|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
41-298 |
1.13e-150 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 422.19 E-value: 1.13e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 41 APDRAKISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD 120
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 RGVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLL 200
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 201 MDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPGRVHRVVEVPLPRPRTEELRLSREF 280
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPEF 241
|
250
....*....|....*...
gi 1154143773 281 AEVRNEVWHAVYHQEPAT 298
Cdd:COG1116 242 AALRAEILDLLREEAERA 259
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
47-266 |
1.32e-130 |
|
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: 369.88 E-value: 1.32e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQ 126
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 127 QYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFG 206
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 207 ALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPGRVHRVVEVPL 266
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
44-297 |
2.17e-109 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 317.96 E-value: 2.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 44 RAKISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGV 123
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 VFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDE 203
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 204 PFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPGRVHRVVEVPLPR-----PRTEELRLSR 278
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRrflagEDARAIKSDP 240
|
250
....*....|....*....
gi 1154143773 279 EFAEVRNEVWHAVYHQEPA 297
Cdd:COG4525 241 AFIALREELLDIIFAQEEA 259
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
45-258 |
2.90e-85 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 259.65 E-value: 2.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR--- 121
Cdd:COG3842 4 PALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLM 201
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 202 DEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRI 214
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
46-287 |
6.02e-85 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 255.44 E-value: 6.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 46 KISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVF 125
Cdd:NF040729 1 KLKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 126 QQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:NF040729 81 QNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 206 GALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPGRVHRVVEVPLPRPRTeelRLSREFAEVRN 285
Cdd:NF040729 161 GAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRN---RESEKYLEYKD 237
|
..
gi 1154143773 286 EV 287
Cdd:NF040729 238 HL 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
66-287 |
3.39e-82 |
|
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: 247.76 E-value: 3.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQYALFPWLTVRGNVEFGLR 145
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 146 --LTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAT 223
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 224 WTRERRTVLFVTHDVDEAVYLAGRVVVMAARPG-RVHRVVEVPLPRPRT-EELRLSREFAEVRNEV 287
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDrLEVVEDPSYYDLRNEA 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
61-261 |
1.37e-81 |
|
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: 245.51 E-value: 1.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---GVVFQQYALFPWLTVR 137
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVFQDYALFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 GNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQ 217
Cdd:cd03259 91 ENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154143773 218 EQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRVHRV 261
Cdd:cd03259 171 EELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRIVQV 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
45-258 |
8.14e-79 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 243.06 E-value: 8.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP-DRGV 123
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPkDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 --VFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLM 201
Cdd:COG3839 78 amVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 202 DEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRI 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
47-263 |
2.79e-77 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 234.94 E-value: 2.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ----GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:COG1136 85 rrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 198 VLLMDEPFGALDaltRVRSQE--QLLATWTRER-RTVLFVTHDvDEAVYLAGRVVVMaaRPGRVHRVVE 263
Cdd:COG1136 165 LILADEPTGNLD---SKTGEEvlELLRELNRELgTTIVMVTHD-PELAARADRVIRL--RDGRIVSDER 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
61-258 |
1.08e-76 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 237.74 E-value: 1.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDG------VPVRgpgpDRGV--VFQQYALFP 132
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnLPPR----ERRVgfVFQHYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 WLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAlt 212
Cdd:COG1118 89 HMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154143773 213 RVRSQ--EQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG1118 167 KVRKElrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRI 212
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
61-258 |
3.53e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 232.30 E-value: 3.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---------GVVFQQYALF 131
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 PWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAL 211
Cdd:COG4175 118 PHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 212 TRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:COG4175 198 IRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRI 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
47-251 |
2.55e-73 |
|
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: 225.19 E-value: 2.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---GV 123
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 VFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDE 203
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154143773 204 PFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
65-258 |
1.41e-72 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 223.81 E-value: 1.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQYALFPWLTVRGNVEFGL 144
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 145 RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATW 224
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190
....*....|....*....|....*....|....
gi 1154143773 225 TRERRTVLFVTHDVDEAVYLAGRVVVMAARPGRV 258
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRV 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
47-251 |
1.85e-70 |
|
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: 217.36 E-value: 1.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ----GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 198 VLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYlAGRVVVM 251
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIEL 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
47-258 |
2.22e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 217.65 E-value: 2.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:COG1125 2 IEFENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGL--GDFADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:COG1125 79 GYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 200 LMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:COG1125 159 LMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
59-258 |
1.39e-68 |
|
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: 214.43 E-value: 1.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 59 KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---------GVVFQQYA 129
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 130 LFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154143773 210 ALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRL 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
47-251 |
5.68e-67 |
|
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: 209.08 E-value: 5.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRhhpVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03295 1 IEFENVTK---RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGD--FADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 200 LMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
47-261 |
2.91e-66 |
|
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: 207.19 E-value: 2.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP-DRGV-- 123
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqERNVgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 VFQQYALFPWLTVRGNVEFGLRL----TRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 200 LMDEPFGALDAltRVRSQeqlLATWTRERR-----TVLFVTHDVDEAVYLAGRVVVMaaRPGRVHRV 261
Cdd:cd03296 159 LLDEPFGALDA--KVRKE---LRRWLRRLHdelhvTTVFVTHDQEEALEVADRVVVM--NKGRIEQV 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
61-261 |
1.12e-63 |
|
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: 199.79 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP-DRGV--VFQQYALFPWLTVR 137
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRDIamVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 GNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQ 217
Cdd:cd03301 91 DNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154143773 218 EQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRVHRV 261
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND--GQIQQI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
42-258 |
1.30e-63 |
|
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: 200.59 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 42 PDRAKISFREVSrhhpvKG-GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD 120
Cdd:COG1127 1 MSEPMIEVRNLT-----KSfGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 R--------GVVFQQYALFPWLTVRGNVEFGLR-LTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARA 191
Cdd:COG1127 76 ElyelrrriGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 192 YAVDPAVLLMDEPFGALDALTrVRSQEQLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPIT-SAVIDELIRELRDELGlTSVVVTHDLDSAFAIADRVAVLAD--GKI 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
47-258 |
3.52e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.13 E-value: 3.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD-R---G 122
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 VVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMD 202
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 203 EPFGALDALTR--VRsqeQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG1131 157 EPTSGLDPEARreLW---ELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
47-258 |
1.08e-62 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 197.94 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQ----QyaLF-PwlTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDP 196
Cdd:COG1122 78 GLVFQnpddQ--LFaP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 197 AVLLMDEPFGALDALTRvRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG1122 154 EVLVLDEPTAGLDPRGR-RELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD--GRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
33-258 |
1.74e-61 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 203.21 E-value: 1.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 33 GAPLTRTPAPDRAKISFREVSRHHPVKG-GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDG 111
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 112 VPVRGPGPDR--------GVVFQ--QYALFPWLTVRGNVEFGLRL-TRLPAAERRRRADHAIGLVGLG-DFADALPRTLS 179
Cdd:COG1123 327 KDLTKLSRRSlrelrrrvQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPpDLADRYPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 180 GGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVRSQEQ---LLATWTRER-RTVLFVTHDVDEAVYLAGRVVVMAArp 255
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQilnLLRDLQRELgLTYLFISHDLAVVRYIADRVAVMYD-- 480
|
...
