|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-255 |
2.29e-122 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 349.00 E-value: 2.29e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYaPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW--SAPPGPG-DI 77
Cdd:COG1116 4 AAPALELRGVSKRF-PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgKPVTGPGpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 78 GFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLL 157
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 158 DEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSPRPGRIVAEMAVDLPRPRRPYLRTEAGFG 237
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPEFA 242
|
250
....*....|....*...
gi 501562166 238 VLCREASALLAAAMGDSA 255
Cdd:COG1116 243 ALRAEILDLLREEAERAA 260
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-222 |
2.65e-101 |
|
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: 293.99 E-value: 2.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTAgTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP--GPG-DIGFVFQEP 84
Cdd:cd03293 4 RNVSKTYGGGGGA-VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvtGPGpDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 85 TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAAL 164
Cdd:cd03293 83 ALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 165 DEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSPRPGRIVAEMAVDL 222
Cdd:cd03293 163 DALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-224 |
9.09e-79 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 238.61 E-value: 9.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYaPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP--GPG-DIGF 79
Cdd:COG4525 2 SMLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtGPGaDRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDE 159
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501562166 160 PFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSPRPGRIVAEMAVDLPR 224
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSR 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-216 |
7.09e-71 |
|
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: 216.62 E-value: 7.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------HWSAPPGPGDIG 78
Cdd:cd03259 1 LELKGLSKTYG-----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdVTGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 FVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLD 158
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 159 EPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRIVQ 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
3.07e-67 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 211.88 E-value: 3.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPPGP 74
Cdd:COG3842 2 AMPALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 GDIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRV 154
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 155 LLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVM--NDGRIE 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-226 |
1.92e-62 |
|
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: 195.76 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA----PPGPgDIGFVFQEPTLMPWATVADNVRLPL 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitEPGP-DRMVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 101 D--LAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLA 178
Cdd:TIGR01184 80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501562166 179 LWQETGVTALFVTHSVFEGVYLSTRIAVMSPRPGRIVAE-MAVDLPRPR 226
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQiLEVPFPRPR 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-192 |
1.39e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 193.34 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPGGTAgTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPG 75
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGE-VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGevlidGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 -------DIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARAL 148
Cdd:COG1136 80 larlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501562166 149 VTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH 192
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-224 |
2.57e-59 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 188.76 E-value: 2.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP--GPG-DIGFV 80
Cdd:PRK11248 1 MLQISHLYADYG-----GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPveGPGaERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 81 FQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEP 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501562166 161 FAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSPRPGRIVAEMAVDLPR 224
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFAR 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-216 |
4.49e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 185.74 E-value: 4.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW-------SAPPGPGDIGFVFQEPTLMPWATV 92
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdlftNLPPRERRVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRL 172
Cdd:COG1118 93 AENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501562166 173 NDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVA 216
Cdd:COG1118 173 RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN--QGRIEQ 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-250 |
2.25e-56 |
|
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: 188.19 E-value: 2.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGP-- 74
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsilfdGKDLTKLSRRsl 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 ----GDIGFVFQEPT--LMPWATVADNVRLPLDLAGVAKAEARERAAEQ-LARVGLV-DVAAAFPRELSGGMRMRAALAR 146
Cdd:COG1123 338 relrRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAElLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 147 ALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH--SVFEgvYLSTRIAVMspRPGRIVAEMAVD--L 222
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHdlAVVR--YIADRVAVM--YDGRIVEDGPTEevF 493
|
250 260
....*....|....*....|....*...
gi 501562166 223 PRPRRPYLRteagfgvlcreasALLAAA 250
Cdd:COG1123 494 ANPQHPYTR-------------ALLAAV 508
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-214 |
4.81e-56 |
|
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: 178.84 E-value: 4.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYAPGGTAgTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSappgPGD 76
Cdd:cd03255 1 IELKNLSKTYGGGGEK-VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLS----EKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 --------IGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARAL 148
Cdd:cd03255 76 laafrrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 149 VTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSvFEGVYLSTRIAVMspRPGRI 214
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIEL--RDGKI 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-215 |
5.83e-55 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 180.27 E-value: 5.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPPGPGDIGFVFQEPTLMPWATVAD 94
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtDLPPKDRNIAMVFQSYALYPHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:COG3839 95 NIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501562166 175 ELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:COG3839 175 EIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM--NDGRIQ 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-215 |
2.06e-53 |
|
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: 172.81 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA------PPGPGDIGFVFQEPTLMPWATVAD 94
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlPPHKRPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501562166 175 ELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:cd03300 172 ELKRLQKELGITFVFVTHDQEEALTMSDRIAVM--NKGKIQ 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-232 |
5.65e-53 |
|
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: 171.91 E-value: 5.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYAPGGTaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP--------GPG 75
Cdd:COG1124 1 MLEVRNLSVSYGQGGR-RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkaFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 DIGFVFQEPT--LMPWATVADNVRLPLDLAGVAKAEARERAAeqLARVGL-VDVAAAFPRELSGGMRMRAALARALVTRP 152
Cdd:COG1124 80 RVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREERIAEL--LEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 153 RVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVfeGV--YLSTRIAVMspRPGRIVAEMAVDLPR--PRRP 228
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDL--AVvaHLCDRVAVM--QNGRIVEELTVADLLagPKHP 233
|
....
gi 501562166 229 YLRT 232
Cdd:COG1124 234 YTRE 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-215 |
1.61e-52 |
|
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: 171.67 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 19 TAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG------------DIGFVFQEPTL 86
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelrelrrkKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 87 MPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDE 166
Cdd:cd03294 114 LPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501562166 167 ITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLV 240
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
22-207 |
3.17e-52 |
|
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: 173.30 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS------APPGPGDIGFVFQEPTLMPWATVADN 95
Cdd:TIGR03265 17 FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGgrditrLPPQKRDYGIVFQSYALFPNLTVADN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 96 VRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDE 175
Cdd:TIGR03265 97 IAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTE 176
|
170 180 190
....*....|....*....|....*....|..
gi 501562166 176 LLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:TIGR03265 177 IRQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-217 |
4.58e-52 |
|
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: 169.39 E-value: 4.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPG 75
Cdd:COG1127 2 SEPMIEVRNLTKSFG-----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGeilvdGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 ------DIGFVFQEPTL---MpwaTVADNVRLPL------------DLAgvakaeareraAEQLARVGLVDVAAAFPREL 134
Cdd:COG1127 77 lyelrrRIGMLFQGGALfdsL---TVFENVAFPLrehtdlseaeirELV-----------LEKLELVGLPGAADKMPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 135 SGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH---SVFEgvyLSTRIAVMSprP 211
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHdldSAFA---IADRVAVLA--D 217
|
....*.
gi 501562166 212 GRIVAE 217
Cdd:COG1127 218 GKIIAE 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-221 |
8.30e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.70 E-value: 8.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH------WSAPPGP-GDIGFVFQEPTLMPWATVA 93
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEVrRRIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLN 173
Cdd:COG1131 92 ENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501562166 174 DELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVD 221
Cdd:COG1131 172 ELLREL-AAEGKTVLLSTHYLEEAERLCDRVAII--DKGRIVADGTPD 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-227 |
2.40e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 168.32 E-value: 2.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLrSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP---GPGDIGF 79
Cdd:PRK11247 12 PLL-LNAVSKRYG-----ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPlaeAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEPTLMPWATVADNVRLPLdlagvaKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDE 159
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 160 PFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVDLPRPRR 227
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDLPRPRR 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-207 |
7.28e-51 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 164.28 E-value: 7.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW----------SAPPGPGDIGFVFQEPTLMPW 89
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledELPPLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNVRLPldlagvakaeareraaeqlarvglvdvaaafpreLSGGMRMRAALARALVTRPRVLLLDEPFAALDEITR 169
Cdd:cd03229 91 LTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 501562166 170 FRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:cd03229 137 REVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-217 |
9.61e-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: 9.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYaPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG-------- 75
Cdd:cd03257 1 LLEVKNLSVSF-PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 ---DIGFVFQEP--TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAA---AFPRELSGGMRMRAALARA 147
Cdd:cd03257 80 rrkEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 148 LVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVfeGV--YLSTRIAVMspRPGRIVAE 217
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDL--GVvaKIADRVAVM--YAGKIVEE 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-215 |
7.05e-49 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 160.50 E-value: 7.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS------APPGPGDIGFVFQEPTLMPWATVAD 94
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdLPPKDRDIAMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:cd03301 92 NIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501562166 175 ELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:cd03301 172 ELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM--NDGQIQ 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
21-214 |
9.57e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 164.74 E-value: 9.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS------APPGPGDIGFVFQEPTLMPWATVAD 94
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithVPAENRHVNTVFQSYALFPHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501562166 175 ELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRI 214
Cdd:PRK09452 186 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-215 |
9.80e-49 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 162.95 E-value: 9.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH---------------WSappgpgdIGFVFQEPT 85
Cdd:COG1125 14 GTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILidgedirdldpvelrRR-------IGYVIQQIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 86 LMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGL--VDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAA 163
Cdd:COG1125 87 LFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501562166 164 LDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:COG1125 167 LDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIV 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-215 |
1.30e-48 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 160.54 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGPGDIGFVFQEPTLMPWAT 91
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPVELRRKIGYVIQQIGLFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 92 VADNVRLPLDLAGVAKAEARERAAEQLARVGL--VDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITR 169
Cdd:cd03295 92 VEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501562166 170 FRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:cd03295 172 DQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM--KNGEIV 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
6.73e-47 |
|
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: 163.15 E-value: 6.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPGGTagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTA---GGVH--------WS 69
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDV---PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLldgrdlleLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 70 APPGPGDIGFVFQEPT--LMPwATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARA 147
Cdd:COG1123 78 EALRGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 148 LVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVD--LPRP 225
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVEDGPPEeiLAAP 234
|
..
gi 501562166 226 RR 227
Cdd:COG1123 235 QA 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-192 |
8.15e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 155.60 E-value: 8.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGgtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgpG------------ 75
Cdd:COG2884 5 ENVSKRYPGG----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-----Gqdlsrlkrreip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 ----DIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTR 151
Cdd:COG2884 76 ylrrRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501562166 152 PRVLLLDEPFAALDEITRfrlnDELLALWQE---TGVTALFVTH 192
Cdd:COG2884 156 PELLLADEPTGNLDPETS----WEIMELLEEinrRGTTVLIATH 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-192 |
2.87e-46 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 154.51 E-value: 2.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYaPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS-APPGPGD---- 76
Cdd:COG4181 6 APIIELRGLTKTV-GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgQDLFALDedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -------IGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAeqLARVGLVDVAAAFPRELSGGMRMRAALARALV 149
Cdd:COG4181 85 arlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARAL--LERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501562166 150 TRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH 192
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTH 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
25-217 |
3.44e-46 |
|
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: 154.20 E-value: 3.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPGD------IGFVFQEPTLMPWATVA 93
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGevlidGEDISGLSEAELyrlrrrMGMLFQSGALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNVRLPL------------DLAgvakaeareraAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:cd03261 96 ENVAFPLrehtrlseeeirEIV-----------LEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 162 AALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:cd03261 165 AGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLY--DGKIVAE 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-208 |
2.83e-45 |
|
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: 151.08 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYapgGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH--------WSAPPGPGDIGF 79
Cdd:cd03225 3 KNLSFSY---PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdltkLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEP---TLMPwaTVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLL 156
Cdd:cd03225 80 VFQNPddqFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501562166 157 LDEPFAALDEITRFRLNDELLALWQEtGVTALFVTHSVFEGVYLSTRIAVMS 208
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-214 |
3.56e-45 |
|
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: 151.72 E-value: 3.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPPGPGDIGFVFQEPTLMPWATVADNVR 97
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatDVPVQERNVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 98 LPLDLAGVAKAEARERAAEQ----LARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLN 173
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRAKvhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501562166 174 DELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRI 214
Cdd:cd03296 177 RWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMN--KGRI 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-193 |
1.01e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.58 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 11 GLRYAPGGTAGteaLADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW-----SAPPGP---GDIGFVFQ 82
Cdd:COG4619 5 GLSFRVGGKPI---LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkplSAMPPPewrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 83 EPTLMPwATVADNVRLPLDLAGvaKAEARERAAEQLARVGL-VDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190
....*....|....*....|....*....|..
gi 501562166 162 AALDEITRFRLNDELLALWQETGVTALFVTHS 193
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHD 190
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
25-215 |
5.43e-44 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 151.77 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPPGPGDIGFVFQEPTLMPWATVADNVRL 98
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLdgkditNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 99 PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLA 178
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 501562166 179 LWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIM--LNGRLS 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-207 |
8.08e-44 |
|
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: 146.00 E-value: 8.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPG--PGDIGFVFQEPTLMPWATVA 93
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGeikvlGKDIKKEPEevKRRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNVRLpldlagvakaeareraaeqlarvglvdvaaafprelSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLN 173
Cdd:cd03230 92 ENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....
gi 501562166 174 DELLALwQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:cd03230 136 ELLREL-KKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-216 |
3.11e-43 |
|
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: 145.90 E-value: 3.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 31 TVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHW-------SAPPGPGDIGFVFQEPTLMPWATVADNvrL 98
Cdd:cd03297 19 FDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlnGTVLfdsrkkiNLPPQQRKIGLVFQQYALFPHLNVREN--L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 99 PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLA 178
Cdd:cd03297 97 AFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 501562166 179 LWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:cd03297 177 IKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRLQY 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-162 |
3.94e-43 |
|
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: 143.56 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD--------IGFVFQEPTLMPWATVADNV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerkslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 97 RLPLDLAGVAKAEARERAAEQLARVGLVDVAA----AFPRELSGGMRMRAALARALVTRPRVLLLDEPFA 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-217 |
4.08e-43 |
|
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: 145.94 E-value: 4.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGgtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW--------SAPPGPGDIGF 79
Cdd:COG1122 4 ENLSFSYPGG----TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditkkNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEPT---LMPwaTVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLL 156
Cdd:COG1122 80 VFQNPDdqlFAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 157 LDEPFAALDEITRFRLNDELLALWQEtGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLD--DGRIVAD 215
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-215 |
1.07e-42 |
|
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: 148.03 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 40 LLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA------PPGPGDIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARER 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 114 AAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHS 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|..
gi 501562166 194 VFEGVYLSTRIAVMspRPGRIV 215
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIA 180
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-220 |
2.78e-42 |
|
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: 144.26 E-value: 2.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 16 PGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPG------DIGFVFQEP 84
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsvlvdGTDLTLLSGKElrkarrRIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 85 TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAAL 164
Cdd:cd03258 92 NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 165 DEITrfrlNDELLALW----QETGVTALFVTHSVfEGVY-LSTRIAVMSprPGRIVAEMAV 220
Cdd:cd03258 172 DPET----TQSILALLrdinRELGLTIVLITHEM-EVVKrICDRVAVME--KGEVVEEGTV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-217 |
4.21e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.06 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYaPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPG------D 76
Cdd:COG1135 5 ENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGsvlvdGVDLTALSERElraarrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 IGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLL 156
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 157 LDEPFAALD-EITRfrlndELLALW----QETGVTALFVTH--SVFEGVylSTRIAVMSprPGRIVAE 217
Cdd:COG1135 164 CDEATSALDpETTR-----SILDLLkdinRELGLTIVLITHemDVVRRI--CDRVAVLE--NGRIVEQ 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-208 |
6.17e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 144.59 E-value: 6.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWS-APPGPGDIGFVFQEPTLMPWATVAD 94
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGqimldGVDLShVPPYQRPINMMFQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQL 190
|
170 180 190
....*....|....*....|....*....|....
gi 501562166 175 ELLALWQETGVTALFVTHSVFEGVYLSTRIAVMS 208
Cdd:PRK11607 191 EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-217 |
9.04e-41 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 139.55 E-value: 9.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 30 LTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------HWSAPPGPGDIGFVFQEPTLMPWATVADNVRLPLDLA 103
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 104 GVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQET 183
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178
|
170 180 190
....*....|....*....|....*....|....
