....|....
gi 565781182 31 EGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELR 64
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
110-192 |
9.32e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 110 YAARAEEMLEITGLS---AFKRHLPVQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSvWQtlrTT 186
Cdd:PLN03073 318 YTAEARAASILAGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WP---KT 393
|
....*.
gi 565781182 187 VVFVTH 192
Cdd:PLN03073 394 FIVVSH 399
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-214 |
1.02e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.99 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 6 VTQLSKtyPGVtpvhalDQIDLQVAEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPE----RGVVF 81
Cdd:PRK10762 260 VDNLSG--PGV------NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglaNGIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 82 -----QEAALFPWLNVWENVVFgPKIAGLSRREYAARAEEmlEITGLSAFKRHLPVQ----------LSGGMRQRVGIAR 146
Cdd:PRK10762 332 isedrKRDGLVLGMSVKENMSL-TALRYFSRAGGSLKHAD--EQQAVSDFIRLFNIKtpsmeqaiglLSGGNQQKVAIAR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565781182 147 VLTLGSRVLLMDEPFGALDAQTRLTMQELL-------LSvwqtlrttVVFVTHDIDEAILLADTIYVMsaRPGRI 214
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLInqfkaegLS--------IILVSSEMPEVLGMSDRILVM--HEGRI 473
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
31-67 |
1.24e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 1.24e-03
10 20 30
....*....|....*....|....*....|....*..
gi 565781182 31 EGEFVALLGPSGCGKSTLLNLIAGfeapsGGELRVGG 67
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP-----ELDLRTGE 136
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-202 |
1.27e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 22 LDQIDLQvaEGEFVALLGPSGCGKSTLLNLIAGFEAPSGGELRVGGGAVARPGPER--GVVFQEaalfpWL-NVWENVVF 98
Cdd:PRK10938 21 LPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQlqKLVSDE-----WQrNNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 99 GPKIAGLSRREY-------AARAEEMLEITGLSA-----FKrhlpvQLSGGMRQRVGIARVLTLGSRVLLMDEPFGALDA 166
Cdd:PRK10938 94 GEDDTGRTTAEIiqdevkdPARCEQLAQQFGITAlldrrFK-----YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565781182 167 QTRLTMQELLLSVWQTLRTTVVFVT--HDIDEAI----LLAD 202
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVLNrfDEIPDFVqfagVLAD 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-50 |
3.93e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.93e-03
10 20 30
....*....|....*....|....*....|..
gi 565781182 19 VHALDQIDLQVAEGEFVALLGPSGCGKSTLLN 50
Cdd:TIGR00630 621 ENNLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-219 |
6.38e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.40 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565781182 134 LSGGMRQRVGIARVLTLGSRVLLMDEPFGALDAQTRLTMQELLLSVWQTLRtTVVFVTHDIDEAILLADTIYVMSArpGR 213
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSN--GL 468
|
....*.
gi 565781182 214 IATRIE 219
Cdd:PRK10982 469 VAGIVD 474
|
|
| |