gi 1154143773 256 GRV 258
Cdd:COG1123 481 GRI 483
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
48-251 |
5.03e-61 |
|
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: 192.68 E-value: 5.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 48 SFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-----G 122
Cdd:cd03225 1 ELKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 VVFQ----QyaLFPwLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:cd03225 79 LVFQnpddQ--FFG-PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 199 LLMDEPFGALDALTRVRSQEqLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLE-LLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
59-253 |
3.50e-60 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 195.84 E-value: 3.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 59 KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---------GVVFQQYA 129
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrkkiGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 130 LFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:TIGR01186 82 LFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154143773 210 ALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAA 253
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKA 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
47-253 |
3.64e-60 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 189.71 E-value: 3.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKggafTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 --GVVFQQYALFPWLTVRGNVEFGlrltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVL 199
Cdd:cd03229 77 riGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 200 LMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAA 253
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
47-258 |
6.18e-60 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 195.55 E-value: 6.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG-PGPDRGV-- 123
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENRHVnt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 VFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDE 203
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 204 PFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
61-299 |
1.28e-59 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 191.04 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQYALFPWLTVRGNV 140
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGLRltrlpaAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQL 220
Cdd:PRK11247 103 GLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 221 LATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRVHRVVEVPLPRPRTeelRLSREFAEVRNEVWHAVYHQEPATP 299
Cdd:PRK11247 177 ESLWQQHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDLPRPRR---RGSARLAELEAEVLQRVMSRGESEP 250
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
47-258 |
1.92e-58 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 186.94 E-value: 1.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSrhhpVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03261 1 IELRGLT----KSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQQYALFPWLTVRGNVEFGLR-LTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:cd03261 77 rrmGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 198 VLLMDEPFGALD--ALTRVrsqEQLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAarPGRV 258
Cdd:cd03261 157 LLLYDEPTAGLDpiASGVI---DDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLY--DGKI 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
47-263 |
5.86e-58 |
|
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: 185.86 E-value: 5.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 199 LLMDEPFGALDALTrVRSQEQLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAARpgrvhRVVE 263
Cdd:cd03258 162 LLCDEATSALDPET-TQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKG-----EVVE 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
47-280 |
3.58e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 187.21 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 199 LLMDEPFGALDALTrVRSQEQLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAArpGRV---HRVVEVpLPRPRTEel 274
Cdd:COG1135 162 LLCDEATSALDPET-TRSILDLLKDINRELGlTIVLITHEMDVVRRICDRVAVLEN--GRIveqGPVLDV-FANPQSE-- 235
|
....*.
gi 1154143773 275 rLSREF 280
Cdd:COG1135 236 -LTRRF 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
47-263 |
6.89e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 182.56 E-value: 6.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:COG2884 79 rriGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 199 LLMDEPFGALDALTrvrSQE--QLLATWTRERRTVLFVTHD---VDEavyLAGRVVVMAArpGRVHRVVE 263
Cdd:COG2884 159 LLADEPTGNLDPET---SWEimELLEEINRRGTTVLIATHDlelVDR---MPKRVLELED--GRLVRDEA 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
66-258 |
1.30e-56 |
|
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: 181.72 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIA---EGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVP-------VRGPGPDR--GVVFQQYALFPW 133
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkINLPPQQRkiGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 134 LTVRGNVEFGLRltRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTR 213
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154143773 214 VRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRL 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
45-251 |
4.67e-56 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 184.66 E-value: 4.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP-DRGV 123
Cdd:PRK11650 2 AGLKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 --VFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLM 201
Cdd:PRK11650 79 amVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154143773 202 DEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
68-259 |
5.53e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 180.72 E-value: 5.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 68 RLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP-DRGV--VFQQYALFPWLTVRGNVEFGL 144
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaERPVsmLFQENNLFPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 145 RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvrsQE--QLLA 222
Cdd:COG3840 97 RPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR---QEmlDLVD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 223 TWTRERR-TVLFVTHDVDEAVYLAGRVVVMAArpGRVH 259
Cdd:COG3840 174 ELCRERGlTVLMVTHDPEDAARIADRVLLVAD--GRIA 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
61-278 |
7.63e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 180.58 E-value: 7.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-------GVVFQQYALFPW 133
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvGMVFQQFNLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 134 LTVRGNVEFGLRLTR-LPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD--- 209
Cdd:COG1126 92 LTVLENVTLAPIKVKkMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpel 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 210 ---ALTRVRSqeqlLAtwtRERRTVLFVTHDVDEAVYLAGRVVVMAArpGrvhRVVEVPLPR-----PRTEELR--LSR 278
Cdd:COG1126 172 vgeVLDVMRD----LA---KEGMTMVVVTHEMGFAREVADRVVFMDG--G---RIVEEGPPEeffenPQHERTRafLSK 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
66-273 |
3.69e-55 |
|
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: 178.68 E-value: 3.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---GVVFQQYALFPWLTVRGNVEF 142
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 143 GLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEqLLA 222
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE-ELK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 223 TWTRERR-TVLFVTHDVDEAVYLAGRVVVMaaRPGRVHRV--VEVPLPRPRTEE 273
Cdd:cd03299 174 KIRKEFGvTVLHVTHDFEEAWALADKVAIM--LNGKLIQVgkPEEVFKKPKNEF 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
47-263 |
5.46e-55 |
|
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: 178.08 E-value: 5.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQQY--ALFPWLTVRGNVEFGLRL-TRLPAAERRRRADHAIgLVGLG---DFADALPRTLSGGMKQRCALARAY 192
Cdd:cd03257 82 keiQMVFQDPmsSLNPRMTIGEQIAEPLRIhGKLSKKEARKEAVLLL-LVGVGlpeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 193 AVDPAVLLMDEPFGALDALTrvrsQEQLLATWTRERR----TVLFVTHDVDEAVYLAGRVVVMAArpGrvhRVVE 263
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSV----QAQILDLLKKLQEelglTLLFITHDLGVVAKIADRVAVMYA--G---KIVE 226
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
66-273 |
1.65e-53 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 177.96 E-value: 1.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD-RGV--VFQQYALFPWLTVRGNVEF 142
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEkRGIayVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 143 GLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQlLA 222
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIRE-MK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 223 TWTRERR-TVLFVTHDVDEAVYLAGRVVVM-AARPGRVHRVVEVpLPRPRTEE 273
Cdd:NF040840 175 RWHREFGfTAIHVTHNFEEALSLADRVGIMlNGRLSQVGDVREV-FRRPKNEF 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
61-258 |
6.62e-53 |
|
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: 176.44 E-value: 6.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTaLDrLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDG-----------VPVRgpgpDR--GVVFQQ 127
Cdd:COG4148 12 GGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargifLPPH----RRriGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 128 YALFPWLTVRGNVEFGLRltRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGA 207
Cdd:COG4148 86 ARLFPHLSVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 208 LDaltRVRSQEQL--LATWTRERRT-VLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG4148 164 LD---LARKAEILpyLERLRDELDIpILYVSHSLDEVARLADHVVLLEQ--GRV 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
47-252 |
8.39e-53 |
|
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: 171.94 E-value: 8.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD----R- 121
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 --GVVFQQYALFPWLTVRGNVEFGLRLTR-LPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:cd03262 77 kvGMVFQQFNLFPHLTVLENITLAPIKVKgMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 199 LLMDEPFGALDALTrVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:cd03262 157 MLFDEPTSALDPEL-VGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