gi 501562166 184 GVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLD--NGRIAAQ 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-215 |
1.51e-40 |
|
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: 140.01 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYApggtAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP---------- 74
Cdd:cd03256 1 IEVENLSKTYP----NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgkalrql 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 -GDIGFVFQEPTLMPWATVADNV------RLPL--DLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALA 145
Cdd:cd03256 77 rRQIGMIFQQFNLIERLSVLENVlsgrlgRRSTwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 146 RALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGL--KDGRIV 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-221 |
1.07e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.19 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 30 LTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPPGPGDIGFVFQEPTLMPWATVADNVRLPLDLA 103
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltALPPAERPVSMLFQENNLFPHLTVAQNIGLGLRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 104 GVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQET 183
Cdd:COG3840 100 LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRER 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 501562166 184 GVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAVD 221
Cdd:COG3840 180 GLTVLMVTHDPEDAARIADRVLLVA--DGRIAADGPTA 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-217 |
1.66e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.05 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGP-----GDIGFVFQEPTLMPWA 90
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtitvdGEDLTDSKKDinklrRKVGMVFQQFNLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 TVADNVRL-PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD-EIT 168
Cdd:COG1126 93 TVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpELV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 169 RfrlndELLALWQE---TGVTALFVTH------SVfegvylSTRIAVMSprPGRIVAE 217
Cdd:COG1126 173 G-----EVLDVMRDlakEGMTMVVVTHemgfarEV------ADRVVFMD--GGRIVEE 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-216 |
1.75e-39 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 137.08 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA------PPGPGDIGFVFQEPTLMPWATVADNVRL 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 99 PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLA 178
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 501562166 179 LWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQ 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-192 |
5.55e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 5.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP---GPGDI 77
Cdd:COG1121 3 MMPAIELENLTVSYG-----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 78 GFVFQEPTL---MPwATVADNVRLPLD----LAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVT 150
Cdd:COG1121 78 GYVPQRAEVdwdFP-ITVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501562166 151 RPRVLLLDEPFAALDEITRFRLNDeLLALWQETGVTALFVTH 192
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTH 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-250 |
5.71e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 138.33 E-value: 5.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPGG-----TAGT-EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW-----S 69
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRGglfgrTVGVvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdgqdiT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 70 APPGPG------DIGFVFQEP--TLMPWATVADNVRLPLDLAGVAKAEARERAAEQ-LARVGL-VDVAAAFPRELSGGMR 139
Cdd:COG4608 84 GLSGRElrplrrRMQMVFQDPyaSLNPRMTVGDIIAEPLRIHGLASKAERRERVAElLELVGLrPEHADRYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 140 MRAALARALVTRPRVLLLDEPFAALD-----EItrfrLNdeLLA-LWQETGVTALFVTH--SVFEgvYLSTRIAVMspRP 211
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDvsiqaQV----LN--LLEdLQDELGLTYLFISHdlSVVR--HISDRVAVM--YL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 501562166 212 GRIVaEMAvdlP------RPRRPYLRteagfgvlcreasALLAAA 250
Cdd:COG4608 234 GKIV-EIA---PrdelyaRPLHPYTQ-------------ALLSAV 261
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-220 |
3.69e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 136.47 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 16 PGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPG------DIGFVFQEP 84
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGrvlvdGQDLTALSEKElrkarrQIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 85 TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAAL 164
Cdd:PRK11153 92 NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 165 D-EITRFRLndELLA-LWQETGVTALFVTH--SVFEGVylSTRIAVMSprPGRIVAEMAV 220
Cdd:PRK11153 172 DpATTRSIL--ELLKdINRELGLTIVLITHemDVVKRI--CDRVAVID--AGRLVEQGTV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-215 |
6.14e-38 |
|
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: 132.69 E-value: 6.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYAPGgtagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLP-----PTAGGVHW--SAPPGPGD- 76
Cdd:cd03260 1 IELRDLNVYYGDK-----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLdgKDIYDLDVd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -------IGFVFQEPTLMPwATVADNVRLPLDLAGVAKAEARERAAEQ-LARVGLVDVAA--AFPRELSGGMRMRAALAR 146
Cdd:cd03260 76 vlelrrrVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEaLRKAALWDEVKdrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 147 ALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETgvTALFVTHSVFEGVYLSTRIAVMSprPGRIV 215
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLL--NGRLV 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
23-217 |
6.92e-38 |
|
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: 133.06 E-value: 6.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPPGP-GDIGFVFQEPTLMPWATVADN 95
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrKEPREArRQIGVLPDERGLYDRLTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 96 VRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDE 175
Cdd:COG4555 95 IRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501562166 176 LLALWQEtGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:COG4555 175 LRALKKE-GKTVLFSSHIMQEVEALCDRVVIL--HKGKVVAQ 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-215 |
1.80e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 132.06 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH-------WSAPPGPGDI-------GFVFQEPTLM 87
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIrelrrnvGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 88 PWATVADN-VRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD- 165
Cdd:PRK11124 95 PHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501562166 166 EITRFRLN--DELlalwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:PRK11124 175 EITAQIVSiiREL----AETGITQVIVTHEVEVARKTASRVVYM--ENGHIV 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-207 |
2.12e-37 |
|
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: 129.43 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPgPGD----IG 78
Cdd:cd03228 4 KNVSFSYPGRPK---PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGeilidGVDLRDLD-LESlrknIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 FVFQEPTLMPwATVADNVrlpldlagvakaeareraaeqlarvglvdvaaafpreLSGGMRMRAALARALVTRPRVLLLD 158
Cdd:cd03228 80 YVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501562166 159 EPFAALDEITRFRLNDELLALwqETGVTALFVTHSvfegvyLST-----RIAVM 207
Cdd:cd03228 122 EATSALDPETEALILEALRAL--AKGKTVIVIAHR------LSTirdadRIIVL 167
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-192 |
4.98e-37 |
|
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: 129.52 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW-------SAPPGPG 75
Cdd:COG4133 1 MMLEAENLSCRRG-----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirdAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 DIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAeqLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVL 155
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEA--LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 501562166 156 LLDEPFAALDEITRFRLNdELLALWQETGVTALFVTH 192
Cdd:COG4133 154 LLDEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTH 189
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
23-192 |
5.95e-37 |
|
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: 129.57 E-value: 5.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPGD-----IGFVFQEPTLMPWATV 92
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidGLKLTDDKKNINelrqkVGMVFQQFNLFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRL-PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD-EITRf 170
Cdd:cd03262 94 LENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpELVG- 172
|
170 180
....*....|....*....|....*
gi 501562166 171 rlndELLALWQ---ETGVTALFVTH 192
Cdd:cd03262 173 ----EVLDVMKdlaEEGMTMVVVTH 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
27-254 |
8.88e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 132.92 E-value: 8.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGpgDIGFVFQEPTLMPWATVADNVRL 98
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvtHRSIQQR--DICMVFQSYALFPHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 99 PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLA 178
Cdd:PRK11432 102 GLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 179 LWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIvaeMAVDLPRP--RRPylrteagfgvlcreASALLAAAMGDS 254
Cdd:PRK11432 182 LQQQFNITSLYVTHDQSEAFAVSDTVIVMN--KGKI---MQIGSPQElyRQP--------------ASRFMASFMGDA 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-192 |
9.60e-37 |
|
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: 129.19 E-value: 9.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP---GPGDIGFVFQEPTL---MPwATVAD 94
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekERKRIGYVPQRRSIdrdFP-ISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQ----LARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:cd03235 90 VVLMGLYGHKGLFRRLSKADKAKvdeaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180
....*....|....*....|..
gi 501562166 171 RLNdELLALWQETGVTALFVTH 192
Cdd:cd03235 170 DIY-ELLRELRREGMTILVVTH 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-217 |
1.55e-36 |
|
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: 129.78 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSappgPG 75
Cdd:COG1120 1 MLEAENLSVGYG-----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLS----RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 D----IGFVFQEPTLMPWATVADNV---RLP-LDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARA 147
Cdd:COG1120 72 ElarrIAYVPQEPPAPFGLTVRELValgRYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 148 LVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRIVAQ 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-221 |
2.77e-36 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 128.26 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH---WSAPPGPGD----IGFVFQEPTLMPWATVA 93
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvagHDVVREPREvrrrIGIVFQDLSVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLN 173
Cdd:cd03265 92 ENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501562166 174 DELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAVD 221
Cdd:cd03265 172 EYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID--HGRIIAEGTPE 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-229 |
4.15e-36 |
|
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: 130.56 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYaPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPP---TAGGVHW------SAPPG- 73
Cdd:COG0444 1 LLEVRNLKVYF-PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFdgedllKLSEKe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 74 -----PGDIGFVFQEP--TLMPWATVADNVRLPLDLAGVAKAEARERAAEQ-LARVGL---VDVAAAFPRELSGGMRMRA 142
Cdd:COG0444 80 lrkirGREIQMIFQDPmtSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIElLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 143 ALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVfeGV--YLSTRIAVMspRPGRIVaEMA- 219
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDL--GVvaEIADRVAVM--YAGRIV-EEGp 234
|
250
....*....|..
gi 501562166 220 VD--LPRPRRPY 229
Cdd:COG0444 235 VEelFENPRHPY 246
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-208 |
7.40e-36 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 130.59 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG------DIGFVFQEPTLMPWATVADN 95
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhardrKVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 96 VRLPL---------DLAGVAKAEARERAAEQLARVglvdvAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDE 166
Cdd:PRK10851 95 IAFGLtvlprrerpNAAAIKAKVTQLLEMVQLAHL-----ADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501562166 167 ITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMS 208
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-207 |
1.09e-35 |
|
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: 124.66 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPgpgdigfvfqeptlm 87
Cdd:cd00267 3 ENLSFRYG-----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 88 pwatvadnvrlpldlagvakaEARERAAEQLARVGLVDvaaafprELSGGMRMRAALARALVTRPRVLLLDEPFAALDEI 167
Cdd:cd00267 63 ---------------------IAKLPLEELRRRIGYVP-------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501562166 168 TRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:cd00267 115 SRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-194 |
1.13e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.44 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH-------WSAPPGPGDI-------GFVFQEPT 85
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdFSQKPSEKAIrllrqkvGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 86 LMPWATVADN-VRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAAL 164
Cdd:COG4161 93 LWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190
....*....|....*....|....*....|...
gi 501562166 165 D-EITRFRLN--DELlalwQETGVTALFVTHSV 194
Cdd:COG4161 173 DpEITAQVVEiiREL----SQTGITQVIVTHEV 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-217 |
2.24e-35 |
|
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: 126.69 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPP-- 72
Cdd:COG0411 1 SDPLLEVRGLTKRFG-----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgrditGLPPhr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 ----GpgdIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAE---------------QLARVGLVDVAAAFPRE 133
Cdd:COG0411 76 iarlG---IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPrarreereareraeeLLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 134 LSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHS---VFEgvyLSTRIAVMSpr 210
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmdlVMG---LADRIVVLD-- 227
|
....*..
gi 501562166 211 PGRIVAE 217
Cdd:COG0411 228 FGRVIAE 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-249 |
2.35e-35 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 129.45 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHW--SA-----PPGPGDIGFVFQEPTLMPWATVAD 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGrirlgGEVLqdSArgiflPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NvrlpldLAGVAKAEARERAAEQLARV----GLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:COG4148 97 N------LLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 171 RLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAVD--LprpRRPYLRTEAGFgvlcREASALLA 248
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLE--QGRVVASGPLAevL---SRPDLLPLAGG----EEAGSVLE 241
|
.
gi 501562166 249 A 249
Cdd:COG4148 242 A 242
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-217 |
3.26e-35 |
|
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: 133.04 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPggtAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV-------------HWSAppgp 74
Cdd:COG2274 477 ENVSFRYPG---DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaSLRR---- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 gDIGFVFQEPTLMPwATVADNVRL---PLDLAGVakaeareraaEQLAR-VGLVDVAAAFP-----------RELSGGMR 139
Cdd:COG2274 550 -QIGVVLQDVFLFS-GTIRENITLgdpDATDEEI----------IEAARlAGLHDFIEALPmgydtvvgeggSNLSGGQR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 140 MRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHSvfegvyLST-----RIAVMspRPGRI 214
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR------LSTirladRIIVL--DKGRI 687
|
...
gi 501562166 215 VAE 217
Cdd:COG2274 688 VED 690
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-192 |
3.62e-35 |
|
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: 125.54 E-value: 3.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYAPGGTAgTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP----GPGDI-- 77
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLD-TRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlsklSSNERak 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 78 ------GFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTR 151
Cdd:TIGR02211 80 lrnkklGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501562166 152 PRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH 192
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTH 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-215 |
6.02e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.08 E-value: 6.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 30 LTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPT------AGGVHWSAPPGPGDIGFVFQEPTLMPWATVADNVRLPLDlA 103
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPAsgsltlNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLN-P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 104 GVAKAEARERAAEQLA-RVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRfrlnDELLALW-- 180
Cdd:PRK10771 99 GLKLNAAQREKLHAIArQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR----QEMLTLVsq 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501562166 181 --QETGVTALFVTHSVFEgvylSTRIAvmsPRP-----GRIV 215
Cdd:PRK10771 175 vcQERQLTLLMVSHSLED----AARIA---PRSlvvadGRIA 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-208 |
1.10e-34 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 123.82 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 30 LTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------HWSAPPGPGDIGFVFQEPTLMPWATVADNVRLPLDlA 103
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIkvndqsHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH-P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 104 GVAKAEARERAAEQLAR-VGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRfrlnDELLAL--- 179
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQqVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR----EEMLALvkq 173
|
170 180 190
....*....|....*....|....*....|
gi 501562166 180 -WQETGVTALFVTHSVFEGVYLSTRIAVMS 208
Cdd:TIGR01277 174 lCSERQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
1.39e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS----APPGPGD 76
Cdd:COG1129 1 AEPLLEMRGISKSFG-----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvRFRSPRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -----IGFVFQEPTLMPWATVADNV---RLPLDLAGVAKAEARERAAEQLARVGL-VDVAAafP-RELSGGMRMRAALAR 146
Cdd:COG1129 76 aqaagIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLdIDPDT--PvGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 147 ALVTRPRVLLLDEPFAALD--EITR-FRLNDELlalwQETGVTALFVTHS---VFEgvyLSTRIAVMspRPGRIVAEMAV 220
Cdd:COG1129 154 ALSRDARVLILDEPTASLTerEVERlFRIIRRL----KAQGVAIIYISHRldeVFE---IADRVTVL--RDGRLVGTGPV 224
|
....*..
gi 501562166 221 -DLPRPR 226
Cdd:COG1129 225 aELTEDE 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-207 |
3.99e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 126.30 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS------APPGPGDIGFVFQEPTLMPWATVADNVRLPL 100
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmndVPPAERGVGMVFQSYALYPHLSVAENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 101 DLAGVAKAEAR-----ERAAEQLARvgLVDVAaafPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDE 175
Cdd:PRK11000 101 KLAGAKKEEINqrvnqVAEVLQLAH--LLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
|
170 180 190
....*....|....*....|....*....|..
gi 501562166 176 LLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK11000 176 ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-208 |
4.06e-34 |
|
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: 122.61 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYAPGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-------GVHWSAPPGPGDI 77
Cdd:cd03263 1 LQIRNLTKTYKKGTKP---AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayingySIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 78 GFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLL 157
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501562166 158 DEPFAALDEITRFRLNDELLALWQETGVtaLFVTHSVFEGVYLSTRIAVMS 208
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMS 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-192 |
1.20e-33 |
|
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: 121.36 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG-----------DIGFVFQEPTLMP 88
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraipylrrKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 89 WATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180
....*....|....*....|....
gi 501562166 169 RFRLNDeLLALWQETGVTALFVTH 192
Cdd:cd03292 172 TWEIMN-LLKKINKAGTTVVVATH 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-217 |
3.86e-33 |
|
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: 120.62 E-value: 3.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH------WSAPP------ 72
Cdd:cd03219 1 LEVRGLTKRFG-----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgediTGLPPheiarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 GpgdIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQ----------LARVGLVDVAAAFPRELSGGMRMRA 142
Cdd:cd03219 76 G---IGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEreareraeelLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 143 ALARALVTRPRVLLLDEPFAAL--DEITRFRlndELLALWQETGVTALFVTH---SVFEgvyLSTRIAVMSprPGRIVAE 217
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLnpEETEELA---ELIRELRERGITVLLVEHdmdVVMS---LADRVTVLD--QGRVIAE 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-232 |
4.85e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.99 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGP-------GDIGFVFQEPTLMPWAT 91
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqvlidGVDIAKISDAelrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 92 VADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFR 171
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501562166 172 LNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVD--LPRPRRPYLRT 232
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM--QNGEVVQVGTPDeiLNNPANDYVRT 263
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-207 |
2.80e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 121.10 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS------APPGPGDIGFVFQEPTLMPWATVA 93
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGgrvvneLEPADRDIAMVFQNYALYPHMSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNVRLPLDLAGVAKAEAReraaeqlARVGlvDVAAAF---------PRELSGGMRMRAALARALVTRPRVLLLDEPFAAL 164
Cdd:PRK11650 95 ENMAYGLKIRGMPKAEIE-------ERVA--EAARILeleplldrkPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501562166 165 DEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK11650 166 DAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-217 |
5.47e-32 |
|
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: 118.71 E-value: 5.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW---SAPPGPG--------D 76
Cdd:TIGR04521 4 KNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgrDITAKKKkklkdlrkK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 IGFVFQEP--TLMPwATVADNVRL-PLDLaGVAKAEARERAAEQLARVGL-VDVAAAFPRELSGGMRMRAALARALVTRP 152
Cdd:TIGR04521 84 VGLVFQFPehQLFE-ETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501562166 153 RVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVM--HKGKIVLD 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-220 |
6.18e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 118.25 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYAPGGTAGTEA----LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG--- 75
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 --------DIGFVFQEP--TLMPWATVADNVRLPL-DLAGVAKAEARERAAEQLARVGLVD-VAAAFPRELSGGMRMRAA 143
Cdd:PRK10419 82 aqrkafrrDIQMVFQDSisAVNPRKTVREIIREPLrHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501562166 144 LARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAV 220
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD--NGQIVETQPV 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-233 |
8.14e-32 |
|
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: 119.83 E-value: 8.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSA-------PPGPGDIGFVFQEPTLMPWATVAD 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeivlnGRTLFDsrkgiflPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLarVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIEL--LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 175 ELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVD--LPRPRRPYLRTE 233
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVAAAGPIAevWASPDLPWLARE 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-192 |
8.59e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.43 E-value: 8.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 19 TAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPP--TAGGVHW-------SAPPGPGDIGFVFQEPTLMPW 89
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafSASGEVLlngrrltALPAEQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNvrLPLDL-AGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:COG4136 91 LSVGEN--LAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180
....*....|....*....|....