65-251 |
7.89e-52 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 174.64 E-value: 7.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---GVVFQQYALFPWLTVRGNVE 141
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpiNMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 142 FGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLL 221
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190
....*....|....*....|....*....|
gi 1154143773 222 ATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
66-251 |
8.07e-52 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 173.73 E-value: 8.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-RGPGPDR--GVVFQQYALFPWLTVRGNVEF 142
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsRLHARDRkvGFVFQHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 143 GL----RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAltRVRSQe 218
Cdd:PRK10851 98 GLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA--QVRKE- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 219 qlLATWTRE-----RRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK10851 175 --LRRWLRQlheelKFTSVFVTHDQEEAMEVADRVVVM 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
47-253 |
1.50e-51 |
|
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: 169.98 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQY--ALFPWLTVRGNVEFGLRLTRLPaaERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 199 LLMDEPFGALDALTrvrsQEQLLATWTRERR----TVLFVTHDVDEAVYLAGRVVVMAA 253
Cdd:COG1124 160 LLLDEPTSALDVSV----QAEILNLLKDLREerglTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
81-261 |
1.61e-51 |
|
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: 172.29 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 81 VVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRR 157
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 158 ADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHD 237
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 1154143773 238 VDEAVYLAGRVVVMaaRPGRVHRV 261
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
64-252 |
6.42e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.96 E-value: 6.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQYAL---FPwLTVRGNV 140
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdwdFP-ITVRDVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGL----RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAltrvRS 216
Cdd:COG1121 99 LMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA----AT 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154143773 217 QE---QLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:COG1121 175 EEalyELLRELRREGKTILVVTHDLGAVREYFDRVLLLN 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
61-258 |
9.74e-51 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 167.73 E-value: 9.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----GVVFQQYALFPWLTV 136
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqiGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVRS 216
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD----VMA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154143773 217 QEQL---LATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG4555 168 RRLLreiLRALKKEGKTVLFSSHIMQEVEALCDRVVILHK--GKV 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
45-261 |
9.87e-51 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 171.37 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHpvkGGAFTALDrLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG-PGPDRGV 123
Cdd:PRK11000 2 ASVTLRNVTKAY---GDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 --VFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLM 201
Cdd:PRK11000 78 gmVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 202 DEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRVHRV 261
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQV 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
61-251 |
1.07e-50 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 170.67 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-------RgpgpDRGVVFQQYALFPW 133
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrsiqqR----DICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 134 LTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTR 213
Cdd:PRK11432 93 MSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 214 VRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11432 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
47-259 |
9.36e-49 |
|
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: 162.22 E-value: 9.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ----GVVFQQYALFPWLTVRGNVefGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:COG4181 89 arhvGFVFQSFQLLPTLTALENV--MLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 198 VLLMDEPFGALDALTRVRSQEqLLATWTRERRTVLF-VTHDVDeavyLA---GRVVVMAArpGRVH 259
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIID-LLFELNRERGTTLVlVTHDPA----LAarcDRVLRLRA--GRLV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
47-258 |
1.58e-48 |
|
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: 168.93 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSG---GEVLVDGVPVRGP-----G 118
Cdd:COG1123 5 LEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELsealrG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 119 PDRGVVFQ--QYALFPwLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDP 196
Cdd:COG1123 83 RRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 197 AVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRI 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
61-259 |
2.60e-48 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 161.75 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG-PGPDR----GVVFQQYALFPWLT 135
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELarriAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFG----LRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDal 211
Cdd:COG1120 92 VRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD-- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 212 trVRSQEQ---LLATWTRER-RTVLFVTHDVDEAVYLAGRVVVMaaRPGRVH 259
Cdd:COG1120 170 --LAHQLEvleLLRRLARERgRTVVMVLHDLNLAARYADRLVLL--KDGRIV 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
61-249 |
3.64e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 160.01 E-value: 3.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQYAL---FPwLTVR 137
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFP-ISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 GNVEFGL----RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltr 213
Cdd:cd03235 89 DVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD---- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154143773 214 VRSQEQ---LLATWTRERRTVLFVTHD-------VDEAVYLAGRVV 249
Cdd:cd03235 165 PKTQEDiyeLLRELRREGMTILVVTHDlglvleyFDRVLLLNRTVV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
66-205 |
1.27e-47 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 156.27 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-----GVVFQQYALFPWLTVRGNV 140
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 141 EFGLRLTRLPAAERRRRADHAIGLVGLGDFAD----ALPRTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
47-258 |
2.63e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 158.11 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL-----DAPSGGEVLVDGVPVRGPGPDR 121
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -------GVVFQQYALFPwLTVRGNVEFGLRLTR-LPAAERRRRADHAIGLVGLGD-FADAL-PRTLSGGMKQRCALARA 191
Cdd:cd03260 77 lelrrrvGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDeVKDRLhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 192 YAVDPAVLLMDEPFGALDALTRvRSQEQLLATwTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPIST-AKIEELIAE-LKKEYTIVIVTHNMQQAARVADRTAFLLN--GRL 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
61-258 |
3.14e-47 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 156.02 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----GVVFQQYALFPWLTV 136
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEfglrltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvRS 216
Cdd:cd03230 91 RENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR-RE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154143773 217 QEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03230 134 FWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
47-258 |
3.26e-47 |
|
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: 157.67 E-value: 3.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRgpgPDR----- 121
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---TDRkaarq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 --GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:cd03263 76 slGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 200 LMDEPFGALDALTRvRSQEQLLAtWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03263 156 LLDEPTSGLDPASR-RAIWDLIL-EVRKGRSIILTTHSMDEAEALCDRIAIMSD--GKL 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
68-258 |
5.20e-47 |
|
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: 156.88 E-value: 5.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 68 RLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP-DRGV--VFQQYALFPWLTVRGNVEFG- 143
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPaDRPVsmLFQENNLFAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 144 ---LRLTrlpaAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQeQL 220
Cdd:cd03298 96 spgLKLT----AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-DL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154143773 221 LATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03298 171 VLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDN--GRI 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
47-280 |
7.99e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.35 E-value: 7.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:PRK11153 82 rqiGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 199 LLMDEPFGALDALTrVRSQEQLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAArpGRV---HRVVEVPLpRPRTEel 274
Cdd:PRK11153 162 LLCDEATSALDPAT-TRSILELLKDINRELGlTIVLITHEMDVVKRICDRVAVIDA--GRLveqGTVSEVFS-HPKHP-- 235
|
....*.