gi 501562166 169 RFRLNDELLALWQETGVTALFVTH 192
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTH 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-216 |
9.51e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 116.23 E-value: 9.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYAPggtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP----GPGDIGFV 80
Cdd:cd03269 1 LEVENVTKRFGR-----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 81 FQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEP 160
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 161 FAALDEITRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:cd03269 156 FSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLL--NKGRAVL 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-217 |
2.84e-31 |
|
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: 114.07 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH--------WSAPPGPGDIGF 79
Cdd:cd03214 3 ENLSVGYG-----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlasLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQeptlmpwatvadnvrlpldlagvakaeareraaeQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDE 159
Cdd:cd03214 78 VPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 160 PFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILL--KDGRIVAQ 179
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-220 |
4.98e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.91 E-value: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYAPGGTAgTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP---------- 72
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQ-TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 --GPGDIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVT 150
Cdd:PRK11629 83 elRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 151 RPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVmspRPGRIVAEMAV 220
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM---RDGRLTAELSL 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-217 |
9.11e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.50 E-value: 9.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYaPGgtAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH-----------Ws 69
Cdd:PRK13635 2 KEEIIRVEHISFRY-PD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvW- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 70 appgpgDI----GFVFQEP-TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAAL 144
Cdd:PRK13635 78 ------DVrrqvGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501562166 145 ARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEgVYLSTRIAVMspRPGRIVAE 217
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDE-AAQADRVIVM--NKGEILEE 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-220 |
1.22e-30 |
|
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: 114.90 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYAPGGTAGTEA----LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP-----GP 74
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlyqldRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 G------DIGFVFQEP--TLMPWATVADNVRLPL-DLAGVAKAEARERAAEQLARVGL-VDVAAAFPRELSGGMRMRAAL 144
Cdd:TIGR02769 82 QrrafrrDVQLVFQDSpsAVNPRMTVRQIIGEPLrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 145 ARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAV 220
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD--KGQIVEECDV 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-194 |
7.82e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.51 E-value: 7.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA-----------PPGPGDIGFVFQEPTLMPW 89
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEitr 169
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD--- 170
|
170 180
....*....|....*....|....*...
gi 501562166 170 fRLNDELLALWQE---TGVTALFVTHSV 194
Cdd:PRK10908 171 -ALSEGILRLFEEfnrVGVTVLMATHDI 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-217 |
1.47e-29 |
|
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: 116.40 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYAPGGTAgteaLADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGP 74
Cdd:COG4988 335 PSIELEDVSFSYPGGRPA----LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 GDIGFVFQEPTLMPwATVADNVRL------PLDLAGVakaeareraaeqLARVGLVDVAAAFP-----------RELSGG 137
Cdd:COG4988 411 RQIAWVPQNPYLFA-GTIRENLRLgrpdasDEELEAA------------LEAAGLDEFVAALPdgldtplgeggRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 138 MRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHSVfEGVYLSTRIAVMspRPGRIVAE 217
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVL--DDGRIVEQ 552
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-251 |
1.68e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.94 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYA-PGG-----TAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPpTAG-----GVHWSA 70
Cdd:COG4172 273 PPLLEARDLKVWFPiKRGlfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGeirfdGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 71 PPGPG------DIGFVFQEP--TLMPWATVADNVRLPLDLAGVAKAEARERAAEQ--LARVGL-VDVAAAFPRELSGGMR 139
Cdd:COG4172 352 LSRRAlrplrrRMQVVFQDPfgSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAeaLEEVGLdPAARHRYPHEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 140 MRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH--SVFEgvYLSTRIAVMspRPGRIVAE 217
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHdlAVVR--ALAHRVMVM--KDGKVVEQ 507
|
250 260 270
....*....|....*....|....*....|....*.
gi 501562166 218 MAVD--LPRPRRPYLRteagfgvlcreasALLAAAM 251
Cdd:COG4172 508 GPTEqvFDAPQHPYTR-------------ALLAAAP 530
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-194 |
3.23e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.18 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGpgDI-------GFVFQEPTLMPW 89
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdGLKVNDPKV--DErlirqeaGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNVRL-PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEit 168
Cdd:PRK09493 92 LTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP-- 169
|
170 180
....*....|....*....|....*....
gi 501562166 169 rfRLNDELLALWQ---ETGVTALFVTHSV 194
Cdd:PRK09493 170 --ELRHEVLKVMQdlaEEGMTMVIVTHEI 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-215 |
4.62e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 114.51 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG------GVHW--SAPPG 73
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvGDEWvdMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 74 PGD-------IGFVFQEPTLMPWATVADN------VRLPLDLAgvakaeaRERAAEQLARVGLVDVAAA-----FPRELS 135
Cdd:TIGR03269 357 PDGrgrakryIGILHQEYDLYPHRTVLDNlteaigLELPDELA-------RMKAVITLKMVGFDEEKAEeildkYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 136 GGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIV 507
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
21-217 |
1.46e-28 |
|
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: 110.17 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG--------------GVHWSappgpgdIGFVFQEPTL 86
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtarvagydvvreprKVRRS-------IGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 87 MPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDE 166
Cdd:TIGR01188 78 DEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501562166 167 ITRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:TIGR01188 158 RTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAII--DHGRIIAE 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-218 |
4.25e-28 |
|
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: 106.53 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAP-PGPGDIG 78
Cdd:cd03268 1 LKTNDLTKTYG-----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeitfdGKSYQKNiEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 FVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERaaeqLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLD 158
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 159 EPFAALDE--ITRFRlndELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEM 218
Cdd:cd03268 152 EPTNGLDPdgIKELR---ELILSLRDQGITVLISSHLLSEIQKVADRIGII--NKGKLIEEG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-217 |
5.84e-28 |
|
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: 104.82 E-value: 5.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS----APPGPGD---- 76
Cdd:cd03216 1 LELRGITKRFG-----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkevSFASPRDarra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -IGFVFQeptlmpwatvadnvrlpldlagvakaeareraaeqlarvglvdvaaafpreLSGGMRMRAALARALVTRPRVL 155
Cdd:cd03216 76 gIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 156 LLDEPFAALDEITRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVL--RDGRVVGT 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
6.49e-28 |
|
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: 111.31 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTA----GGVHW------SA 70
Cdd:COG4172 3 SMPLLSVEDLSVAFG-QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFdgqdllGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 71 PP-------GpGDIGFVFQEP--TLMPWATVADNVRLPLDL-AGVAKAEARERAAEQLARVGLVDVA---AAFPRELSGG 137
Cdd:COG4172 82 SErelrrirG-NRIAMIFQEPmtSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 138 MRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVfeGV--YLSTRIAVMspRPGRIV 215
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL--GVvrRFADRVAVM--RQGEIV 236
|
250
....*....|....*...
gi 501562166 216 AEMAVD--LPRPRRPYLR 231
Cdd:COG4172 237 EQGPTAelFAAPQHPYTR 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-193 |
8.44e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 8.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRyapggTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA------PPGP-- 74
Cdd:PRK10247 6 PLLQLQNVGYL-----AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlKPEIyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 GDIGFVFQEPTLMPwATVADNVRLPLDLAGvaKAEARERAAEQLARVGLVDVAAAFP-RELSGGMRMRAALARALVTRPR 153
Cdd:PRK10247 81 QQVSYCAQTPTLFG-DTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501562166 154 VLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHS 193
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-192 |
1.11e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.01 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 18 GTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappGPGDIGFVFQ---EPTLMPwATVAD 94
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---GGARVAYVPQrseVPDSLP-LTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRL----PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:NF040873 77 LVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|..
gi 501562166 171 RLNDeLLALWQETGVTALFVTH 192
Cdd:NF040873 157 RIIA-LLAEEHARGATVVVVTH 177
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-229 |
1.16e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.55 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPGgtagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP------ 74
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPR-----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlya 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 -----------GDIGFVFQEPT--LMPWATVADNVRLPLDLAGVAKAEARERAAEQ-LARVglvDVAAA----FPRELSG 136
Cdd:PRK11701 78 lseaerrrllrTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDwLERV---EIDAAriddLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 137 GMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQGRVVE 232
|
250
....*....|....*
gi 501562166 217 EMAVD--LPRPRRPY 229
Cdd:PRK11701 233 SGLTDqvLDDPQHPY 247
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-192 |
1.79e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 105.63 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP------------GPGDIGFVFQEPTLMPWATV 92
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdeearaklRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRL 172
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|
gi 501562166 173 NDELLALWQETGVTALFVTH 192
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTH 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-217 |
2.83e-27 |
|
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: 104.58 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYApggtaGTEALADVGLTVARGEFVsLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD-------IGFV 80
Cdd:cd03264 4 ENLTKRYG-----KKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQpqklrrrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 81 FQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEP 160
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 161 FAALD--EITRFRlndELLALwQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:cd03264 158 TAGLDpeERIRFR---NLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLN--KGKLVFE 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-217 |
5.73e-27 |
|
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: 104.05 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPP------GpgdIGFVFQEPTLMP 88
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditGLPPheraraG---IGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 89 WATVADNVRLpldlagVAKAEARERAAEQLARvglvdVAAAFPR----------ELSGGMRMRAALARALVTRPRVLLLD 158
Cdd:cd03224 89 ELTVEENLLL------GAYARRRAKRKARLER-----VYELFPRlkerrkqlagTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 159 EPFAAL-----DEITRF--RLNDEllalwqetGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:cd03224 158 EPSEGLapkivEEIFEAirELRDE--------GVTILLVEQNARFALEIADRAYVL--ERGRVVLE 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-168 |
6.75e-27 |
|
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: 104.16 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------------HWSAPP 72
Cdd:cd03218 1 LRAENLSKRYG-----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 GpgdIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRP 152
Cdd:cd03218 76 G---IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170
....*....|....*.
gi 501562166 153 RVLLLDEPFAALDEIT 168
Cdd:cd03218 153 KFLLLDEPFAGVDPIA 168
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-221 |
7.55e-27 |
|
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: 104.40 E-value: 7.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV---------HWSAPP 72
Cdd:COG1119 1 DPLLELRNVTVRRG-----GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerrgGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 GPGDIGFV-------FQEP-------------TLMPWATVADNVRlplDLAgvakaeareraAEQLARVGLVDVAAAFPR 132
Cdd:COG1119 76 LRKRIGLVspalqlrFPRDetvldvvlsgffdSIGLYREPTDEQR---ERA-----------RELLELLGLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 133 ELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPG 212
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDG 219
|
....*....
gi 501562166 213 RIVAEMAVD 221
Cdd:COG1119 220 RVVAAGPKE 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-216 |
8.27e-27 |
|
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: 108.70 E-value: 8.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYAPGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGP 74
Cdd:COG4987 332 PSLELEDVSFRYPGAGRP---VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 GDIGFVFQEPTLMPwATVADNVRL------PLDLAGVakaeareraaeqLARVGLVDVAAAFP-----------RELSGG 137
Cdd:COG4987 409 RRIAVVPQRPHLFD-TTLRENLRLarpdatDEELWAA------------LERVGLGDWLAALPdgldtwlgeggRRLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 138 MRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHsVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITH-RLAGLERMDRILVL--EDGRIVE 549
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-216 |
2.28e-26 |
|
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: 102.28 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH------WSAPPGP--GDIGFVFQEPTLMpWATVA 93
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdiRQLDPADlrRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNvrlpLDLAGVAKAEARERAAEQLArvGLVDVAAAFP-----------RELSGGMRMRAALARALVTRPRVLLLDEPFA 162
Cdd:cd03245 96 DN----ITLGAPLADDERILRAAELA--GVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 163 ALDEITRFRLNDELLALWQETgvTALFVTH--SVFEgvyLSTRIAVMspRPGRIVA 216
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDK--TLIIITHrpSLLD---LVDRIIVM--DSGRIVA 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-192 |
2.38e-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: 100.75 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYapgGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP----GPGD---- 76
Cdd:cd03246 1 LEVENVSFRY---PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwDPNElgdh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 IGFVFQEPTLMPwATVADNVrlpldlagvakaeareraaeqlarvglvdvaaafpreLSGGMRMRAALARALVTRPRVLL 156
Cdd:cd03246 78 VGYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 501562166 157 LDEPFAALDEITRFRLNDELLALwQETGVTALFVTH 192
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH 154
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-193 |
4.77e-26 |
|
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: 106.22 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYaPGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGP 74
Cdd:TIGR02857 320 SSLEFSGVSVAY-PGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvplaDADADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 GDIGFVFQEPTLMPwATVADNVRLPLDLAGVAKAEAReraaeqLARVGLVDVAAAFP-----------RELSGGMRMRAA 143
Cdd:TIGR02857 396 DQIAWVPQHPFLFA-GTIAENIRLARPDASDAEIREA------LERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501562166 144 LARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHS 193
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-168 |
1.10e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.87 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWS---- 69
Cdd:COG1137 1 MMTLEAENLVKSYG-----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfldgeditHLPmhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 70 APPGpgdIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALV 149
Cdd:COG1137 76 ARLG---IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170
....*....|....*....
gi 501562166 150 TRPRVLLLDEPFAALDEIT 168
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIA 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-217 |
1.12e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.25 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGgtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVhwsappgpgD------ 76
Cdd:COG1132 343 ENVSFSYPGD----RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrilidGV---------Dirdltl 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 ------IGFVFQEPTLMPwATVADNVRL---PLDLAGVAKAeareraaeqLARVGLVDVAAAFP-----------RELSG 136
Cdd:COG1132 410 eslrrqIGVVPQDTFLFS-GTIRENIRYgrpDATDEEVEEA---------AKAAQAHEFIEALPdgydtvvgergVNLSG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 137 GMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHSvfegvyLST-----RIAVMSprP 211
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHR------LSTirnadRILVLD--D 549
|
....*.
gi 501562166 212 GRIVAE 217
Cdd:COG1132 550 GRIVEQ 555
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-230 |
7.16e-25 |
|
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: 98.52 E-value: 7.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW------SAPP--- 72
Cdd:COG0410 1 MPMLEVENLHAGYG-----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgeditGLPPhri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 ---GpgdIGFVFQE----PTLmpwaTVADNVRLpldlaGVAKAEARERAAEQLARVglvdvAAAFPR----------ELS 135
Cdd:COG0410 76 arlG---IGYVPEGrrifPSL----TVEENLLL-----GAYARRDRAEVRADLERV-----YELFPRlkerrrqragTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 136 GGMRMRAALARALVTRPRVLLLDEPFAAL-----DEITRF--RLNDEllalwqetGVTALFVTHSVFEGVYLSTRIAVMs 208
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivEEIFEIirRLNRE--------GVTILLVEQNARFALEIADRAYVL- 209
|
250 260
....*....|....*....|....*..
gi 501562166 209 pRPGRIV-----AEMAVDlPRPRRPYL 230
Cdd:COG0410 210 -ERGRIVlegtaAELLAD-PEVREAYL 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-217 |
8.54e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.80 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS-APPGPGD---IGFVFQE 83
Cdd:COG4152 5 KGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgEPLDPEDrrrIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 84 PTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAA 163
Cdd:COG4152 80 RGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501562166 164 LDEITRFRLNDELLALwQETGVTALFVTH---SVFEgvyLSTRIAVMspRPGRIVAE 217
Cdd:COG4152 160 LDPVNVELLKDVIREL-AAKGTTVIFSSHqmeLVEE---LCDRIVII--NKGRKVLS 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
25-207 |
1.01e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgpGD-------------IGFVFQEP-TLMPWA 90
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-----GDllteenvwdirhkIGMVFQNPdNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 TVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 501562166 171 RLNDELLALWQETGVTALFVTHSVFEgVYLSTRIAVM 207
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-192 |
1.11e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVhwsappGPGDI----------------------G 78
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI------RVGDItidtarslsqqkglirqlrqhvG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 FVFQEPTLMPWATVADNV-RLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLL 157
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 501562166 158 DEPFAALD-EITRFRLNdELLALWQETGvTALFVTH 192
Cdd:PRK11264 169 DEPTSALDpELVGEVLN-TIRQLAQEKR-TMVIVTH 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-196 |
2.33e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 98.30 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 26 ADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG-----------DIGFVFQEPTLMPWATVAD 94
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsrlytvrkRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPL-DLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITR---F 170
Cdd:PRK11831 104 NVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMgvlV 183
|
170 180
....*....|....*....|....*..
gi 501562166 171 RLNDEL-LALwqetGVTALFVTHSVFE 196
Cdd:PRK11831 184 KLISELnSAL----GVTCVVVSHDVPE 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-217 |
2.61e-24 |
|
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: 96.67 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPP--GPGDIGFVFQEPTLMPWATVADNV 96
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfatvdGFDVVKEPaeARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 97 RLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDEL 176
Cdd:cd03266 100 EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501562166 177 LALwQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:cd03266 180 RQL-RALGKCILFSTHIMQEVERLCDRVVVLH--RGRVVYE 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-192 |
5.40e-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: 95.79 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP-----GDIGFVFQEPTLMPW-ATVAD 94
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrKSIGYVMQDVDYQLFtDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGvakaEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:cd03226 92 ELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170
....*....|....*...
gi 501562166 175 ELLALwQETGVTALFVTH 192
Cdd:cd03226 168 LIREL-AAQGKAVIVITH 184
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-215 |
6.98e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.43 E-value: 6.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH------WSAPPGPGDI---- 77
Cdd:PRK13637 6 ENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvdiTDKKVKLSDIrkkv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 78 GFVFQEPTLMPWA-TVADNVRL-PLDLaGVAKAEARERAAEQLARVGLV--DVAAAFPRELSGGMRMRAALARALVTRPR 153
Cdd:PRK13637 86 GLVFQYPEYQLFEeTIEKDIAFgPINL-GLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 154 VLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIV 215
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMN--KGKCE 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-217 |
1.32e-23 |
|
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: 95.48 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH------WSAPPG-PGDIGFVFQEPTLMPW-ATVAD 94
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRKKfLRRIGVVFGQKTQLWWdLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERA-----AEQLARvgLVDVAAafpRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITR 169
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLdelseLLDLEE--LLDTPV---RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501562166 170 FRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID--KGRLLYD 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
2.13e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYapGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS----APPGPGD 76
Cdd:COG3845 2 MPPALELRGITKRF--GGVV---ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvRIRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -----IGFVFQEPTLMPWATVADNVRLpldlaGVAKAEARERAAEQLARVgLVDVAAAFP---------RELSGGMRMRA 142
Cdd:COG3845 77 aialgIGMVHQHFMLVPNLTVAENIVL-----GLEPTKGGRLDRKAARAR-IRELSERYGldvdpdakvEDLSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 143 ALARALVTRPRVLLLDEPFAAL--DEItrfrlnDELLALWQ---ETGVTALFVTH---SVFEgvyLSTRIAVMspRPGRI 214
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLtpQEA------DELFEILRrlaAEGKSIIFITHklrEVMA---IADRVTVL--RRGKV 219
|
....*..