gi 1154143773 275 rLSREF 280
Cdd:PRK11153 236 -LTREF 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
47-251 |
1.75e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 156.41 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 --GVVFQQYALFPWLTVRGNVEFGLRLTR-LPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:PRK09493 78 eaGMVFQQFYLFPHLTALENVMFGPLRVRgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 199 LLMDEPFGALDALTR--VRSQEQLLATwtrERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK09493 158 MLFDEPTSALDPELRheVLKVMQDLAE---EGMTMVIVTHEIGFAEKVASRLIFI 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
61-258 |
8.18e-46 |
|
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: 154.52 E-value: 8.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----GVV--FQQYALFPWL 134
Cdd:cd03219 11 GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlGIGrtFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRL----------TRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEP 204
Cdd:cd03219 91 TVLENVMVAAQArtgsglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 205 FGALDALTRVRSQEqLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03219 171 AAGLNPEETEELAE-LIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ--GRV 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
30-258 |
8.30e-46 |
|
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: 164.24 E-value: 8.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 30 EETGAPLTRTPAPDRAKISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLV 109
Cdd:COG2274 457 EREEGRSKLSLPRLKGDIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 110 DGVPVRGPGPD--R---GVVFQQYALFPwLTVRGNvefgLRLTRLPAAErrRRADHAIGLVGLGDFADALP--------- 175
Cdd:COG2274 535 DGIDLRQIDPAslRrqiGVVLQDVFLFS-GTIREN----ITLGDPDATD--EEIIEAARLAGLHDFIEALPmgydtvvge 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 176 --RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQlLATWTRErRTVLFVTHDvDEAVYLAGRVVVMAA 253
Cdd:COG2274 608 ggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKG-RTVIIIAHR-LSTIRLADRIIVLDK 684
|
....*
gi 1154143773 254 rpGRV 258
Cdd:COG2274 685 --GRI 687
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
66-254 |
2.59e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 152.64 E-value: 2.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAG-LDAP--SGGEVLVDGVPV-RGPGPDR--GVVFQQYALFPWLTVRGN 139
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLtALPAEQRriGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 VEFGLRlTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQ 219
Cdd:COG4136 97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1154143773 220 LLATWTRERRTVLFVTHDVDEAVyLAGRVVVMAAR 254
Cdd:COG4136 176 VFEQIRQRGIPALLVTHDEEDAP-AAGRVLDLGNW 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
66-254 |
1.32e-44 |
|
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: 150.71 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----GVVFQQYALFPWLTVRGNVE 141
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAYLGHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 142 FGLRLTRLPAAerRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSqEQLL 221
Cdd:COG4133 98 FWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL-AELI 174
|
170 180 190
....*....|....*....|....*....|...
gi 1154143773 222 ATWTRERRTVLFVTHDVDEavYLAGRVVVMAAR 254
Cdd:COG4133 175 AAHLARGGAVLLTTHQPLE--LAAARVLDLGDF 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
61-258 |
2.42e-44 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 151.34 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----GVV--FQQYALFPWL 134
Cdd:COG0411 15 GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarlGIArtFQNPRLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFG-------------LRLTRLPAAER--RRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:COG0411 95 TVLENVLVAaharlgrgllaalLRLPRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 200 LMDEPFGAL-----DALTRvrsqeqLLATWTRER-RTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG0411 175 LLDEPAAGLnpeetEELAE------LIRRLRDERgITILLIEHDMDLVMGLADRIVVLDF--GRV 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
47-251 |
4.64e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.04 E-value: 4.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPgpDR----- 121
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE--ENlweir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQ----QyalFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAV 194
Cdd:TIGR04520 77 kkvGMVFQnpdnQ---FVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 195 DPAVLLMDEPFGALDALTRvrsqEQLLATWTRERR----TVLFVTHDVDEAVyLAGRVVVM 251
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGR----KEVLETIRKLNKeegiTVISITHDMEEAV-LADRVIVM 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
68-259 |
5.96e-44 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 149.73 E-value: 5.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 68 RLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVV---FQQYALFPWLTVRGNVEFGL 144
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVsmlFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 145 RLT-RLPAAERRRRADHAiGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvrsQE--QLL 221
Cdd:PRK10771 97 NPGlKLNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR---QEmlTLV 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154143773 222 ATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAArpGRVH 259
Cdd:PRK10771 173 SQVCQERQlTLLMVSHSLEDAARIAPRSLVVAD--GRIA 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
59-251 |
1.04e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 153.65 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 59 KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---------GVVFQQYA 129
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 130 LFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154143773 210 ALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
66-253 |
2.67e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 147.27 E-value: 2.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG-PGPD--RGV--VFQQYALFPwLTVRGNV 140
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwrRQVayVPQEPALWG-GTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGLRLTRLPAaeRRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvRSQEQ 219
Cdd:COG4619 95 PFPFQLRERKF--DRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT-RRVEE 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1154143773 220 LLATW-TRERRTVLFVTHDVDEAVYLAGRVVVMAA 253
Cdd:COG4619 172 LLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
47-251 |
4.05e-43 |
|
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: 145.60 E-value: 4.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03228 1 IEFKNVSFSYP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPwLTVRGNVefglrltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVLLM 201
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154143773 202 DEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTHDVdEAVYLAGRVVVM 251
Cdd:cd03228 121 DEATSALDPETEALILEALRA--LAKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
29-258 |
7.99e-43 |
|
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: 154.54 E-value: 7.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 29 REETGAPLTRTPAPDRAKISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVL 108
Cdd:COG4987 316 PPAVTEPAEPAPAPGGPSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 109 VDGVPVRGPGPDR-----GVVFQQYALFPwLTVRGNvefgLRLTRLPAAERRRRAdhAIGLVGLGDFADALP-------- 175
Cdd:COG4987 394 LGGVDLRDLDEDDlrrriAVVPQRPHLFD-TTLREN----LRLARPDATDEELWA--ALERVGLGDWLAALPdgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 176 ---RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrvrSQE--QLLATWTRErRTVLFVTHDvDEAVYLAGRVVV 250
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAAT---EQAllADLLEALAG-RTVLLITHR-LAGLERMDRILV 541
|
....*...
gi 1154143773 251 MAArpGRV 258
Cdd:COG4987 542 LED--GRI 547
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
47-258 |
3.16e-42 |
|
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: 144.86 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPgPDR----- 121
Cdd:cd03292 1 IEFINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGRaipyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ----GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:cd03292 77 rrkiGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 198 VLLMDEPFGALDALTRVRSQEqLLATWTRERRTVLFVTHDVDeaVYLAGRVVVMAARPGRV 258
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKE--LVDTTRHRVIALERGKL 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
48-251 |
6.97e-42 |
|
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: 142.00 E-value: 6.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 48 SFREVSRHHPVKggafTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVrgpgpdrgvvfqq 127
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 128 yalfpwltvrgnvefglrlTRLPAAERRRRadhaIGLVGlgdfadalprTLSGGMKQRCALARAYAVDPAVLLMDEPFGA 207
Cdd:cd00267 64 -------------------AKLPLEELRRR----IGYVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154143773 208 LDALTRvRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd00267 111 LDPASR-ERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
47-258 |
7.99e-42 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 144.63 E-value: 7.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVFQQYALFPWLTVRGNVEFGlRLTRLPA---------AERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALA 189
Cdd:cd03256 78 rqiGMIFQQFNLIERLSVLENVLSG-RLGRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 190 RAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRI 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-263 |
1.19e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 151.06 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 26 EKSREETGAPLTRTPAPDRAKISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGG 105
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 106 EVLVDGVPVRGPGPDR-----GVVFQQYALFPWlTVRGNvefgLRLTRLPAAERRRRAdhAIGLVGLGDFADALP----- 175
Cdd:COG4988 393 SILINGVDLSDLDPASwrrqiAWVPQNPYLFAG-TIREN----LRLGRPDASDEELEA--ALEAAGLDEFVAALPdgldt 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 176 ------RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAltrvRSQEQLLATWTR--ERRTVLFVTHDvDEAVYLAGR 247
Cdd:COG4988 466 plgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDA----ETEAEILQALRRlaKGRTVILITHR-LALLAQADR 540
|
250
....*....|....*.