gi 501562166 215 VAEMAVD 221
Cdd:COG3845 220 VGTVDTA 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-160 |
2.28e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVhwSAPPGpGDIGFVFQEPTLM 87
Cdd:COG0488 2 ENLSKSFG-----GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--SIPKG-LRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 88 PWATVADNV--------RLPLDLAGVAKAEARERAAEQ------------------------LARVGLVDVAAAFP-REL 134
Cdd:COG0488 74 DDLTVLDTVldgdaelrALEAELEELEAKLAEPDEDLErlaelqeefealggweaearaeeiLSGLGFPEEDLDRPvSEL 153
|
170 180
....*....|....*....|....*.
gi 501562166 135 SGGMRMRAALARALVTRPRVLLLDEP 160
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-217 |
3.51e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.77 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGPGDIGFVFQEPtLM---PWATV 92
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtKLPEYKRAKYIGRVFQDP-MMgtaPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRL------PLDLAGVAKAEARERAAEQLARVGL-----VDVAAAFpreLSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:COG1101 100 EENLALayrrgkRRGLRRGLTKKRRELFRELLATLGLglenrLDTKVGL---LSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501562166 162 AALD--------EITrfrlnDELLAlwqETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:COG1101 177 AALDpktaalvlELT-----EKIVE---ENNLTTLMVTHNMEQALDYGNRLIMMH--EGRIILD 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-194 |
3.87e-23 |
|
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: 93.30 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsappgPGDIGFVFQEPTLM 87
Cdd:cd03250 4 EDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----PGSIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 88 PwATVADNVR--LPLDlagvakaeareraAEQLARVglVDVAA------AFPR-------E----LSGGMRMRAALARAL 148
Cdd:cd03250 79 N-GTIRENILfgKPFD-------------EERYEKV--IKACAlepdleILPDgdlteigEkginLSGGQKQRISLARAV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501562166 149 VTRPRVLLLDEPFAALDEITRFRLNDE-LLALWQEtGVTALFVTHSV 194
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLN-NKTRILVTHQL 188
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-229 |
4.53e-23 |
|
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: 94.51 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPGgtagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP------- 74
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGG-----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAelelyql 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 ----------GDIGFVFQEPT--LMPWATVADNV-RLPLDLAGVAKAEARERAAEQLARVGL-VDVAAAFPRELSGGMRM 140
Cdd:TIGR02323 76 seaerrrlmrTEWGFVHQNPRdgLRMRVSAGANIgERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 141 RAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAV 220
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRVVESGLT 233
|
250
....*....|.
gi 501562166 221 D--LPRPRRPY 229
Cdd:TIGR02323 234 DqvLDDPQHPY 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-238 |
5.66e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 94.70 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 13 RYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW-----SAPPGPGD-------IGFV 80
Cdd:PRK13634 11 RYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgerviTAGKKNKKlkplrkkVGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 81 FQEPTLMPW-ATVADNVRL-PLDLaGVAKAEARERAAEQLARVGLV-DVAAAFPRELSGG-MRmRAALARALVTRPRVLL 156
Cdd:PRK13634 91 FQFPEHQLFeETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPeELLARSPFELSGGqMR-RVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 157 LDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVM---------SPRP----GRIVAEMAVDLP 223
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMhkgtvflqgTPREifadPDELEAIGLDLP 248
|
250
....*....|....*
gi 501562166 224 RPRRPYLRTEAGFGV 238
Cdd:PRK13634 249 ETVKFKRALEEKFGI 263
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-221 |
6.13e-23 |
|
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: 93.59 E-value: 6.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPP----TAGGVHWSAPPGPG------DIGFVFQEP--TLMPWATVAD 94
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPlsirgrHIATIMQNPrtAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVA---AAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFR 171
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501562166 172 LNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAVD 221
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMD--DGRIVERGTVK 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-192 |
1.58e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYaPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPG 75
Cdd:PRK10535 1 MTALLELKDIRRSY-PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvaGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 -------DIGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARAL 148
Cdd:PRK10535 80 laqlrreHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501562166 149 VTRPRVLLLDEPFAALDEitrfRLNDELLAL---WQETGVTALFVTH 192
Cdd:PRK10535 160 MNGGQVILADEPTGALDS----HSGEEVMAIlhqLRDRGHTVIIVTH 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-194 |
2.19e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.36 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 14 YAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPGD-------IGFVF 81
Cdd:PRK13641 12 YSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGtitiaGYHITPETGNKNlkklrkkVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 82 QEPTLMPWA-TVADNVRL-PLDLaGVAKAEARERAAEQLARVGL-VDVAAAFPRELSGGMRMRAALARALVTRPRVLLLD 158
Cdd:PRK13641 92 QFPEAQLFEnTVLKDVEFgPKNF-GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 501562166 159 EPFAALDEITRFRLNdELLALWQETGVTALFVTHSV 194
Cdd:PRK13641 171 EPAAGLDPEGRKEMM-QLFKDYQKAGHTVILVTHNM 205
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-250 |
3.03e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.49 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAP-----GGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSA 70
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGelyyqGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 71 PPGPG------DIGFVFQEP--TLMPWATVADNVRLPLDL-AGVAKAEARERAAEQLARVGL-VDVAAAFPRELSGGMRM 140
Cdd:PRK11308 82 ADPEAqkllrqKIQIVFQNPygSLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 141 RAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH--SVFEgvylstRIA--VMSPRPGRIV- 215
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHdlSVVE------HIAdeVMVMYLGRCVe 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 501562166 216 -AEMAVDLPRPRRPYLRteagfgvlcreasALLAAA 250
Cdd:PRK11308 236 kGTKEQIFNNPRHPYTQ-------------ALLSAT 258
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-192 |
3.30e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------------HWSAP 71
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstskQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 72 PGPGDIGFVFQEP-TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLV-DVAAAFPRELSGGMRMRAALARALV 149
Cdd:PRK13643 81 PVRKKVGVVFQFPeSQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501562166 150 TRPRVLLLDEPFAALDEITRFrlndELLALWQ---ETGVTALFVTH 192
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARI----EMMQLFEsihQSGQTVVLVTH 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-193 |
3.37e-22 |
|
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: 91.44 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG------GVHWsaPPGPGdIGFvfqeptlMPWATVADNVR 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtvtvrgRVSS--LLGLG-GGF-------NPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 98 LPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEitRFRLN-DEL 176
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA--AFQEKcQRR 184
|
170
....*....|....*..
gi 501562166 177 LALWQETGVTALFVTHS 193
Cdd:cd03220 185 LRELLKQGKTVILVSHD 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-207 |
4.72e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPggtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLI--AGLLPP---TAGGVHWSAPP--G 73
Cdd:PRK14239 2 TEPILQVSDLSVYYNK-----KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNiyS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 74 P--------GDIGFVFQEPTLMPWaTVADNVRLPLDLAGVAKAEARERAAEQLARVG---------LVDVAAAfpreLSG 136
Cdd:PRK14239 77 PrtdtvdlrKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGAsiwdevkdrLHDSALG----LSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 137 GMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQEtgVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFF 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-207 |
5.80e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.85 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG-----------DIGFVFQEP--TLMPWA 90
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddewravrsDIQMIFQDPlaSLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 TVADNVRLPLDL--AGVAKAEARERAAEQLARVGLV-DVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEI 167
Cdd:PRK15079 116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501562166 168 TRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-231 |
1.10e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPGG------TAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA----- 70
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridt 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 71 ------PPGPGDIGFVFQEP--TLMPWATVADNVRLPLDLAGVAKAEARERAAEQL-ARVGLV-DVAAAFPRELSGGMRM 140
Cdd:PRK10261 391 lspgklQALRRDIQFIFQDPyaSLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLlERVGLLpEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 141 RAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVaEMAv 220
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY--LGQIV-EIG- 546
|
250
....*....|....*..
gi 501562166 221 dlPR------PRRPYLR 231
Cdd:PRK10261 547 --PRravfenPQHPYTR 561
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-217 |
1.26e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.91 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD----------IGFVFQEPTLMPWA 90
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksllevrktVGIVFQNPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 -TVADNVRL-PLDLaGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD--- 165
Cdd:PRK13639 94 pTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmg 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501562166 166 --EITR--FRLNDEllalwqetGVTALFVTHSV-FEGVYlSTRIAVMSprPGRIVAE 217
Cdd:PRK13639 173 asQIMKllYDLNKE--------GITIIISTHDVdLVPVY-ADKVYVMS--DGKIIKE 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-217 |
2.11e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.53 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPGG-TAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH------------ 67
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 68 WsappgpgDI----GFVFQEPTLMPWAT-VADNVRL-PLDLaGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMR 141
Cdd:PRK13633 81 W-------DIrnkaGMVFQNPDNQIVATiVEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 142 AALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYlSTRIAVMSprPGRIVAE 217
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMD--SGKVVME 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-198 |
3.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.86 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPP--------TAGGVH------WSAPPgpgDIGFVFQEP-TLMP 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITltaktvWDIRE---KVGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 89 WATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190
....*....|....*....|....*....|
gi 501562166 169 RFRLNDELLALWQETGVTALFVTHSVFEGV 198
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEAN 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-192 |
4.27e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.48 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTaggvhwsappgPGDIGFVFQEPTLMPWATVADNVRLPLDLAG 104
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT-----------PVAGCVDVPDNQFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 105 VAKAeareraaeqLARVGLVDVAA--AFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQE 182
Cdd:COG2401 115 AVEL---------LNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARR 185
|
170
....*....|
gi 501562166 183 TGVTALFVTH 192
Cdd:COG2401 186 AGITLVVATH 195
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-172 |
4.51e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGgvHWSAPPGpGDIGFVFQEPtLMPWATVADNVRLPLDLAG 104
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RIARPAG-ARVLFLPQRP-YLPLGTLREALLYPATAEA 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501562166 105 VAKAEARERaaeqLARVGL------VDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRL 172
Cdd:COG4178 455 FSDAELREA----LEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-165 |
4.57e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAP--- 71
Cdd:PRK13548 1 AMLEARNLSVRLG-----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrplaDWSPAela 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 72 ------PGPGDIGFVFqeptlmpwaTVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALA 145
Cdd:PRK13548 76 rrravlPQHSSLSFPF---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180
....*....|....*....|....*.
gi 501562166 146 RALV------TRPRVLLLDEPFAALD 165
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALD 172
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-219 |
5.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.38 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPggTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD---- 76
Cdd:PRK13642 1 MNKILEVENLVFKYEK--ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvwn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 ----IGFVFQEP-TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTR 151
Cdd:PRK13642 79 lrrkIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 152 PRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYlSTRIAVMspRPGRIVAEMA 219
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVM--KAGEIIKEAA 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-216 |
6.07e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 91.73 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 11 GLRYAPGGtAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSappgPGD----IG 78
Cdd:COG4618 335 NLTVVPPG-SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQWD----REElgrhIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 FVFQEPTLMPwATVADNVrlpldlagvakaeareraaeqlARVGLVD----VAAA-----------FP-----------R 132
Cdd:COG4618 410 YLPQDVELFD-GTIAENI----------------------ARFGDADpekvVAAAklagvhemilrLPdgydtrigeggA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 133 ELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALwQETGVTALFVTH--SVFEGVylsTRIAVMspR 210
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHrpSLLAAV---DKLLVL--R 540
|
....*.
gi 501562166 211 PGRIVA 216
Cdd:COG4618 541 DGRVQA 546
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-165 |
7.04e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.03 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGDIGFVFQE-------PTLMPWATVA 93
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylghlPGLKPELSAL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 94 DNVRLPLDLAGvakaEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:TIGR01189 92 ENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-192 |
1.04e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAP------PGPGDIG---------------FVF 81
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrDKDGQLKvadknqlrllrtrltMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 82 QEPTLMPWATVADNV-RLPLDLAGVAKAEARERAAEQLARVGLVDVA-AAFPRELSGGMRMRAALARALVTRPRVLLLDE 159
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 501562166 160 PFAALDEitrfRLNDELLALWQ---ETGVTALFVTH 192
Cdd:PRK10619 179 PTSALDP----ELVGEVLRIMQqlaEEGKTMVVVTH 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-192 |
1.73e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsappGPG-DIGFVF 81
Cdd:COG0488 314 KVLELEGLSKSYG-----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----GETvKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 82 QEP-TLMPWATVADNVRlpldlaGVAKAEARERAAEQLARVGlvdvaaaFPRE--------LSGGMRMRAALARALVTRP 152
Cdd:COG0488 385 QHQeELDPDKTVLDELR------DGAPGGTEQEVRGYLGRFL-------FSGDdafkpvgvLSGGEKARLALAKLLLSPP 451
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501562166 153 RVLLLDEPFAALDEITRFRLNdELLALWQetGvTALFVTH 192
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALE-EALDDFP--G-TVLLVSH 487
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-215 |
1.98e-20 |
|
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: 86.82 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV-------------HWSAppgpgDIGFVFQEPTLMPw 89
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRS-----QIGLVSQEPVLFD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNVRLPLDLAGVAKAEareraaeQLARV-GLVDVAAAFPR-----------ELSGGMRMRAALARALVTRPRVLLL 157
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVE-------EAAKKaNIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 158 DEPFAALDEITRfrlndellALWQET------GVTALFVTHSvfegvyLST-----RIAVMSprPGRIV 215
Cdd:cd03249 164 DEATSALDAESE--------KLVQEAldramkGRTTIVIAHR------LSTirnadLIAVLQ--NGQVV 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-193 |
2.14e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW----SAPPGPGdIGFvfqeptlMPWATVADNVRLp 99
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVngrvSALLELG-AGF-------HPELTGRENIYL- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 100 ldlagvakaeareraaeqlarVGLV------DVAAAFPR-----EL-----------SGGMRMRAALARALVTRPRVLLL 157
Cdd:COG1134 112 ---------------------NGRLlglsrkEIDEKFDEivefaELgdfidqpvktySSGMRARLAFAVATAVDPDILLV 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 501562166 158 DEPFAALDEitRFR--LNDELLALWQEtGVTALFVTHS 193
Cdd:COG1134 171 DEVLAVGDA--AFQkkCLARIRELRES-GRTVIFVSHS 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-207 |
3.08e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.15 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP-GPGDIGF-------VFQEPT--LMPWATV 92
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlHFGDYSYrsqrirmIFQDPStsLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRLPLDL-AGVAKAEARERAAEQLARVGLV-DVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:PRK15112 107 SQILDFPLRLnTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 501562166 171 RLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-165 |
3.18e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsaPPGPGDIGFVFQEPT-------LMPWATVA 93
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL--DGGDIDDPDVAEACHylghrnaMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 94 DNVRLPLDLAGvakaEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PRK13539 92 ENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
3.97e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.63 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLR-------LIAGllpptaggVHWSappg 73
Cdd:COG1117 8 LEPKIEVRNLNVYYG-----DKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG--------ARVE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 74 pGDI---------------------GFVFQEPTLMPWaTVADNVRLPLDLAGVAKAEARERAAEQ-LARVGLVD-V---- 126
Cdd:COG1117 71 -GEIlldgediydpdvdvvelrrrvGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEEsLRKAALWDeVkdrl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 127 -AAAFprELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQEtgVTALFVTHSVFEGVYLSTRIA 205
Cdd:COG1117 149 kKSAL--GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTA 224
|
250
....*....|
gi 501562166 206 VMSprPGRIV 215
Cdd:COG1117 225 FFY--LGELV 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
6.38e-20 |
|
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: 88.57 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPGgtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPGD 76
Cdd:TIGR02868 332 KPTLELRDLSAGYPGA----PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 ---IGFVFQEPTLMPwATVADNVRLpldlagVAKAEARERAAEQLARVGLVDVAAAFP-----------RELSGGMRMRA 142
Cdd:TIGR02868 408 rrrVSVCAQDAHLFD-TTVRENLRL------ARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501562166 143 ALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALwqETGVTALFVTHS 193
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-217 |
6.43e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 6.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYAPGgtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP----GPG---- 75
Cdd:PRK13636 5 ILKVEELNYNYSDG----THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysRKGlmkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 --DIGFVFQEPTLMPW-ATVADNVRL-PLDLaGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTR 151
Cdd:PRK13636 81 reSVGMVFQDPDNQLFsASVYQDVSFgAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 152 PRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK--EGRVILQ 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-165 |
9.44e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.55 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH--------WSAP---- 71
Cdd:COG4559 1 MLEAENLSVRLG-----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaaWSPWelar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 72 -----PGPGDIGFVFqeptlmpwaTVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALAR 146
Cdd:COG4559 76 rravlPQHSSLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLAR 146
|
170 180
....*....|....*....|....*.