gi 1154143773 248 VVVMAArpgrvHRVVE 263
Cdd:COG4988 541 ILVLDD-----GRIVE 551
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
47-264 |
1.26e-41 |
|
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: 146.35 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAP---SGGEVLVDGVPVRGPGPDR-- 121
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -------GVVFQ--QYALFPWLTVRGNVEFGLRL-TRLPAAERRRRADHAIGLVGLGD---FADALPRTLSGGMKQRCAL 188
Cdd:COG0444 82 kirgreiQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 189 ARAYAVDPAVLLMDEPFGALDaltrVRSQEQ---LLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMAArpGrvhRVVEV 264
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD----VTIQAQilnLLKDLQRELGlAILFITHDLGVVAEIADRVAVMYA--G---RIVEE 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
30-249 |
2.13e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.70 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 30 EETGAPLTRTPAPDRAKISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLV 109
Cdd:COG1132 323 EIPDPPGAVPLPPVRGEIEFENVSFSYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 110 DGVPVRGPGPDR-----GVVFQQYALFPwLTVRGNVEFGlrltRLPAAERRRRAdhAIGLVGLGDFADALP--------- 175
Cdd:COG1132 400 DGVDIRDLTLESlrrqiGVVPQDTFLFS-GTIRENIRYG----RPDATDEEVEE--AAKAAQAHEFIEALPdgydtvvge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 176 --RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTH------DVDEAVYL-AG 246
Cdd:COG1132 473 rgVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER--LMKGRTTIVIAHrlstirNADRILVLdDG 550
|
...
gi 1154143773 247 RVV 249
Cdd:COG1132 551 RIV 553
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
59-251 |
8.55e-41 |
|
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: 141.35 E-value: 8.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 59 KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-RGPGPDR---GVVFQQYALFPWL 134
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPREVRrriGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRV 214
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154143773 215 RSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd03265 169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
64-259 |
1.17e-39 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 136.80 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPvrgpgpdrgvvfqqyalfpwltvrgnvefg 143
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD------------------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 144 lrLTRLPAAERRRRADH---AIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVRSQE-- 218
Cdd:cd03214 63 --LASLSPKELARKIAYvpqALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD----IAHQIel 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154143773 219 -QLLATWTRER-RTVLFVTHDVDEAVYLAGRVVVMAArpGRVH 259
Cdd:cd03214 137 lELLRRLARERgKTVVMVLHDLNLAARYADRVILLKD--GRIV 177
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
64-258 |
4.89e-39 |
|
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: 140.25 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDrLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPG------PDR---GVVFQQYALFPWL 134
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKrriGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRLTRlpAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltRV 214
Cdd:TIGR02142 91 SVRGNLRYGMKRAR--PSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD---DP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 215 RSQEQL--LATWTRERRT-VLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:TIGR02142 166 RKYEILpyLERLHAEFGIpILYVSHSLQEVLRLADRVVVL--EDGRV 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
50-251 |
5.62e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.48 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 50 REVSRHHPVKGGAFT-------ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD-- 120
Cdd:COG4608 11 RDLKKHFPVRGGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 ----RGV--VFQQ-YA-LFPWLTVRGNVEFGLRL-TRLPAAERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALAR 190
Cdd:COG4608 91 rplrRRMqmVFQDpYAsLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIAR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 191 AYAVDPAVLLMDEPFGALDaltrVRSQEQ---LLATWTRERR-TVLFVTHDVdeAV--YLAGRVVVM 251
Cdd:COG4608 171 ALALNPKLIVCDEPVSALD----VSIQAQvlnLLEDLQDELGlTYLFISHDL--SVvrHISDRVAVM 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
61-251 |
8.91e-38 |
|
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: 135.60 E-value: 8.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-RGPGPDR---GVVFQQYALFPWLTV 136
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREPRKVRrsiGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvRS 216
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR-RA 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1154143773 217 QEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:TIGR01188 163 IWDYIRALKEEGVTILLTTHYMEEADKLCDRIAII 197
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
65-260 |
2.59e-37 |
|
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: 131.93 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFvAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-RGPGPDRGVVF---QQYALFPWLTVRGNV 140
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlKQPQKLRRRIGylpQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQL 220
Cdd:cd03264 94 DYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154143773 221 --LAtwtrERRTVLFVTHDVDEAVYLAGRVVVMAArpGRVHR 260
Cdd:cd03264 174 seLG----EDRIVILSTHIVEDVESLCNQVAVLNK--GKLVF 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
64-259 |
4.22e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.55 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD-----RGVVFQQYAL-FPWlTVR 137
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRAVLPQHSSLaFPF-TVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 GNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYA-------VDPAVLLMDEPFGALDa 210
Cdd:COG4559 94 EVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 211 ltrVRSQEQLLA---TWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRVH 259
Cdd:COG4559 173 ---LAHQHAVLRlarQLARRGGGVVAVLHDLNLAAQYADRILLLHQ--GRLV 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
48-259 |
3.60e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 3.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 48 SFRE-VSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGvpvRGPGP-DRGVVF 125
Cdd:COG1134 23 SLKElLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSALlELGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 126 QqyalfPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADaLP-RTLSGGMKQRCALARAYAVDPAVLLMDEP 204
Cdd:COG1134 100 H-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 205 FGALDALTRVRSQEQLLATWtRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRVH 259
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWL--EKGRLV 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
56-251 |
1.53e-35 |
|
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: 127.65 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 56 HPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVrgPGPDRGVVFQqyalfPWLT 135
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS--SLLGLGGGFN-----PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVR 215
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154143773 216 SQEqLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd03220 181 CQR-RLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
64-252 |
1.86e-35 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 126.95 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---GVVFQQYALFPWLTVRGNV 140
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrriGALIEAPGFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGLRLTRLpaaeRRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVRSQEQL 220
Cdd:cd03268 94 RLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG-IKELREL 168
|
170 180 190
....*....|....*....|....*....|..
gi 1154143773 221 LATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:cd03268 169 ILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
61-251 |
6.09e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 126.67 E-value: 6.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTL---LNLaagLDAPSGGEVLVDGVPV---RGPGP--------DRGVVFQ 126
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNL---LEMPRSGTLNIAGNHFdfsKTPSDkairelrrNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 127 QYALFPWLTVRGN-VEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:PRK11124 90 QYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154143773 206 GALDA-LTR--VRSQEQLLATWTrerrTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11124 170 AALDPeITAqiVSIIRELAETGI----TQVIVTHEVEVARKTASRVVYM 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
47-259 |
1.21e-34 |
|
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: 125.17 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-RGPGPDR---G 122
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 VVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMD 202
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 203 EPFGALDALTRvRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRVH 259
Cdd:cd03266 162 EPTTGLDVMAT-RALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR--GRVV 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
37-251 |
1.77e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 37 TRTPAPDRAKISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLL---N----LAAGLDApsGGEVLV 109
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGARV--EGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 110 DGVPVRGPGPD----R---GVVFQQYALFPwLTVRGNVEFGLRLT-RLPAAERRRRADHAIGLVGLGD-FADAL---PRT 177
Cdd:COG1117 76 DGEDIYDPDVDvvelRrrvGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALWDeVKDRLkksALG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 178 LSGGMKQRCALARAYAVDPAVLLMDEPFGALD--ALTRVrsqEQLLATwTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKI---EELILE-LKKDYTIVIVTHNMQQAARVSDYTAFF 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
61-251 |
2.29e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.13 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV---RGPGPDR--------GVVFQQYA 129
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirllrqkvGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 130 LFPWLTVRGN-VEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGAL 208
Cdd:COG4161 93 LWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154143773 209 D-ALTR--VRSQEQLLATWTrerrTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:COG4161 173 DpEITAqvVEIIRELSQTGI----TQVIVTHEVEFARKVASQVVYM 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
65-259 |
3.13e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVP--------VRgpgPDRGVVFQ----QyalFP 132
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdVR---RQVGMVFQnpdnQ---FV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 WLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALT 212
Cdd:PRK13635 96 GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 213 RvrsqEQLLATWTRERR----TVLFVTHDVDEAVYlAGRVVVMaaRPGRVH 259
Cdd:PRK13635 176 R----REVLETVRQLKEqkgiTVLSITHDLDEAAQ-ADRVIVM--NKGEIL 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
34-251 |
1.38e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 128.56 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 34 APLTRTPAPdraKISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVP 113
Cdd:TIGR02857 312 APVTAAPAS---SLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 114 VRGPGPDR-----GVVFQQYALFPwltvrGNVEFGLRLTRLPAAERRRRAdhAIGLVGLGDFADALP-----------RT 177
Cdd:TIGR02857 386 LADADADSwrdqiAWVPQHPFLFA-----GTIAENIRLARPDASDAEIRE--ALERAGLDEFVAALPqgldtpigeggAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 178 LSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTHDvDEAVYLAGRVVVM 251
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA--LAQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
64-241 |
2.78e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.80 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVlvdgvpVRGPGPDRGVVFQQYAL---FPwLTVRGNV 140
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------RRAGGARVAYVPQRSEVpdsLP-LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGL----RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRS 216
Cdd:NF040873 79 AMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|....*
gi 1154143773 217 qEQLLATWTRERRTVLFVTHDVDEA 241
Cdd:NF040873 159 -IALLAEEHARGATVVVVTHDLELV 182
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
64-251 |
4.81e-33 |
|
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: 122.22 E-value: 4.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP--------DRGVVFQQY--ALFPW 133
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrrafrrDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 134 LTVRGNVEFGLR-LTRLPAAERRRRADHAIGLVGL-GDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAL 211
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154143773 212 TRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
46-251 |
7.02e-33 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 120.39 E-value: 7.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 46 KISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP-----D 120
Cdd:cd03245 2 RIEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPadlrrN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 RGVVFQQYALFpWLTVRGNVEFGlrltrLPAAERRRRADhAIGLVGLGDFADALP-----------RTLSGGMKQRCALA 189
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNITLG-----APLADDERILR-AAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 190 RAYAVDPAVLLMDEPFGALDaltrVRSQEQL---LATWTRErRTVLFVTHDVdEAVYLAGRVVVM 251
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMD----MNSEERLkerLRQLLGD-KTLIIITHRP-SLLDLVDRIIVM 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-290 |
7.37e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 127.53 E-value: 7.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR--- 121
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ------GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVD 195
Cdd:PRK10535 83 lrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 196 PAVLLMDEPFGALDAltrvRSQEQLLATWT--RER-RTVLFVTHDVDEAVYlAGRVV------VMAARPGRVHRVV---E 263
Cdd:PRK10535 163 GQVILADEPTGALDS----HSGEEVMAILHqlRDRgHTVIIVTHDPQVAAQ-AERVIeirdgeIVRNPPAQEKVNVaggT 237
|
250 260
....*....|....*....|....*..
gi 1154143773 264 VPLPRPRTEELRLSREFAEVRNEVWHA 290
Cdd:PRK10535 238 EPVVNTASGWRQFVSGFREALTMAWRA 264
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-258 |
1.41e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 125.69 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 26 EKSRE-ETGAPLTRTpapdrakisfREVSRHH-PVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPS 103
Cdd:TIGR03269 268 EKECEvEVGEPIIKV----------RNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 104 GGEVLV----DGVPVRGPGPDR--------GVVFQQYALFPWLTVRGNVEFGLRLtRLPAAERRRRADHAIGLVGLGD-- 169
Cdd:TIGR03269 338 SGEVNVrvgdEWVDMTKPGPDGrgrakryiGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEek 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 170 ---FADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAG 246
Cdd:TIGR03269 417 aeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
250
....*....|..
gi 1154143773 247 RVVVMaaRPGRV 258
Cdd:TIGR03269 497 RAALM--RDGKI 506
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
40-263 |
5.44e-32 |
|
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: 124.03 E-value: 5.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 40 PAPDRAK--ISFREVSRHHPVKGG-------AFTALDRLSLDIAEGEFVAVVGPSGCGKSTL----LNLaagldAPSGGE 106
Cdd:COG4172 267 PVPPDAPplLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRL-----IPSEGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 107 VLVDGVPVRGPGPDRG--------VVFQQ-YA-LFPWLTVRGNVEFGLRL--TRLPAAERRRRADHAIGLVGL-GDFADA 173
Cdd:COG4172 342 IRFDGQDLDGLSRRALrplrrrmqVVFQDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 174 LPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrvRS-QEQ---LLATWTRERR-TVLFVTHDVdeAV--YLAG 246
Cdd:COG4172 422 YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-----VSvQAQildLLRDLQREHGlAYLFISHDL--AVvrALAH 494
|
250
....*....|....*..
gi 1154143773 247 RVVVMaaRPGrvhRVVE 263
Cdd:COG4172 495 RVMVM--KDG---KVVE 506
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
65-251 |
1.10e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-------GVVFQ--QYALFPwLT 135
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdirkkvGLVFQypEYQLFE-ET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFGLRLTRLPAAERRRRADHAIGLVGLG--DFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTR 213
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 214 VRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
80-251 |
1.54e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 120.36 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 80 AVVGPSGCGKSTLLNLAAGLDAPS------GGEVLVD---GVPVrgPGPDR--GVVFQQYALFPWLTVRGNVEFGLrltr 148
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQkgrivlNGRVLFDaekGICL--PPEKRriGYVFQDARLFPHYKVRGNLRYGM---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 149 lpAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaLTRVRSQEQLLATWTRER 228
Cdd:PRK11144 102 --AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKRELLPYLERLAREI 178
|
170 180
....*....|....*....|....