gi 501562166 147 ALV-------TRPRVLLLDEPFAALD 165
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALD 172
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
1.03e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPggtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTA---------GGVHWSAP 71
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQ-----HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 72 PGPGDI-------GFVFQEPTLMPWATVADNVRL------PLDLAGVA--KAEARERAAEQLARVGLVDVAAAFPRELSG 136
Cdd:PRK09984 76 RLARDIrksrantGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 137 GMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRI 214
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHV 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-219 |
1.09e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD-------IGFVFQEPTLMPWATVADNVRLP 99
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRarharqrVGVVPQFDNLDPDFTVRENLLVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 100 LDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLAL 179
Cdd:PRK13537 105 GRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501562166 180 WQeTGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMA 219
Cdd:PRK13537 185 LA-RGKTILLTTHFMEEAERLCDRLCVIE--EGRKIAEGA 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-192 |
1.34e-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: 84.08 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 28 VGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsaPPGPGDigfvFQEPTL---MPWATVADNVRLPL---- 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL--NGGPLD----FQRDSIargLLYLGHAPGIKTTLsvle 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 101 DLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLnDELLALW 180
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF-AEAMAGH 171
|
170
....*....|..
gi 501562166 181 QETGVTALFVTH 192
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-209 |
1.39e-19 |
|
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: 84.41 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPGGTAGTE--ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD-- 76
Cdd:COG4778 1 MTTLLEVENLSKTFTLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 --------------IGFVFQEPTLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLvdvaaafPREL-------- 134
Cdd:COG4778 81 qaspreilalrrrtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatf 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501562166 135 SGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALwQETGVTALFVTH--SVFEGVylSTRIAVMSP 209
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHdeEVREAV--ADRVVDVTP 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-231 |
1.52e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGLRYAPGGTAGTeALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPptaggvhwsAPPG---PGDIGF 79
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRT-VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLP---------SPPVvypSGDIRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 -----------------------VFQEP--TLMPWATVADNVRLPLDL-AGVAKAEARERAAEQLARVGLVDVA---AAF 130
Cdd:PRK15134 74 hgesllhaseqtlrgvrgnkiamIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAkrlTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 131 PRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspR 210
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--Q 231
|
250 260
....*....|....*....|...
gi 501562166 211 PGRIVAEMAVD--LPRPRRPYLR 231
Cdd:PRK15134 232 NGRCVEQNRAAtlFSAPTHPYTQ 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
25-192 |
2.67e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.34 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsapPGPGDIGFVFQeptlmpwatvadnvrlpldlag 104
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW---GSTVKIGYFEQ---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 105 vakaeareraaeqlarvglvdvaaafpreLSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELlalwQETG 184
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----KEYP 117
|
....*...
gi 501562166 185 VTALFVTH 192
Cdd:cd03221 118 GTVILVSH 125
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-165 |
3.68e-19 |
|
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: 83.69 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV----HWSAPPGPG----DIGF 79
Cdd:cd03252 4 EHVRFRYKPDGP---VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdgHDLALADPAwlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEPTLMPwATVADNVRLpldlAGVAKAEARERAAEQLARvglvdvAAAFPRE---------------LSGGMRMRAAL 144
Cdd:cd03252 81 VLQENVLFN-RSIRDNIAL----ADPGMSMERVIEAAKLAG------AHDFISElpegydtivgeqgagLSGGQRQRIAI 149
|
170 180
....*....|....*....|.
gi 501562166 145 ARALVTRPRVLLLDEPFAALD 165
Cdd:cd03252 150 ARALIHNPRILIFDEATSALD 170
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-207 |
4.20e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 40 LLGSSGCGKSTLLRLIAGLLPPTAGGVHW------------SAPPGPGDIGFVFQEPTLMPWATVADNVRLpldlaGVAK 107
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaekgiCLPPEKRRIGYVFQDARLFPHYKVRGNLRY-----GMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 108 AEAReraaeQLAR-VGLVDVAA---AFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDeITRFRlndELLA----L 179
Cdd:PRK11144 104 SMVA-----QFDKiVALLGIEPlldRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKR---ELLPylerL 174
|
170 180
....*....|....*....|....*...
gi 501562166 180 WQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK11144 175 AREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-215 |
5.22e-19 |
|
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: 82.21 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 18 GTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTA--GGVHWSAPPGPGD-----IGFVFQEPTLMPWA 90
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRsfrkiIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 TVADNVRLpldlagvakaeareraaeqlarvglvdvaAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:cd03213 98 TVRETLMF-----------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501562166 171 RLNDELLALWQeTGVTALFVTHSV-FEGVYLSTRIAVMSprPGRIV 215
Cdd:cd03213 149 QVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLS--QGRVI 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-217 |
6.54e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD-------IGFVFQEPTLMPWATVADNVRLP 99
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARarlararIGVVPQFDNLDLEFTVRENLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 100 LDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLAL 179
Cdd:PRK13536 139 GRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL 218
|
170 180 190
....*....|....*....|....*....|....*...
gi 501562166 180 WQEtGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:PRK13536 219 LAR-GKTILLTTHFMEEAERLCDRLCVL--EAGRKIAE 253
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-192 |
6.64e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGT----EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPGDI-------GFVFQE 83
Cdd:PRK13649 14 AGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvdDTLITSTSKNKDIkqirkkvGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 84 PTLMPWA-TVADNVRLPLDLAGVAKAEARERAAEQLARVGLV-DVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:PRK13649 94 PESQLFEeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190
....*....|....*....|....*....|....
gi 501562166 162 AALDEITRfrlnDELLALWQ---ETGVTALFVTH 192
Cdd:PRK13649 174 AGLDPKGR----KELMTLFKklhQSGMTIVLVTH 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-193 |
1.63e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.89 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsapPGPGDIGFVFQEPtLMPWATVADNVRLPLDlag 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---PEGEDLLFLPQRP-YLPLGTLREQLIYPWD--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 105 vakaeareraaeqlarvglvdvaaafpRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRlndeLLALWQETG 184
Cdd:cd03223 90 ---------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR----LYQLLKELG 138
|
....*....
gi 501562166 185 VTALFVTHS 193
Cdd:cd03223 139 ITVISVGHR 147
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-165 |
1.72e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.00 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 30 LTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP----GP---GDIGFVFQEPTLMPWATVADNVRLPLDL 102
Cdd:PRK13538 22 FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqRDeyhQDLLYLGHQPGIKTELTALENLRFYQRL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 103 AGVAKAEARERAaeqLARVGLV---DVAAafpRELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PRK13538 102 HGPGDDEALWEA---LAQVGLAgfeDVPV---RQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-221 |
4.19e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.39 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 19 TAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD--------IGFVFQEPTLMPWA 90
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevrkfVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 -TVADNVRL-PLDLaGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:PRK13652 94 pTVEQDIAFgPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501562166 169 RFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAVD 221
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMD--KGRIVAYGTVE 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-215 |
4.34e-18 |
|
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: 80.39 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLP--PTAGGVHW--SAPPGPGD----IGFVFQEPTLMPWATVAD-- 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEggGTTSGQILfnGQPRKPDQfqkcVAYVRQDDILLPGLTVREtl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 ----NVRLPLDLAGvaKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:cd03234 103 tytaILRLPRKSSD--AIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501562166 171 RLNdELLALWQETGVTALFVTH----SVFEgvyLSTRIAVMSprPGRIV 215
Cdd:cd03234 181 NLV-STLSQLARRNRIVILTIHqprsDLFR---LFDRILLLS--SGEIV 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-216 |
1.03e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP-------- 72
Cdd:PRK11288 1 SSPYLSFDGIGKTFP-----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfastta 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 --GPGdIGFVFQEPTLMPWATVADNV---RLPLDLAGVAKAEARERAAEQLARVGlVDVAAAFP-RELSGGMRMRAALAR 146
Cdd:PRK11288 76 alAAG-VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLG-VDIDPDTPlKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501562166 147 ALVTRPRVLLLDEPFAALD--EITR-FRLNDELLAlwqeTGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSarEIEQlFRVIRELRA----EGRVILYVSHRMEEIFALCDAITVF--KDGRYVA 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-207 |
1.05e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGL--LPPTA---GGVH------WSAPPGP----GDIGFVFQEPTLM 87
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRlfgrniYSPDVDPievrREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 88 PWATVADNVRLPLDLAGVAKAEARERAAEQ--LARVGLVDVAAA----FPRELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKKELDERVEwaLKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501562166 162 AALDEITRFRLNDELLALWQEtgVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFL 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-217 |
1.18e-17 |
|
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: 78.12 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPG--PGDIGFVFQEPTLMPwATVAD 94
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGeitldGVPVSDLEKalSSLISVLNQRPYLFD-TTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVrlpldlagvakaeareraaeqlarvglvdvaaafPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRfrlnD 174
Cdd:cd03247 94 NL----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE----R 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501562166 175 ELLALWQET--GVTALFVTHSVfEGVYLSTRIAVMSprPGRIVAE 217
Cdd:cd03247 136 QLLSLIFEVlkDKTLIWITHHL-TGIEHMDKILFLE--NGKIIMQ 177
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-232 |
1.52e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.36 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 26 ADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPP----TAGGVHWSAPP-GPGD-----IGFVFQEP--TLMPWATVA 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPvAPCAlrgrkIATIMQNPrsAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNVRLPLDLAGVAKAEARERAAeqLARVGLVD---VAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:PRK10418 100 THARETCLALGKPADDATLTAA--LEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501562166 171 RLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIV--AEMAVDLPRPRRPYLRT 232
Cdd:PRK10418 178 RILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMS--HGRIVeqGDVETLFNAPKHAVTRS 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-216 |
1.63e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------------HWSAPPGpgdIGFVFQEPTLMP 88
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRG---IGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 89 WATVADNVRLPLDLAGVAKAEARERAAEQL-ARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEI 167
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLSAEQREDRANELmEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501562166 168 TRFRLNdELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVA 216
Cdd:PRK10895 172 SVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVS--QGHLIA 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-217 |
1.65e-17 |
|
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: 78.81 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG--------DIGFVFQEPTLMPwATV 92
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrkslrsMIGVVLQDTFLFS-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRLPLDLAGVAKAEAReraaeqLARVGLVDVAAAFPR-----------ELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:cd03254 94 MENIRLGRPNATDEEVIEA------AKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 162 AALDEITRFRLNDELLALWQetGVTALFVTHSvfegvyLST-----RIAVMspRPGRIVAE 217
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMK--GRTSIIIAHR------LSTiknadKILVL--DDGKIIEE 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-192 |
2.49e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGgvhwSA-----PPGPGDI------GFVFQEPTLMPWATV 92
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEG----EAwlfgqPVDAGDIatrrrvGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRL 172
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180
....*....|....*....|.
gi 501562166 173 NDELLALWQETGVTaLFV-TH 192
Cdd:NF033858 437 WRLLIELSREDGVT-IFIsTH 456
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
5.42e-17 |
|
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: 76.32 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYApggtagteaLADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS----APPGPGD- 76
Cdd:cd03215 2 EPVLEVRGLSVKGA---------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvTRRSPRDa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 ----IGFVFQEPT---LMPWATVADNVrlpldlagvakaeareraaeqlarvglvdvaaAFPRELSGGMRMRAALARALV 149
Cdd:cd03215 73 iragIAYVPEDRKregLVLDLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501562166 150 TRPRVLLLDEPFAALDEITRFRLNDELLALWQEtGVTALFVTHSVFEGVYLSTRIAVMspRPGRI 214
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVM--YEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-219 |
6.54e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRyapggtagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS----APPGPGD- 76
Cdd:COG1129 254 EVVLEVEGLSVG---------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkpvRIRSPRDa 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 ----IGFVfqepT-------LMPWATVADNVRLPLdlagvakaeareraAEQLARVGLVD------VAAAF--------P 131
Cdd:COG1129 325 iragIAYV----PedrkgegLVLDLSIRENITLAS--------------LDRLSRGGLLDrrreraLAEEYikrlriktP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 132 ------RELSGGMRMRAALARALVTRPRVLLLDEPFAALD-----EItrFRLNDELLAlwqeTGVTALFVTHSVFEGVYL 200
Cdd:COG1129 387 speqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakaEI--YRLIRELAA----EGKAVIVISSELPELLGL 460
|
250
....*....|....*....
gi 501562166 201 STRIAVMspRPGRIVAEMA 219
Cdd:COG1129 461 SDRILVM--REGRIVGELD 477
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.30e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.08 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPGgtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------------HW 68
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDG----TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaeneKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 69 SAppgpGDIGFVFQEPTLMPWA-TVADNVRL-PLDLaGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALAR 146
Cdd:PRK13647 77 VR----SKVGLVFQDPDDQVFSsTVWDDVAFgPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 147 ALVTRPRVLLLDEPFAALDEITRFRLNdELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVDL 222
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVL--KEGRVLAEGDKSL 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-192 |
1.33e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHwsappgP--------GDIGFVF-QEPTLMP 88
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGevrvlGYV------PfkrrkefaRRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 89 WATVADNVRL-------P--------------LDLAgvakaeareraaeqlarvGLVDVAAafpRELSGGMRMRAALARA 147
Cdd:COG4586 110 DLPAIDSFRLlkaiyriPdaeykkrldelvelLDLG------------------ELLDTPV---RQLSLGQRMRCELAAA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501562166 148 LVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH 192
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-217 |
1.46e-16 |
|
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: 76.50 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYAPggtAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGPGD 76
Cdd:cd03251 1 VEFKNVTFRYPG---DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdvrDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 IGFVFQEPTLMPwATVADNVRLPLDLAGvakaearERAAEQLAR-VGLVDVAAAFPR-----------ELSGGMRMRAAL 144
Cdd:cd03251 78 IGLVSQDVFLFN-DTVAENIAYGRPGAT-------REEVEEAARaANAHEFIMELPEgydtvigergvKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 145 ARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHSvfegvyLST-----RIAVMSprPGRIVAE 217
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHR------LSTienadRIVVLE--DGKIVER 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-217 |
2.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGPGDI-GFVFQEP-TLMPWA 90
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgDFSKLQGIRKLvGIVFQNPeTQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 TVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501562166 171 RLNDELLALwQETGVTALFVTHSVfEGVYLSTRIAVMSprPGRIVAE 217
Cdd:PRK13644 174 AVLERIKKL-HEKGKTIVYITHNL-EELHDADRIIVMD--RGKIVLE 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-207 |
3.18e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGP- 74
Cdd:PRK11300 2 SQPLLSVSGLMMRFG-----GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGtillrGQHIEGLPGHq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 -GDIGFV--FQEPTLMPWATVADN--------VRLPLdLAGVAKAEARERAAEQ--------LARVGLVDVAAAFPRELS 135
Cdd:PRK11300 77 iARMGVVrtFQHVRLFREMTVIENllvaqhqqLKTGL-FSGLLKTPAFRRAESEaldraatwLERVGLLEHANRQAGNLA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 136 GGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
24-216 |
3.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.80 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGP---GDIGFVFQEP-TLMPWATVAD 94
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGeikidGITISKENLKeirKKIGIIFQNPdNQFIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:PRK13632 104 DIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501562166 175 ELLALWQETGVTALFVTHSVFEgVYLSTRIAVMSprPGRIVA 216
Cdd:PRK13632 184 IMVDLRKTRKKTLISITHDMDE-AILADKVIVFS--EGKLIA 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-198 |
7.55e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD--------IGFVFQEP-TLMPWATVAD 94
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnfeklrkhIGIVFQNPdNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 95 NVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLND 174
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180
....*....|....*....|....
gi 501562166 175 ELLALWQETGVTALFVTHSVFEGV 198
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAM 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-194 |
7.65e-16 |
|
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: 74.29 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 19 TAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA--PPGPG----------DIGFVFQEPTL 86
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknESEPSfeatrsrnrySVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 87 MPwATVADNVRL--PLDLAGVAKAEARERAAEQLARVGLVDVAAAFPR--ELSGGMRMRAALARALVTRPRVLLLDEPFA 162
Cdd:cd03290 91 LN-ATVEENITFgsPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|...
gi 501562166 163 ALD-EITRFRLNDELLALWQETGVTALFVTHSV 194
Cdd:cd03290 170 ALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKL 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-215 |
8.29e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV----HWSAPPGPGD 76
Cdd:PRK15439 8 APPLLCARSISKQYS-----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -----IGFVFQEPTLMPWATVADNVrlpldLAGVAKAEARERAAEQL-----------ARVGLVDVAaafPRELSGGMR- 139
Cdd:PRK15439 83 ahqlgIYLVPQEPLLFPNLSVKENI-----LFGLPKRQASMQKMKQLlaalgcqldldSSAGSLEVA---DRQIVEILRg 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501562166 140 -MRAAlaralvtrpRVLLLDEPFAALDEITRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIV 215
Cdd:PRK15439 155 lMRDS---------RILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVM--RDGTIA 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-208 |
9.70e-16 |
|
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: 76.59 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHwsapPGPGDI-----------GFVFQEPTLMPW 89
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL----VGGKDIetnldavrqslGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITR 169
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190
....*....|....*....|....*....|....*....
gi 501562166 170 FRLNDELLALwqETGVTALFVTHSVFEGVYLSTRIAVMS 208
Cdd:TIGR01257 1098 RSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-192 |
6.24e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH--------WSAPPGPGDIGFVFQEPTLMPWAT 91
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddveaLSARAASRRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 92 VADNVRLP----LDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDeI 167
Cdd:PRK09536 94 VRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-I 172
|
170 180
....*....|....*....|....*
gi 501562166 168 TRFRLNDELLALWQETGVTALFVTH 192
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-216 |
7.05e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLP--PTAGGVHWSAPP----GPGD-----IGFVFQEPTLMPW 89
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPlkasNIRDteragIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNVRL--PLDLAGVAKAEARERAAEQ--LARVGLVDVAAAFP-RELSGGMRMRAALARALVTRPRVLLLDEPFAAL 164
Cdd:TIGR02633 93 LSVAENIFLgnEITLPGGRMAYNAMYLRAKnlLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501562166 165 DEITRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:TIGR02633 173 TEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVI--RDGQHVA 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-192 |
1.09e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHwsaPPGPGDIGFVFQ----EPTLMpwATVADNVRLPl 100
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGKLRIGYVPQklylDTTLP--LTVNRFLRLR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 101 dlAGVAKAEARERaaeqLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALW 180
Cdd:PRK09544 94 --PGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170
....*....|..