gi 1154143773 229 RT-VLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11144 179 NIpILYVSHSLDEILRLADRVVVL 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
65-252 |
1.74e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-----GVVFQ----QyalFPWLT 135
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirkkiGIIFQnpdnQ---FIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVR 215
Cdd:PRK13632 101 VEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154143773 216 SQEQLLATWTRERRTVLFVTHDVDEAVyLAGRVVVMA 252
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFS 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
64-251 |
2.59e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.16 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-------------GVVFQQYAL 130
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglirqlrqhvGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 131 FPWLTVRGNV-EFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:PRK11264 97 FPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154143773 210 ------ALTRVRSQEQllatwtrERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11264 177 pelvgeVLNTIRQLAQ-------EKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
54-251 |
2.98e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.48 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 54 RHHPV--KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV--------RGPGPDRGV 123
Cdd:PRK10419 14 AHGGLsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnraqrKAFRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 VFQQY--ALFPWLTVRGNVEFGLR-LTRLPAAERRRRADHAIGLVGLGD-FADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:PRK10419 94 VFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 200 LMDEPFGALDALTrvrsQEQLLATWTRERR----TVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK10419 174 ILDEAVSNLDLVL----QAGVIRLLKKLQQqfgtACLFITHDLRLVERFCQRVMVM 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
50-251 |
3.17e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 118.91 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 50 REVSRHHPVKGGAFT------ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD--- 120
Cdd:PRK11308 9 IDLKKHYPVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 ---RGV--VFQQ-YA-LFPWLTVRGNVEFGLRL-TRLPAAERRRRADHAIGLVGL-GDFADALPRTLSGGMKQRCALARA 191
Cdd:PRK11308 89 llrQKIqiVFQNpYGsLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 192 YAVDPAVLLMDEPFGALDaltrVRSQEQ---LLATWTRERRTV-LFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11308 169 LMLDPDVVVADEPVSALD----VSVQAQvlnLMMDLQQELGLSyVFISHDLSVVEHIADEVMVM 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
61-258 |
7.51e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 7.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP----DRGV--VFQQYALFPWL 134
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaqAAGIaiIHQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRLTRLPA---AERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDA- 210
Cdd:COG1129 95 SVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEr 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 211 -----LTRVRsqeQLlatwtRER-RTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:COG1129 175 everlFRIIR---RL-----KAQgVAIIYISHRLDEVFEIADRVTVL--RDGRL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
61-258 |
9.19e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 114.84 E-value: 9.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR------GVVFQQYALFPWL 134
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragiGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRltRLPAAERRRRADHAIGLV-GLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALdALTR 213
Cdd:cd03224 91 TVEENLLLGAY--ARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL-APKI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154143773 214 VRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03224 168 VEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLER--GRV 210
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
47-217 |
9.53e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.09 E-value: 9.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVR-GPGPDRG--- 122
Cdd:COG4167 10 LSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyGDYKYRCkhi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 -VVFQ--QYALFPWLTVRGNVEFGLRL-TRLPAAERRRRADHAIGLVGL-GDFADALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:COG4167 90 rMIFQdpNTSLNPRLNIGQILEEPLRLnTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPK 169
|
170 180
....*....|....*....|
gi 1154143773 198 VLLMDEPFGALDAltRVRSQ 217
Cdd:COG4167 170 IIIADEALAALDM--SVRSQ 187
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
58-259 |
1.42e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.64 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG-PGPD----RGVVFQQYAL-F 131
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAElarrRAVLPQHSSLsF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 PWlTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARA------YAVDPAVLLMDEPF 205
Cdd:PRK13548 90 PF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVlaqlwePDGPPRWLLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 206 GALDaltrVRSQE---QLLATWTRER-RTVLFVTHDVDEAVYLAGRVVVMAArpGRVH 259
Cdd:PRK13548 169 SALD----LAHQHhvlRLARQLAHERgLAVIVVLHDLNLAARYADRIVLLHQ--GRLV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
66-251 |
1.93e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.60 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGvpvrgpgpDR-------------GVVFQ----Qy 128
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG--------DLlteenvwdirhkiGMVFQnpdnQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 129 alFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDE----- 203
Cdd:PRK13650 94 --FVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEatsml 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 204 -PFGALD---ALTRVRSQEQLlatwtrerrTVLFVTHDVDEaVYLAGRVVVM 251
Cdd:PRK13650 172 dPEGRLElikTIKGIRDDYQM---------TVISITHDLDE-VALSDRVLVM 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
61-251 |
2.69e-30 |
|
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: 113.53 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-GVVFQQYALFPWLTVRGN 139
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 VEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVRSQEQ 219
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN-VELLKD 169
|
170 180 190
....*....|....*....|....*....|..
gi 1154143773 220 LLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd03269 170 VIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
46-252 |
3.21e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 113.12 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 46 KISFREvsrhhpvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVrgPGPDR---- 121
Cdd:cd03226 4 NISFSY--------KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERrksi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQ--QYALFpwltvRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:cd03226 74 GYVMQdvDYQLF-----TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 200 LMDEPFGALDaLTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:cd03226 149 IFDEPTSGLD-YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
61-258 |
3.68e-30 |
|
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: 111.75 E-value: 3.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR------GVVFQqyalfpwl 134
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarragiAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 tvrgnvefglrltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrV 214
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT----P 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 215 RSQEQLLATWTRERR---TVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:cd03216 116 AEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVL--RDGRV 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-237 |
1.76e-29 |
|
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: 117.08 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 29 REETGAPLTRTPAPDRAKISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVL 108
Cdd:TIGR02868 317 VAEGSAPAAGAVGLGKPTLELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 109 VDGVPVRGPGPDR-----GVVFQQYALFPwLTVRGNvefgLRLTRLPAAERRRRAdhAIGLVGLGDFADALP-------- 175
Cdd:TIGR02868 394 LDGVPVSSLDQDEvrrrvSVCAQDAHLFD-TTVREN----LRLARPDATDEELWA--ALERVGLADWLRALPdgldtvlg 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 176 ---RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTHD 237
Cdd:TIGR02868 467 eggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA--ALSGRTVVLITHH 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
47-263 |
2.05e-29 |
|
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: 111.86 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAfTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03249 1 IEFKNVSFRYPSRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrsqi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPwLTVRGNVEFGLRLTRLPAAERrrradhAIGLVGLGDFADALPR-----------TLSGGMKQRCALAR 190
Cdd:cd03249 80 GLVSQEPVLFD-GTIAENIRYGKPDATDEEVEE------AAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTH------DVDEAVYL-AGRVVVMA------ARPGR 257
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHrlstirNADLIAVLqNGQVVEQGthdelmAQKGV 230
|
....*.
gi 1154143773 258 VHRVVE 263
Cdd:cd03249 231 YAKLVK 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
64-252 |
2.23e-29 |
|
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: 111.66 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGvpvRGPGPDR-------GVVFQQYALFPW-LT 135
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVPWKRRkkflrriGVVFGQKTQLWWdLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVR 215
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 216 SQEqLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:cd03267 192 IRN-FLKEYNRERGtTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
47-251 |
2.35e-29 |
|
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: 110.64 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVS-RHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVdgvpvrgpGPDRGVVF 125
Cdd:cd03250 1 ISVEDASfTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--------PGSIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 126 QQyalfPWL---TVRGNVEFGLRLTrlpaAERRRRADHAIGLvgLGDFaDALPR-----------TLSGGMKQRCALARA 191
Cdd:cd03250 73 QE----PWIqngTIRENILFGKPFD----EERYEKVIKACAL--EPDL-EILPDgdlteigekgiNLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 192 -YAvDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVdEAVYLAGRVVVM 251
Cdd:cd03250 142 vYS-DADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
65-258 |
3.63e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRgPGPDR------GVVFQQY--ALFPwLTV 136
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKwvrskvGLVFQDPddQVFS-STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAltrvRS 216
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP----RG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154143773 217 QEQL---LATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:PRK13647 174 QETLmeiLDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE--GRV 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
47-260 |
4.39e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 111.33 E-value: 4.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-RGPGPDR---- 121
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELakrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPWLTVRGNVEFGL------RLTrlpaAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVD 195
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFGRfpyskgRLT----AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 196 PAVLLMDEPFGALDaLTRVRSQEQLLATWTRER-RTVLFVTHDVDEAVYLAGRVVVMaaRPGRVHR 260
Cdd:COG4604 154 TDYVLLDEPLNNLD-MKHSVQMMKLLRRLADELgKTVVIVLHDINFASCYADHIVAM--KDGRVVA 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
66-248 |
2.06e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 109.13 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-------RGPGPDR--GVVFQQYALFPWLTV 136
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaaKAELRNQklGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVRS 216
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN-ADS 183
|
170 180 190
....*....|....*....|....*....|...
gi 1154143773 217 QEQLLATWTRERRTV-LFVTHDVDeavyLAGRV 248
Cdd:PRK11629 184 IFQLLGELNRLQGTAfLVVTHDLQ----LAKRM 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
64-251 |
3.10e-28 |
|
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: 108.78 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----GVVF--QQYALFPWLTVR 137
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlGIGYlpQEASIFRKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 GNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVRSQ 217
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA-VQDI 172
|
170 180 190
....*....|....*....|....*....|....