gi 501562166 181 QETGVTALFVTH 192
Cdd:PRK09544 168 RELDCAVLMVSH 179
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-219 |
1.27e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 5 LRSEGLGLRYapggtaGTEALA-DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGPG 75
Cdd:PRK10253 8 LRGEQLTLGY------GKYTVAeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqHYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 76 DIGFVFQEPTLMPWATVADNV---RLPLD-LAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTR 151
Cdd:PRK10253 82 RIGLLAQNATTPGDITVQELVargRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 152 PRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMA 219
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIVAQGA 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-172 |
1.44e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 4 LLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP--------- 74
Cdd:PRK13638 1 MLATSDLWFRYQ-----DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllal 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 -GDIGFVFQEPTLMPWATVAD-NVRLPLDLAGVAKAEARERAAEQLArvgLVDvAAAFPRE----LSGGMRMRAALARAL 148
Cdd:PRK13638 76 rQQVATVFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALT---LVD-AQHFRHQpiqcLSHGQKKRVAIAGAL 151
|
170 180
....*....|....*....|....
gi 501562166 149 VTRPRVLLLDEPFAALDEITRFRL 172
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQM 175
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-217 |
3.73e-14 |
|
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: 69.57 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 14 YAPGGtagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsappgpgD---------------IG 78
Cdd:cd03253 10 YDPGR----PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-------DgqdirevtldslrraIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 FVFQEPTLMPwATVADNVRLpldlAGVAKAEARERAAEQLARVGlvDVAAAFPR-----------ELSGGMRMRAALARA 147
Cdd:cd03253 79 VVPQDTVLFN-DTIGYNIRY----GRPDATDEEVIEAAKAAQIH--DKIMRFPDgydtivgerglKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 148 LVTRPRVLLLDEPFAALDEITRFRLNDELLALwqETGVTALFVTHSVFEgVYLSTRIAVMSprPGRIVAE 217
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST-IVNADKIIVLK--DGRIVER 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-217 |
5.46e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSA------------PPGPGDIGFVFQEPTLMPWa 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyiRPVRKRIGMVFQFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 tvADNVR---------LPLDLAGVAKAEARERAAEQLARvglvDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:PRK13646 100 --EDTVEreiifgpknFKMNLDEVKNYAHRLLMDLGFSR----DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 162 AALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM--KEGSIVSQ 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-168 |
5.56e-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: 71.48 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgpGDIGFVFQEPTLMPwATVADNVrlpl 100
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS-----GRISFSPQTSWIMP-GTIKDNI---- 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 101 dLAGVAKAEARERAAEQLARvgLVDVAAAFPRE-----------LSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:TIGR01271 508 -IFGLSYDEYRYTSVIKACQ--LEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-168 |
5.71e-14 |
|
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: 69.89 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgpGDIGFVFQEPTLMPwATVADNVrlpl 100
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-----GRISFSSQFSWIMP-GTIKENI---- 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 101 dLAGVAKAEARERAAEQLARvgLVDVAAAFPRE-----------LSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:cd03291 119 -IFGVSYDEYRYKSVVKACQ--LEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-217 |
5.78e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.34 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH--------WsappgPGD-----IGFVFQEPTLM 87
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldvatT-----PSRelakrLAILRQENHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 88 PWATVADNV----------RL-PLDLAGVAKAeareraaeqLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLL 156
Cdd:COG4604 88 SRLTVRELVafgrfpyskgRLtAEDREIIDEA---------IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 157 LDEPFAALD-----EITRF--RLNDELlalwqetGVTALFVTHSV-FEGVYlSTRIAVMspRPGRIVAE 217
Cdd:COG4604 159 LDEPLNNLDmkhsvQMMKLlrRLADEL-------GKTVVIVLHDInFASCY-ADHIVAM--KDGRVVAQ 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-211 |
6.74e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.43 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGL--LPPTA---GGV--HWSAPPGP 74
Cdd:PRK14243 8 ETVLRTENLNVYYG-----SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVtfHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 G--------DIGFVFQEPTLMPwATVADNVRLPLDLAGVAKAEARERAAEqLARVGLVDVAAAFPRE----LSGGMRMRA 142
Cdd:PRK14243 83 DvdpvevrrRIGMVFQKPNPFP-KSIYDNIAYGARINGYKGDMDELVERS-LRQAALWDEVKDKLKQsglsLSGGQQQRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 143 ALARALVTRPRVLLLDEPFAALDEITRFRLnDELLALWQETgVTALFVTHSVFEGVYLSTRIAVMSPRP 211
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRI-EELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVEL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-193 |
1.07e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLP------PTAGGVHW--------SAPPGPGDIGFVFQEPTLMPWA 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 TVADNVRLPLDLAGVAKAEARERAAEQ-LARVGL----VDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEEcLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180
....*....|....*....|....*...
gi 501562166 166 EITRFRLNDELLALWQEtgVTALFVTHS 193
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHN 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-215 |
1.08e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 68.29 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPgPGD----IG 78
Cdd:cd03244 6 KNVSLRYRPNLPP---VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGsilidGVDISKIG-LHDlrsrIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 FVFQEPTLMPwATVADNVRlPLD------LAGVakaeareraaeqLARVGLVDVAAAFP-----------RELSGGMRMR 141
Cdd:cd03244 82 IIPQDPVLFS-GTIRSNLD-PFGeysdeeLWQA------------LERVGLKEFVESLPggldtvveeggENLSVGQRQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 142 AALARALVTRPRVLLLDEPFAALDEITrfrlnDELLalwQET------GVTALFVTHSVfEGVYLSTRIAVMSprPGRIV 215
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPET-----DALI---QKTireafkDCTVLTIAHRL-DTIIDSDRILVLD--KGRVV 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-215 |
1.16e-13 |
|
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: 70.13 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPggtAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPG 73
Cdd:TIGR02203 328 RGDVEFRNVTFRYPG---RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdlaDYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 74 PGDIGFVFQEPTLMPwATVADNVRLpldlaGVAKAEARERAAEQLARVGLVDVAAAFPR-----------ELSGGMRMRA 142
Cdd:TIGR02203 405 RRQVALVSQDVVLFN-DTIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 143 ALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHSvfegvyLST-----RIAVMSprPGRIV 215
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHR------LSTiekadRIVVMD--DGRIV 546
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-207 |
1.71e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.16 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPP----TAGGVHW------SAPPGP------GDIGFVFQEPT-- 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWngidllKLSPRErrkiigREIAMIFQEPSsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 86 LMPWATVADNVR--LPLDLAGVAKAEARERAAEQ----LARVGL---VDVAAAFPRELSGGMRMRAALARALVTRPRVLL 156
Cdd:COG4170 102 LDPSAKIGDQLIeaIPSWTFKGKWWQRFKWRKKRaielLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501562166 157 LDEPFAALDEITR---FRLndeLLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:COG4170 182 ADEPTNAMESTTQaqiFRL---LARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-192 |
2.52e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPGG------TAGTEALADVGLTVARGEFVSLLGSSGCGKST----LLRLIAgllppTAGGVHWSAP 71
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 72 PGPG-----------DIGFVFQEP--TLMPWATVADNVR--LPLDLAGVAKAEARERAAEQLARVGL-VDVAAAFPRELS 135
Cdd:PRK15134 348 PLHNlnrrqllpvrhRIQVVFQDPnsSLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFS 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501562166 136 GGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH 192
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-165 |
2.86e-13 |
|
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: 67.11 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP--------GDIGFVFQEPTLMPwATVA 93
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehkylhSKVSLVGQEPVLFA-RSLQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 94 DNVrlPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRE-------LSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:cd03248 106 DNI--AYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-189 |
3.00e-13 |
|
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: 66.52 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 13 RYAPGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTA---GGVHWS-------APPGPGDIGFVFQ 82
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNgipykefAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 83 EPTLMPWATVADNVRLPLDLAGvakaeareraaeqlarvglvdvaAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFA 162
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180
....*....|....*....|....*..
gi 501562166 163 ALDEITRFRLNDELLALWQETGVTALF 189
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-217 |
3.34e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 18 GTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIaGLLPPTAGGVHWSAPPGPGD---------------IGFVFQ 82
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNDKVSGYRYSGDVLLGGrsifnyrdvlefrrrVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 83 EPTLMPwATVADNVrlpldLAGVAKAEAR------ERAAEQLARVGLVDVA----AAFPRELSGGMRMRAALARALVTRP 152
Cdd:PRK14271 109 RPNPFP-MSIMDNV-----LAGVRAHKLVprkefrGVAQARLTEVGLWDAVkdrlSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501562166 153 RVLLLDEPFAALDEITRFRLNDELLALWQEtgVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFF--DGRLVEE 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-216 |
4.15e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLP--PTAGGVHWSAPP----GP 74
Cdd:PRK13549 2 MEYLLEMKNITKTFG-----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEElqasNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 75 GD-----IGFVFQEPTLMPWATVADNVRLPLDL--AGVAKAEARERAAEQ-LARVGLvDVAAAFP-RELSGGMRMRAALA 145
Cdd:PRK13549 77 RDteragIAIIHQELALVKELSVLENIFLGNEItpGGIMDYDAMYLRAQKlLAQLKL-DINPATPvGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501562166 146 RALVTRPRVLLLDEPFAALDEI-TRFRLNdeLLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVA 216
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESeTAVLLD--IIRDLKAHGIACIYISHKLNEVKAISDTICVI--RDGRHIG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-232 |
5.23e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH------------------WSAPPGPG----DIGF 79
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvielseQSAAQMRHvrgaDMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEP--TLMPWATV----ADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPR 153
Cdd:PRK10261 109 IFQEPmtSLNPVFTVgeqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 154 VLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVD--LPRPRRPYLR 231
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM--YQGEAVETGSVEqiFHAPQHPYTR 266
|
.
gi 501562166 232 T 232
Cdd:PRK10261 267 A 267
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-192 |
8.61e-13 |
|
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: 67.52 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGL--LPPTAGGV----------HWSAPP---------------- 72
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcGYVERPskvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 ------GPGD---------IGFVFQEP-TLMPWATVADNVRLPLDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSG 136
Cdd:TIGR03269 92 eevdfwNLSDklrrrirkrIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 137 GMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTH 192
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-215 |
1.28e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 67.07 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP--------GDIGFVFQEPTLMPwATV 92
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidrhtlrQFINYLPQEPYIFS-GSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVrlpldLAGVAKAEARERAAEQLARVGLVDVAAAFPR-----------ELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:TIGR01193 565 LENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 162 AALDEITRFRLNDELLALWQEtgvTALFVTH--SVFEgvyLSTRIAVMSprPGRIV 215
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHrlSVAK---QSDKIIVLD--HGKII 687
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-192 |
1.33e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.16 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRYAPGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPG 73
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQP---VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpiaDYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 74 PGDIGFVFQEPTLMPwATVADNVRLPLDLAGVAKAEAReraaeqLARVGLVDVAAAFP----------RELSGGMRMRAA 143
Cdd:PRK11160 413 RQAISVVSQRVHLFS-ATLRDNLLLAAPNASDEALIEV------LQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLG 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501562166 144 LARALVTRPRVLLLDEPFAALDEITRfrlnDELLALWQE--TGVTALFVTH 192
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETE----RQILELLAEhaQNKTVLMITH 532
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-217 |
1.50e-12 |
|
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: 64.47 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGL-------------------LPPT----AGgvhwsappgpgd 76
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkyevtegeilfkgeditdLPPEerarLG------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 IGFVFQEPTLMPWATVADNVRlpldlagvakaeareraaeqlarvglvDVAAAFprelSGGMRMRAALARALVTRPRVLL 156
Cdd:cd03217 79 IFLAFQYPPEIPGVKNADFLR---------------------------YVNEGF----SGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501562166 157 LDEPFAALDeITRFRLNDELLALWQETGVTALFVTH--SVFEGVyLSTRIAVMspRPGRIVAE 217
Cdd:cd03217 128 LDEPDSGLD-IDALRLVAEVINKLREEGKSVLIITHyqRLLDYI-KPDRVHVL--YDGRIVKS 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-192 |
1.53e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLP----PTAGGV--------HWSAppgpgDIGFVFQEPTLmP 88
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgsLKINGIelreldpeSWRK-----HLSWVGQNPQL-P 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 89 WATVADNVRL------------PLDLAGVAKAEARERAAEQLArVGlvDVAAAfpreLSGGMRMRAALARALVTRPRVLL 156
Cdd:PRK11174 436 HGTLRDNVLLgnpdasdeqlqqALENAWVSEFLPLLPQGLDTP-IG--DQAAG----LSVGQAQRLALARALLQPCQLLL 508
|
170 180 190
....*....|....*....|....*....|....*.
gi 501562166 157 LDEPFAALDEITRFRLNDELLALWQetGVTALFVTH 192
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTH 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-221 |
1.74e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYAPggtagTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV------------HW 68
Cdd:PRK09700 2 ATPYISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 69 SAPPGpgdIGFVFQEPTLMPWATVADNV---RLPL-DLAGVAK---AEARERAAEQLARVGLVDVAAAFPRELSGGMRMR 141
Cdd:PRK09700 77 AAQLG---IGIIYQELSVIDELTVLENLyigRHLTkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 142 AALARALVTRPRVLLLDEPFAAL--DEITR-FRLNDELlalwQETGVTALFVTHSVFEGVYLSTRIAVM---SPRPGRIV 215
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLtnKEVDYlFLIMNQL----RKEGTAIVYISHKLAEIRRICDRYTVMkdgSSVCSGMV 229
|
....*.
gi 501562166 216 AEMAVD 221
Cdd:PRK09700 230 SDVSND 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-212 |
1.75e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.12 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 31 TVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPpgpgDIGFVFQEPTLMPWATVADNVRLPLDLAGvakaeA 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD----TVSYKPQYIKADYEGTVRDLLSSITKDFY-----T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 111 RERAAEQLAR-VGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDE---------ITRFRLNDEllalw 180
Cdd:cd03237 92 HPYFKTEIAKpLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlmaskvIRRFAENNE----- 166
|
170 180 190
....*....|....*....|....*....|..
gi 501562166 181 qetgVTALFVTHSVFEGVYLSTRIAVMSPRPG 212
Cdd:cd03237 167 ----KTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-217 |
3.41e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGPGDIGFVFQEPTLMPWATVADNV 96
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpisMLSSRQLARRLALLPQHHLTPEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 97 ---RLP-LDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDeitrfrL 172
Cdd:PRK11231 98 aygRSPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD------I 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501562166 173 ND--ELLALWQE---TGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAE 217
Cdd:PRK11231 172 NHqvELMRLMRElntQGKTVVTVLHDLNQASRYCDHLVVLA--NGHVMAQ 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-220 |
4.30e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 1 MEPLLRSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP----GPGD 76
Cdd:PRK10762 1 MQALLQLKGIDKAFP-----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvtfnGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -----IGFVFQEPTLMPWATVADNVRLPLD----LAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARA 147
Cdd:PRK10762 76 sqeagIGIIHQELNLIPQLTIAENIFLGREfvnrFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 148 LVTRPRVLLLDEPFAALDEI---TRFRLNDELlalwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAV 220
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTeteSLFRVIREL----KSQGRGIVYISHRLKEIFEICDDVTVF--RDGQFIAEREV 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-165 |
5.09e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.51 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP--------GDIGFVFQEPTLMPwATVADNV 96
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhylhRQVALVGQEPVLFS-GSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 97 RLPLDLAgvakAEARERAAEQLArvGLVDVAAAFPR-----------ELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:TIGR00958 576 AYGLTDT----PDEEIMAAAKAA--NAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-188 |
8.30e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 35 GEFVSLLGSSGCGKSTLLRLIAGLLPPT--AGGVHWS----APPGPGDIGFVFQEPTLMPWATVADNV------RLPLDL 102
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANnrkpTKQILKRTGFVTQDDILYPHLTVRETLvfcsllRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 103 AGVAKAEARERAAEQL--ARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALW 180
Cdd:PLN03211 174 TKQEKILVAESVISELglTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170
....*....|
gi 501562166 181 Q--ETGVTAL 188
Cdd:PLN03211 254 QkgKTIVTSM 263
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-192 |
9.41e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.43 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTagtEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS----APPGPGD----IGF 79
Cdd:cd03369 10 ENLSVRYAPDLP---PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidiSTIPLEDlrssLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEPTLMpwatvADNVRLPLDLAGvakaeareraaeqlaRVGLVDVAAAFP-----RELSGGMRMRAALARALVTRPRV 154
Cdd:cd03369 87 IPQDPTLF-----SGTIRSNLDPFD---------------EYSDEEIYGALRvseggLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501562166 155 LLLDEPFAALDEITRfrlndellALWQET------GVTALFVTH 192
Cdd:cd03369 147 LVLDEATASIDYATD--------ALIQKTireeftNSTILTIAH 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-215 |
1.30e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.21 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG-----GVHWSAPPGPG---DIGFVFQEPTLMPwATVADN 95
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGrilidGTDIRTVTRASlrrNIAVVFQDAGLFN-RSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 96 VRL---PLDLAGVAKAEARERAAEQLAR--VGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF 170
Cdd:PRK13657 429 IRVgrpDATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501562166 171 RLNDELLALWQetGVTALFVTHSvfegvyLST-----RIAVMSprPGRIV 215
Cdd:PRK13657 509 KVKAALDELMK--GRTTFIIAHR------LSTvrnadRILVFD--NGRVV 548
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-204 |
1.45e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 35 GEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP-GD----IGFVFQEPTLMPWATVADNVRLpldLAGVAKAE 109
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrGDrsrfMAYLGHLPGLKADLSTLENLHF---LCGLHGRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 110 ARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDeITRFRLNDELLALWQETGVTALF 189
Cdd:PRK13543 114 AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMISAHLRGGGAALV 192
|
170
....*....|....*
gi 501562166 190 VTHSVFEGVYLSTRI 204
Cdd:PRK13543 193 TTHGAYAAPPVRTRM 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-226 |
1.55e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.62 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLL-----PPTAGGVHWSAPpgpgDI------------GFVFQEP 84
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQ----DIfkmdvielrrrvQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 85 TLMPWATVADNVRLPLDLAGVAKAEARERAAEQ--LARVGLVDVAA----AFPRELSGGMRMRAALARALVTRPRVLLLD 158
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSKKELQERVRwaLEKAQLWDEVKdrldAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 159 EPFAALDEITRFRLNDELLALWQEtgVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAVD--LPRPR 226
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLY--KGQIVEWGPTRevFTNPR 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-192 |
4.60e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW-------SAPPGPGD-------------------- 76
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknKKKTKEKEkvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 -----IGFVFQ--EPTLMPWATVADNVRLPLDLaGVAKAEARERAAEQLARVGL-VDVAAAFPRELSGGMRMRAALARAL 148
Cdd:PRK13651 102 eirrrVGVVFQfaEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501562166 149 VTRPRVLLLDEPFAALD-----EITrfrlndELLALWQETGVTALFVTH 192
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDpqgvkEIL------EIFDNLNKQGKTIILVTH 223
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-192 |
5.07e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 59.31 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 34 RGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVhwsappgpgdigfvfqeptlmpwatvadnVRLPLDlagvakaeareR 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------IYIDGE-----------D 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 114 AAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDE-----LLALWQETGVTAL 188
Cdd:smart00382 41 ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLTVI 120
|
....
gi 501562166 189 FVTH 192
Cdd:smart00382 121 LTTN 124
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-192 |
6.48e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPG--------DIGFVFQEPTLMPwATVADNV 96
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvlrqGVAMVQQDPVVLA-DTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 97 RLPLDLAgvakaeaRERAAEQLARVGLVDVAAAFP-----------RELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PRK10790 436 TLGRDIS-------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180
....*....|....*....|....*..
gi 501562166 166 EITRFRLNDELLALWQETgvTALFVTH 192
Cdd:PRK10790 509 SGTEQAIQQALAAVREHT--TLVVIAH 533
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-214 |
7.82e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIaGLLPPTAGGVHWSappgpGDIGF---------------------VFQE 83
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVE-----GRVEFfnqniyerrvnlnrlrrqvsmVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 84 PTLMPwATVADNV---------RLPLDLAGVAKAEARERAAEQLARVGLVDVAAafprELSGGMRMRAALARALVTRPRV 154
Cdd:PRK14258 97 PNLFP-MSVYDNVaygvkivgwRPKLEIDDIVESALKDADLWDEIKHKIHKSAL----DLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 155 LLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSPRPGRI 214
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-168 |
8.95e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 8.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGDIG-------FVFQEPTLMPWATVADNVR 97
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyqkqlcFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 98 LPLDLAGVAKAEARERAAEQLARvgLVDVAAAFpreLSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:PRK13540 97 YDIHFSPGAVGITELCRLFSLEH--LIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-221 |
9.92e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 2 EPLLRSEGLGLRyapgGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS----APPGPGD- 76
Cdd:COG3845 255 EVVLEVENLSVR----DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgediTGLSPREr 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 77 ----IGFVFQEPT---LMPWATVADNVRLpldlagvakaeaRERAAEQLARVGLV----------------DVAAAFP-- 131
Cdd:COG3845 331 rrlgVAYIPEDRLgrgLVPDMSVAENLIL------------GRYRRPPFSRGGFLdrkairafaeelieefDVRTPGPdt 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 132 --RELSGGMRMRAALARALVTRPRVLLLDEPFAALD----EITRFRLNDEllalwQETGVTALFVthS-----VFEgvyL 200
Cdd:COG3845 399 paRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLEL-----RDAGAAVLLI--SedldeILA---L 468
|
250 260
....*....|....*....|.
gi 501562166 201 STRIAVMSprPGRIVAEMAVD 221
Cdd:COG3845 469 SDRIAVMY--EGRIVGEVPAA 487
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
118-221 |
1.30e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 118 LARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQEtGVTALFVTHSVFEG 197
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEA 207
|
90 100
....*....|....*....|....
gi 501562166 198 VYLSTRIAVMSprPGRIVAEMAVD 221
Cdd:NF000106 208 EQLAHELTVID--RGRVIADGKVD 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-165 |
1.46e-10 |
|
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: 61.10 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGgvhwSAPPGPG-DIGFVFQEPTLMPWATVADNVrlpld 101
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----EARPQPGiKVGYLPQEPQLDPTKTVRENV----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 102 LAGVAKAEAReraaeqLARvgLVDVAAAFPRE------------------------------------------------ 133
Cdd:TIGR03719 90 EEGVAEIKDA------LDR--FNEISAKYAEPdadfdklaaeqaelqeiidaadawdldsqleiamdalrcppwdadvtk 161
|
170 180 190
....*....|....*....|....*....|..
gi 501562166 134 LSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-229 |
2.33e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPpTAGGVHWSAPPGPG-----------------DIGFVFQEP-- 84
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGqdlqrisekerrnlvgaEVAMIFQDPmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 85 TLMPWATVADNVRLPLDL-AGVAKAEARERAAEQLARVGLVDVAA---AFPRELSGGMRMRAALARALVTRPRVLLLDEP 160
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501562166 161 FAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE-MAVDLPR-PRRPY 229
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM--YAGQVVETgKAHDIFRaPRHPY 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-207 |
2.36e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.64 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV---HWSAPPG----------PGDIGFVFQEPTLMPW 89
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgDYAIPANlkkikevkrlRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 A-TVADNVRL-PLDLAG----VAKAEARERAAEQLARvglvDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAA 163
Cdd:PRK13645 105 QeTIEKDIAFgPVNLGEnkqeAYKKVPELLKLVQLPE----DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501562166 164 LDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-221 |
3.51e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGllpptaggVHwsaPPGP--GDIGF------------------- 79
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG--------VY---PHGSyeGEILFdgevcrfkdirdsealgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 -VFQEPTLMPWATVADNVRLPLDLA--GVAKAEARERAAEQL-ARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVL 155
Cdd:NF040905 82 iIHQELALIPYLSIAENIFLGNERAkrGVIDWNETNRRARELlAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 156 LLDEPFAALDEITRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAVD 221
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVL--RDGRTIETLDCR 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-217 |
3.94e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HW-SAPPGPGDIGFVFQEPTLMPWATVA 93
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkditDWqTAKIMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNvrlpLDLAGVAKAEareraaeQLARVGLVDVAAAFPR----------ELSGGMRMRAALARALVTRPRVLLLDEPFAA 163
Cdd:PRK11614 99 EN----LAMGGFFAER-------DQFQERIKWVYELFPRlherriqragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501562166 164 LDEITRFRLNDELLALWQEtGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAE 217
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVL--ENGHVVLE 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-194 |
6.91e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP-----GPGDIGFVFQEPTLmPWA---TV 92
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqalQKNLVAYVPQSEEV-DWSfpvLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 93 ADNVRLP----LDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:PRK15056 98 EDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....*.
gi 501562166 169 RFRLNDELLALWQEtGVTALFVTHSV 194
Cdd:PRK15056 178 EARIISLLRELRDE-GKTMLVSTHNL 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-192 |
7.23e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 31 TVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsappgpG---DIGFVFQ-EPTLMPWATVADNVrlpldlagva 106
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------GtklEVAYFDQhRAELDPEKTVMDNL---------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 107 kaeareRAAEQLARVGLVDVAA-------AFP--------RELSGGMRMRAALARaLVTRPRVLL-LDEPFAALDeITRF 170
Cdd:PRK11147 405 ------AEGKQEVMVNGRPRHVlgylqdfLFHpkramtpvKALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD-VETL 476
|
170 180
....*....|....*....|..
gi 501562166 171 RLNDELLALWQEtgvTALFVTH 192
Cdd:PRK11147 477 ELLEELLDSYQG---TVLLVSH 495
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-194 |
9.88e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVhWSAPpgpgDIGFVFQEPTLMPwATVADNVRL-----P 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAER----SIAYVPQQAWIMN-ATVRGNILFfdeedA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 100 LDLAGVAKAEARERAAEQLARvGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLaL 179
Cdd:PTZ00243 750 ARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF-L 827
|
170
....*....|....*
gi 501562166 180 WQETGVTALFVTHSV 194
Cdd:PTZ00243 828 GALAGKTRVLATHQV 842
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-210 |
2.10e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS--APPG--PGDIGFVFQEP-TLMPW----ATVADN-- 95
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGyyAQDHAYDFENDlTLFDWmsqwRQEGDDeq 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 96 -VRlpldlaGVakaeareraaeqLARVgLV--DVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRL 172
Cdd:PRK15064 417 aVR------GT------------LGRL-LFsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL 477
|
170 180 190
....*....|....*....|....*....|....*....
gi 501562166 173 NdelLALWQETGvTALFVTHSVfEGVY-LSTRIAVMSPR 210
Cdd:PRK15064 478 N---MALEKYEG-TLIFVSHDR-EFVSsLATRIIEITPD 511
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-227 |
5.21e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 23 EALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGD---------IGFVFQEPTLMPwATVA 93
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwwrskIGVVSQDPLLFS-NSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNVRLPL----DL----------------------------AGVAKAEARERAAEQL-------------------ARVG 122
Cdd:PTZ00265 478 NNIKYSLyslkDLealsnyynedgndsqenknkrnscrakcAGDLNDMSNTTDSNELiemrknyqtikdsevvdvsKKVL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 123 LVDVAAAFP-----------RELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVT 191
Cdd:PTZ00265 558 IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250 260 270
....*....|....*....|....*....|....*.
gi 501562166 192 HSVFEGVYLSTrIAVMSPRPGRIVAEMAVDLPRPRR 227
Cdd:PTZ00265 638 HRLSTIRYANT-IFVLSNRERGSTVDVDIIGEDPTK 672
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-168 |
6.39e-09 |
|
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: 56.46 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 8 EGLGLRYAPGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPpTAG-----GVHWSAPP---------- 72
Cdd:TIGR01271 1221 QGLTAKYTEAGRA---VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGeiqidGVSWNSVTlqtwrkafgv 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 73 GPGDIgFVFQ---EPTLMPWATVADNvrlplDLAGVAKaeareraaeqlaRVGLVDVAAAFPREL-----------SGGM 138
Cdd:TIGR01271 1297 IPQKV-FIFSgtfRKNLDPYEQWSDE-----EIWKVAE------------EVGLKSVIEQFPDKLdfvlvdggyvlSNGH 1358
|
170 180 190
....*....|....*....|....*....|
gi 501562166 139 RMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-165 |
6.49e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.63 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG---------GVHWSAPPGPGD---------------IGF 79
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyiGDKKNNHELITNpyskkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 80 VFQEPTLMPWA-TVADNVRL-PLDLaGVAKAEARERAAEQLARVGL----VDVAaafPRELSGGMRMRAALARALVTRPR 153
Cdd:PRK13631 121 VFQFPEYQLFKdTIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLddsyLERS---PFGLSGGQKRRVAIAGILAIQPE 196
|
170
....*....|..
gi 501562166 154 VLLLDEPFAALD 165
Cdd:PRK13631 197 ILIFDEPTAGLD 208
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-165 |
7.79e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALAD-VGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsapPGPGDIGFVFQEPTLMPWAT---VADNV 96
Cdd:PRK10636 12 GVRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---PGNWQLAWVNQETPALPQPAleyVIDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 97 RLPLDLAGVAKAEARERAAEQLARV-GLVDVAAAFP-----------------------RELSGGMRMRAALARALVTRP 152
Cdd:PRK10636 89 REYRQLEAQLHDANERNDGHAIATIhGKLDAIDAWTirsraasllhglgfsneqlerpvSDFSGGWRMRLNLAQALICRS 168
|
170
....*....|...
gi 501562166 153 RVLLLDEPFAALD 165
Cdd:PRK10636 169 DLLLLDEPTNHLD 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-219 |
8.57e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 26 ADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPP----GPGDI---GFVF-----QEPTLMPWATVA 93
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPidirSPRDAiraGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 DNV----RLPLDLAGVAKAEARERaaeQLARVGLVDVAAAFP------RELSGGMRMRAALARALVTRPRVLLLDEPFAA 163
Cdd:PRK11288 350 DNInisaRRHHLRAGCLINNRWEA---ENADRFIRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501562166 164 LDEITRFRLNDELLALwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMA 219
Cdd:PRK11288 427 IDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVM--REGRIAGELA 479
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-194 |
1.17e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV--------HWSAPPGPGDIGFVFQEPTLMPWAT 91
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWSSKAFARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 92 VADNV---RLPLDLA-GVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEI 167
Cdd:PRK10575 102 VRELVaigRYPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180
....*....|....*....|....*..
gi 501562166 168 TRFRLNDELLALWQETGVTALFVTHSV 194
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDI 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-215 |
1.20e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.05 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 35 GEFVSLLGSSGCGKSTLLRLIAGLLPPtagGVHwsappGPGDI----------------GFVFQEPTLMPWATVADN--- 95
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPK---GVK-----GSGSVllngmpidakemraisAYVQQDDLFIPTLTVREHlmf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 96 ---VRLPLDLAGVAKAEARERAaeqLARVGLVDVA------AAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDE 166
Cdd:TIGR00955 123 qahLRMPRRVTKKEKRERVDEV---LQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501562166 167 ITRFRLNDELLALWQEtGVTALFVTH----SVFEgvyLSTRIAVMSprPGRIV 215
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQK-GKTIICTIHqpssELFE---LFDKIILMA--EGRVA 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-212 |
1.58e-08 |
|
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: 52.96 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 32 VARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsappgpgDIGFVFQEPTLMpwatvadnvrlpldlagvakaear 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-------DGITPVYKPQYI------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 112 eraaeqlarvglvdvaaafprELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVT 191
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVE 129
|
170 180
....*....|....*....|.
gi 501562166 192 HSVFEGVYLSTRIAVMSPRPG 212
Cdd:cd03222 130 HDLAVLDYLSDRIHVFEGEPG 150
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-207 |
1.63e-08 |
|
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: 55.02 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 32 VARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGDIGFVFQEPTLMPWATVADNV-------RLPLDLAG 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLltgrehlYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 105 VAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQEtG 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-G 2120
|
170 180
....*....|....*....|...
gi 501562166 185 VTALFVTHSVFEGVYLSTRIAVM 207
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
133-165 |
1.64e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.64e-08
10 20 30
....*....|....*....|....*....|...
gi 501562166 133 ELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-165 |
1.82e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 40 LLGSSGCGKSTLLRLIAGLLPPTAGgvhwSAPPGPG-DIGFVFQEPTLMPWATVADNVRlpldlAGVAKAEAReraaeqL 118
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGiKVGYLPQEPQLDPEKTVRENVE-----EGVAEVKAA------L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 119 ARvgLVDVAAAFPRE------------------------------------------------LSGGMRMRAALARALVT 150
Cdd:PRK11819 103 DR--FNEIYAAYAEPdadfdalaaeqgelqeiidaadawdldsqleiamdalrcppwdakvtkLSGGERRRVALCRLLLE 180
|
170
....*....|....*
gi 501562166 151 RPRVLLLDEPFAALD 165
Cdd:PRK11819 181 KPDMLLLDEPTNHLD 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
134-256 |
2.25e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 134 LSGGMRMRAALARALVTRPRVLLLDEPFAALD-----EITrfrlndELLALWQETGVTALFVTHSVFEGVYLSTRIAVMs 208
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgakkEIY------QLINQFKAEGLSIILVSSEMPEVLGMSDRILVM- 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 501562166 209 pRPGRIVAEmavdlprprrpYLRTEAgfgvlcrEASALLAAAMGDSAG 256
Cdd:PRK10762 469 -HEGRISGE-----------FTREQA-------TQEKLMAAAVGKLNR 497
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-205 |
2.39e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgpGDIGFVFQEPTLMPWATVADNVRLPLDLA 103
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN-----GEVSVIAISAGLSGQLTGIENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 104 GVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLAlWQET 183
Cdd:PRK13546 114 GFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE-FKEQ 192
|
170 180
....*....|....*....|..
gi 501562166 184 GVTALFVTHSVFEGVYLSTRIA 205
Cdd:PRK13546 193 NKTIFFVSHNLGQVRQFCTKIA 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-192 |
2.61e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTaGGVHWSA----------PPG------PGDIGFVFQEP--T 85
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSAtfngreilnlPEKelnklrAEQISMIFQDPmtS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 86 LMPWATVADNVRLPLDL-AGVAKAEARERAAEQLARVGLVDV---AAAFPRELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:PRK09473 110 LNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEArkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190
....*....|....*....|....*....|.
gi 501562166 162 AALDEITRFRLNDELLALWQETGVTALFVTH 192
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-213 |
2.90e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 31 TVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAppgpgDIGFVFQEPTLMPWATVADNvrlpldLAGVAKAEA 110
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL-----KISYKPQYIKPDYDGTVEDL------LRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 111 RERAAEQLAR-VGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALF 189
Cdd:PRK13409 430 SSYYKSEIIKpLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALV 509
|
170 180
....*....|....*....|....
gi 501562166 190 VTHSVFEGVYLSTRIAVMSPRPGR 213
Cdd:PRK13409 510 VDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-225 |
3.12e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPptaGGVHWSAPPGPGDIGF------------------VFQEPTL 86
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDVTLngeplaaidaprlarlraVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 87 MPWATVADNV----RLP-LDLAGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALARAL---------VTRP 152
Cdd:PRK13547 94 PAFAFSAREIvllgRYPhARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501562166 153 RVLLLDEPFAALDEITRFRLNDELLALWQETGVTALFVTHSVFEGVYLSTRIAVMSprPGRIVAEMAV-DLPRP 225
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA--DGAIVAHGAPaDVLTP 245
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-168 |
3.93e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.93 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 10 LGLRYAPGGTAgteALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPpTAG-----GVHWSAPP------GPGDIG 78
Cdd:cd03289 8 LTAKYTEGGNA---VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGdiqidGVSWNSVPlqkwrkAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 79 ---FVFQEPtlmpwatvadnVRLPLDLAGVAKAEARERAAEQlarVGLVDVAAAFPREL-----------SGGMRMRAAL 144
Cdd:cd03289 84 qkvFIFSGT-----------FRKNLDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCL 149
|
170 180
....*....|....*....|....
gi 501562166 145 ARALVTRPRVLLLDEPFAALDEIT 168
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPIT 173
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-192 |
1.17e-07 |
|
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: 52.44 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 20 AGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLpPTAGGVhwSAPPGPGDIGFVFQEPtLMPWATVADNVRLP 99
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGR--LTKPAKGKLFYVPQRP-YMTLGTLRDQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 100 LDLAGVAKAEARERAAEQ----------LARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRvllldepFAALDEITR 169
Cdd:TIGR00954 539 DSSEDMKRRGLSDKDLEQildnvqlthiLEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQ-------FAILDECTS 611
|
170 180
....*....|....*....|....*.
gi 501562166 170 ---FRLNDELLALWQETGVTALFVTH 192
Cdd:TIGR00954 612 avsVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-193 |
2.23e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWS-------APPGPGDIGF---------VFQepTLMP 88
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKncninniAKPYCTYIGHnlglklemtVFE--NLKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 89 WATVADNVRLpLDLAgvakaeareraaeqLARVGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:PRK13541 94 WSEIYNSAET-LYAA--------------IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180
....*....|....*....|....*
gi 501562166 169 RFRLNDeLLALWQETGVTALFVTHS 193
Cdd:PRK13541 159 RDLLNN-LIVMKANSGGIVLLSSHL 182
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-165 |
2.46e-07 |
|
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: 49.55 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 35 GEFVSLLGSSGCGKSTLLRLIAGllPPTAGGV----HWSAPPGPGD----IGFVFQEPTLMPWATVADNVRLPLDLagva 106
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG--RKTAGVItgeiLINGRPLDKNfqrsTGYVEQQDVHSPNLTVREALRFSALL---- 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 107 kaeareraaeqlarvglvdvaaafpRELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:cd03232 107 -------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-215 |
4.41e-07 |
|
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: 50.59 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV---------------HwsappgpGDIGFVFQEPTLM-- 87
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaslR-------AAIGIVPQDTVLFnd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 88 ----------PWATVADnVRLPLDLAgvakaeareraaeQL------------ARVGlvdvaaafprE----LSGGMRMR 141
Cdd:COG5265 447 tiayniaygrPDASEEE-VEAAARAA-------------QIhdfieslpdgydTRVG----------ErglkLSGGEKQR 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 142 AALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQetGVTALFVTHSvfegvyLST-----RIAVMspRPGRIV 215
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHR------LSTivdadEILVL--EAGRIV 571
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
134-207 |
6.67e-07 |
|
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: 49.82 E-value: 6.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501562166 134 LSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQEtGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-178 |
1.13e-06 |
|
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: 49.16 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsappgpGD---IGFVFQ-----EPTLMPWATVADNVRL 98
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GEtvkLAYVDQsrdalDPNKTVWEEISGGLDI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 99 pLDLAGVAKAEARERA------AEQLARVGlvdvaaafprELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRL 172
Cdd:TIGR03719 414 -IKLGKREIPSRAYVGrfnfkgSDQQKKVG----------QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
....*.
gi 501562166 173 NDELLA 178
Cdd:TIGR03719 483 EEALLN 488
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-165 |
1.54e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGvhwsAPPGPGDIGFVFQeptlMPW---ATVADNVR--LP 99
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA----SVVIRGTVAYVPQ----VSWifnATVRDNILfgSP 704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 100 LDLAGVAKAEARERAAEQLARVGLVDVAAAFPR--ELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PLN03130 705 FDPERYERAIDVTALQHDLDLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
118-207 |
2.02e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 118 LARVGLVD---VAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITR---FRLndeLLALWQETGVTALFVT 191
Cdd:PRK15093 140 LHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQaqiFRL---LTRLNQNNNTTILLIS 216
|
90
....*....|....*.
gi 501562166 192 HSVFEGVYLSTRIAVM 207
Cdd:PRK15093 217 HDLQMLSQWADKINVL 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-165 |
2.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGgvhwSAPPGPGDIGFVFQeptlMPW---ATVADNVRLPLD 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET----SSVVIRGSVAYVPQ----VSWifnATVRENILFGSD 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501562166 102 LAGVAKAEARERAAEQ----------LARVGLVDVaaafprELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PLN03232 705 FESERYWRAIDVTALQhdldllpgrdLTEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-192 |
2.91e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 47.14 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPtAGGV--------HWSAP-------------PGPGDIGfVFQe 83
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEIllngrplsDWSAAelarhraylsqqqSPPFAMP-VFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 84 ptlmpwatvadnvRLPLDLAGVAKAEARERAAEQLA-RVGLVDvaaAFPR---ELSGGMRMRAALARALVT-------RP 152
Cdd:COG4138 89 -------------YLALHQPAGASSEAVEQLLAQLAeALGLED---KLSRpltQLSGGEWQRVRLAAVLLQvwptinpEG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501562166 153 RVLLLDEPFAALDeITRFRLNDELLALWQETGVTALFVTH 192
Cdd:COG4138 153 QLLLLDEPMNSLD-VAQQAALDRLLRELCQQGITVVMSSH 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
132-165 |
3.52e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 3.52e-06
10 20 30
....*....|....*....|....*....|....
gi 501562166 132 RELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-192 |
3.96e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHW-SAPPGPGD-------IGFVFQ-----EPTLMPWA 90
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQpedyrklFSAVFTdfhlfDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 91 TVADNvrlpldlagvakaearERAAEQLARVGLVD-VAAAFPR----ELSGGMRMRAALARALVTRPRVLLLDEpFAAlD 165
Cdd:PRK10522 418 KPANP----------------ALVEKWLERLKMAHkLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDE-WAA-D 479
|
170 180
....*....|....*....|....*....
gi 501562166 166 EITRFR--LNDELLALWQETGVTALFVTH 192
Cdd:PRK10522 480 QDPHFRreFYQVLLPLLQEMGKTIFAISH 508
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-213 |
4.15e-06 |
|
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: 47.47 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 31 TVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAppgpgDIGFVFQEPTLMPWATVADNVRlpldlAGVAKAEA 110
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDL-----KISYKPQYISPDYDGTVEEFLR-----SANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 111 RERAAEQLAR-VGLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQETGVTALF 189
Cdd:COG1245 432 SSYYKTEIIKpLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMV 511
|
170 180
....*....|....*....|....
gi 501562166 190 VTHSVFEGVYLSTRIAVMSPRPGR 213
Cdd:COG1245 512 VDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
134-217 |
4.79e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 134 LSGGMRMRAALARALVTRPRVLLLDEPFAALD-----EItrFRLNDELLalwqETGVTALFVTHSVFEGVYLSTRIAVMS 208
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakyEI--YKLINQLV----QQGVAIIVISSELPEVLGLSDRVLVMH 479
|
....*....
gi 501562166 209 prPGRIVAE 217
Cdd:PRK13549 480 --EGKLKGD 486
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-64 |
5.60e-06 |
|
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: 47.10 E-value: 5.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 501562166 11 GLRYAPGGTAGTEALAdVG---LTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAG 64
Cdd:COG4615 332 GVTYRYPGEDGDEGFT-LGpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESG 387
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
118-192 |
6.40e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 6.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 118 LARVGLVDVAAAFP-RELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRF---RLNDELLAlwqETGVTALFVTH 192
Cdd:PRK10938 385 LDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLIS---EGETQLLFVSH 460
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-192 |
8.16e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLpPTAGGVH--------WSAPPGPGDIGFVFQE---PTLMPwatva 93
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQfagqpleaWSAAELARHRAYLSQQqtpPFAMP----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 94 dnVRLPLDL---AGVAKAEARERAAEQLARVGLVDVAAAFPRELSGGMRMRAALA-------RALVTRPRVLLLDEPFAA 163
Cdd:PRK03695 86 --VFQYLTLhqpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*....
gi 501562166 164 LDeITRFRLNDELLALWQETGVTALFVTH 192
Cdd:PRK03695 164 LD-VAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-57 |
1.01e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 1.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 501562166 6 RSEGLGLRYApggtaGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAG 57
Cdd:NF033858 3 RLEGVSHRYG-----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
38-165 |
1.09e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 38 VSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGdigfVFQEPTLmpwatvaDNVRLP----LDLAGVAKAEARER 113
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA----VFSQHHV-------DGLDLSsnplLYMMRCFPGVPEQK 606
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 501562166 114 AAEQLARVGLVDVAAAFPR-ELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PLN03073 607 LRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-165 |
2.39e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.09 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGP--------GDIGFVFQEPTLMPwATVADN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqldswrSRLAVVSQTPFLFS-DTVANN 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 96 VRLPLDLAgvakAEARERAAEQLARV--GLVDVAAAFPRE-------LSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PRK10789 409 IALGRPDA----TQQEIEHVARLASVhdDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
130-165 |
2.89e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 2.89e-05
10 20 30
....*....|....*....|....*....|....*.
gi 501562166 130 FPRELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-165 |
3.33e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.90 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGL--LPPTAGGVHW------SAPP------GpgdIGFVFQEPTL 86
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLdgedilELSPderaraG---IFLAFQYPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 87 MPWATVADNVRLPLDlaGVAKAEARERAAEQLAR--VGLVDVAAAFP-REL----SGGMRMRAALARALVTRPRVLLLDE 159
Cdd:COG0396 89 IPGVSVSNFLRTALN--ARRGEELSAREFLKLLKekMKELGLDEDFLdRYVnegfSGGEKKRNEILQMLLLEPKLAILDE 166
|
....*.
gi 501562166 160 PFAALD 165
Cdd:COG0396 167 TDSGLD 172
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-165 |
3.62e-05 |
|
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: 44.94 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 25 LADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgpGDIGFVFQEPTLMPwATVADNVRL--PLDL 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK-----GSVAYVPQQAWIQN-DSLRENILFgkALNE 727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501562166 103 AGVAKAEARERAAEQLARVGLVDVAAAFPR--ELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:TIGR00957 728 KYYQQVLEACALLPDLEILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-66 |
3.89e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 3.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV 66
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-165 |
3.92e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgpgdiGFVFQEPTLMPW----ATVADNVR 97
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD--------GHDLRDYTLASLrnqvALVSQNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 98 LPLD-----LAGVAKAEARERAAEQLARV------------GLVDVAAAFPRELSGGMRMRAALARALVTRPRVLLLDEP 160
Cdd:PRK11176 428 LFNDtiannIAYARTEQYSREQIEEAARMayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
....*
gi 501562166 161 FAALD 165
Cdd:PRK11176 508 TSALD 512
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-190 |
8.96e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 30 LTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVH---------------------WS------APPGPGDIGFVFQ 82
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqfshitrlsfeqlqklvsdeWQrnntdmLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 83 EPTLMpwaTVADNVRLpldlagvakaeareraaEQLARvgLVDVAAAFPRE---LSGGMRMRAALARALVTRPRVLLLDE 159
Cdd:PRK10938 104 EIIQD---EVKDPARC-----------------EQLAQ--QFGITALLDRRfkyLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190
....*....|....*....|....*....|.
gi 501562166 160 PFAALDEITRFRLNDELLALWQEtGVTALFV 190
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-165 |
1.44e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 27 DVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWsappgpGD---IGFVFQE-PTLMPWATVADNVRLPLDl 102
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GEtvkLAYVDQSrDALDPNKTVWEEISGGLD- 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 103 agvakaeareraaeqLARVGLVDVA-----AAFP----------RELSGGMRMRAALARALVTRPRVLLLDEPFAALD 165
Cdd:PRK11819 415 ---------------IIKVGNREIPsrayvGRFNfkggdqqkkvGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-165 |
2.63e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 40 LLGSSGCGKSTLLRLIAGLLPPTAGGVHWSappgPGD-IG------FVFQEPTL-----------------------MPW 89
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD----PNErLGklrqdqFAFEEFTVldtvimghtelwevkqerdriyaLPE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 90 ATVADNVRLPlDLAGVAKAEARERAAeqlARVGLVDVAAAFP--------RELSGGMRMRAALARALVTRPRVLLLDEPF 161
Cdd:PRK15064 108 MSEEDGMKVA-DLEVKFAEMDGYTAE---ARAGELLLGVGIPeeqhyglmSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
....
gi 501562166 162 AALD 165
Cdd:PRK15064 184 NNLD 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
132-207 |
3.70e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.58 E-value: 3.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501562166 132 RELSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRfrlND--ELLALWQETGVTALFVTHSVFEGVYLSTRIAVM 207
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR---NDiyQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-177 |
3.77e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 3 PLLRSEGLGlryapGGTAGTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAggvhwsappgpGDIGfvfq 82
Cdd:PRK10636 311 PLLKMEKVS-----AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVS-----------GEIG---- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 83 eptlmpwatVADNVRL----------------PLD-LAGVAKAEARERAAEQLARVGLV-DVAAAFPRELSGGMRMRAAL 144
Cdd:PRK10636 371 ---------LAKGIKLgyfaqhqleflradesPLQhLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVL 441
|
170 180 190
....*....|....*....|....*....|...
gi 501562166 145 ARALVTRPRVLLLDEPFAALDEITRFRLNDELL 177
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-170 |
3.58e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.55 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 35 GEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGV----HWSAPPG-------PGDIGFVFQEPTLMPWATVADNVRLPLDLA 103
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFHIGVegviTYDGITPeeikkhyRGDVVYNAETDVHFPHLTVGETLDFAARCK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 104 GVAKAEARERAAEQLARVglVDVAAA---------------FPRELSGGMRMRAALARALVTRPRVLLLDEPFAALDEIT 168
Cdd:TIGR00956 167 TPQNRPDGVSREEYAKHI--ADVYMAtyglshtrntkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
..
gi 501562166 169 RF 170
Cdd:TIGR00956 245 AL 246
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-220 |
3.79e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.17 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 21 GTEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPG---------PGDIGFVFQEPTLMPWAT 91
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 92 VADNV---RLPLDLAGVAKAEARERAAEQLARVGlVDVAaafPRE----LSGGMRMRAALARALVTRPRVLLLDEPFAAL 164
Cdd:PRK10982 90 VMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELD-IDID---PRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501562166 165 DEIT---RFRLNDELlalwQETGVTALFVTHSVFEGVYLSTRIAVMspRPGRIVAEMAV 220
Cdd:PRK10982 166 TEKEvnhLFTIIRKL----KERGCGIVYISHKMEEIFQLCDEITIL--RDGQWIATQPL 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-57 |
4.36e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 37.70 E-value: 4.36e-03
10 20 30
....*....|....*....|....*....|....*.
gi 501562166 22 TEALADVGLTVARGEFVSLLGSSGCGKSTLLRLIAG 57
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-213 |
5.88e-03 |
|
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: 36.53 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 24 ALADVGLTVARGEFVSLLGSSGCGKSTLLRLIaglLPPTAGGVHWSAPPGPGDIGFVFqeptlmpwatvadnvrlpLDla 103
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPKFSRNKLIF------------------ID-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 104 gvakaeareraaeQLARvgLVDVAAAFPR------ELSGGMRMRAALARALVTRPR--VLLLDEPFAALDEITRFRLNDE 175
Cdd:cd03238 67 -------------QLQF--LIDVGLGYLTlgqklsTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 501562166 176 LLALWQEtGVTALFVTHSVfEGVYLSTRIAVMSPRPGR 213
Cdd:cd03238 132 IKGLIDL-GNTVILIEHNL-DVLSSADWIIDFGPGSGK 167
|
|
| DTMP_kinase |
TIGR00041 |
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ... |
34-78 |
6.65e-03 |
|
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 161676 Cd Length: 195 Bit Score: 36.57 E-value: 6.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 501562166 34 RGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPGPGDIG 78
Cdd:TIGR00041 2 RGMFIVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREPGGTPIG 46
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
34-159 |
7.38e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 36.33 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501562166 34 RGEFVSLLGSSGCGKSTLLRLIAGLLPPTAGGVHWSAPPgpgdigfvfQEPTLMPWATVADNVRLPLDLAGVAKAEARER 113
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCD---------ENLPYSPLLEALTREGLLRQLLDELESSLLEA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 501562166 114 AAEQLARVglvdVAAAFPRELSGGMRMRAALARALVT-----RPRVLLLDE 159
Cdd:pfam13191 94 WRAALLEA----LAPVPELPGDLAERLLDLLLRLLDLlargeRPLVLVLDD 140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-208 |
9.26e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.02 E-value: 9.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501562166 134 LSGGMRMRAALARALVTRPRVLLLDEPFAALDEITRFRLNDELLALWQEtGVTALFVTHSVFEGVYLSTRIAVMS 208
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMS 465
|
|
| |