gi 1154143773 218 EQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:cd03218 173 QKIIKILKDRGIGVLITDHNVRETLSITDRAYII 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
47-258 |
3.60e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 109.02 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSrhhpVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAP-SGGEVLVDGVPvRGpGPD----R 121
Cdd:COG1119 4 LELRNVT----VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGER-RG-GEDvwelR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---GVVfqQYALFPWLTVRGNVE-------FG-LRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALAR 190
Cdd:COG1119 78 kriGLV--SPALQLRFPRDETVLdvvlsgfFDsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTRvrsqEQLLATWTR----ERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGAR----ELLLALLDKlaaeGAPTLVLVTHHVEEIPPGITHVLLL--KDGRV 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
45-249 |
7.53e-28 |
|
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: 107.70 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVS----RHHPVkggaftaLDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD 120
Cdd:cd03254 1 GEIEFENVNfsydEKKPV-------LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 R-----GVVFQQYALFPWlTVRGNvefgLRLTRLPAAERRRRAdhAIGLVGLGDFADALPR-----------TLSGGMKQ 184
Cdd:cd03254 74 SlrsmiGVVLQDTFLFSG-TIMEN----IRLGRPNATDEEVIE--AAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 185 RCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTH------DVDEAVYL-AGRVV 249
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK--LMKGRTSIIIAHrlstikNADKILVLdDGKII 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
47-249 |
7.66e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 107.70 E-value: 7.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAftALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrqi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPWlTVRGNVEFGLRLTRLPAAERRRRADHAIglvglgDFADALPR-----------TLSGGMKQRCALAR 190
Cdd:cd03251 79 GLVSQDVFLFND-TVAENIAYGRPGATREEVEEAARAANAH------EFIMELPEgydtvigergvKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTRVRSQEQL--LAtwtrERRTVLFVTH------DVDEAVYL-AGRVV 249
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALerLM----KNRTTFVIAHrlstieNADRIVVLeDGKIV 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
71-263 |
1.26e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.79 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 71 LDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---------GVVFQQYALFPWLTVRGNVE 141
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 142 FGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLL 221
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154143773 222 ATWTRERRTVLFVTHDVDeavylagrvvvMAARPGRVHRVVE 263
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQ-----------LAARCDRRLRLVN 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
58-252 |
1.71e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.54 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAFTALDRL-----SLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVrgPGPDRG---------- 122
Cdd:PRK11831 10 MRGVSFTRGNRCifdniSLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--PAMSRSrlytvrkrms 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 VVFQQYALFPWLTVRGNVEFGLR-LTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLM 201
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 202 DEPFGALDALTR---VRSQEQLLATWTrerRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:PRK11831 168 DEPFVGQDPITMgvlVKLISELNSALG---VTCVVVSHDVPEVLSIADHAYIVA 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
47-258 |
2.01e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 104.61 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVkggaftaLDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03246 6 VSFRYPGAEPPV-------LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPWlTVRGNVefglrltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVLLM 201
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 202 DEPFGALDaLTRVRSQEQLLATWTRERRTVLFVTHDVdEAVYLAGRVVVMAArpGRV 258
Cdd:cd03246 121 DEPNSHLD-VEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLED--GRV 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
61-258 |
2.56e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP----DRGV--VFQQYALFPWL 134
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrdaiALGIgmVHQHFMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGL---RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEP------- 204
Cdd:COG3845 96 TVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPtavltpq 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 205 -----FGALDALtrvrsqeqllatwTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:COG3845 176 eadelFEILRRL-------------AAEGKSIIFITHKLREVMAIADRVTVL--RRGKV 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
65-252 |
3.45e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.09 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-------GVVFQQY--ALF-Pwl 134
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevrktvGIVFQNPddQLFaP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrV 214
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG-A 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 215 RSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:PRK13639 174 SQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMS 211
|
|
| COG4754 |
COG4754 |
Extracellular substrate-binding protein [General function prediction only]; |
47-284 |
3.60e-27 |
|
Extracellular substrate-binding protein [General function prediction only];
Pssm-ID: 443787 [Multi-domain] Cd Length: 435 Bit Score: 109.79 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQ 126
Cdd:COG4754 9 VLLLVVKSKKGSTGGSLLLLLDVNLLLLEEEEGGLLGGGGSGSSSLLLLIIGLLGPSSGGGGVLGGPGPPGGPPAVVVFF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 127 QYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFG 206
Cdd:COG4754 89 FFFLLLLLLVVLVVEELLLLAAARAEEARRRRAAAAIIIGLGGGEEAYPPELSGGGGRRRRVAAAAAVLPLLLLLLEPDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 207 ALDALTRV--RSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPGRVHRVVEVPLPRPRTEELRLSREFAEVR 284
Cdd:COG4754 169 ALALLLLTelLLLLLLLLLGEGRPIIIIIIVVVNIEEEEVVVDRIIRVGSSSGRRIAVEIVLPPPPRRRRDRAFFARVDI 248
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-236 |
1.09e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.81 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 25 REKSREETGaplTRTPAPDRAKISFREVSRHHPVKGGAfTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSG 104
Cdd:TIGR00958 460 RKPNIPLTG---TLAPLNLEGLIEFQDVSFSYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 105 GEVLVDGVPVRgpGPDRGVVFQQYALF---PWL---TVRGNVEFGlrLTRLPAAERRRRADHAiglvGLGDFADALPRT- 177
Cdd:TIGR00958 536 GQVLLDGVPLV--QYDHHYLHRQVALVgqePVLfsgSVRENIAYG--LTDTPDEEIMAAAKAA----NAHDFIMEFPNGy 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 178 ----------LSGGMKQRCALARAYAVDPAVLLMDEPFGALDAltrvrSQEQLLATW-TRERRTVLFVTH 236
Cdd:TIGR00958 608 dtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA-----ECEQLLQESrSRASRTVLLIAH 672
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
61-258 |
1.98e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.91 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD----RGVVF--QQYALFPWL 134
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarLGIGYvpEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRlTRLPAAERRRRADHAIGL--VgLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGAL---- 208
Cdd:COG0410 94 TVEENLLLGAY-ARRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLapli 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 209 -----DALTRVRsqeqllatwtRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG0410 172 veeifEIIRRLN----------REGVTILLVEQNARFALEIADRAYVLER--GRI 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
64-250 |
2.21e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.55 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDG-VPVRgpgpDR-------GVVF---QQyaLFP 132
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFK----RRkefarriGVVFgqrSQ--LWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 WLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALT 212
Cdd:COG4586 110 DLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154143773 213 --RVRsqeQLLATWTRERR-TVLFVTHDVDEAVYLAGRVVV 250
Cdd:COG4586 190 keAIR---EFLKEYNRERGtTILLTSHDMDDIEALCDRVIV 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
61-258 |
2.67e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.81 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD--------RGvvfqqyaLFP 132
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeeRG-------LYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 WLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALT 212
Cdd:COG4152 85 KMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154143773 213 RvrsqeQLLATWTRERR----TVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG4152 165 V-----ELLKDVIRELAakgtTVIFSSHQMELVEELCDRIVIINK--GRK 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
62-250 |
5.74e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.40 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 62 AFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGG------------------EVLVDGVPVRGPGPDR-- 121
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEKVLEKLVIQKTRFKKik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ---------GVVFQ--QYALFPwLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALA 189
Cdd:PRK13651 99 kikeirrrvGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 190 RAYAVDPAVLLMDEPFGALDAltrVRSQEQL--LATWTRERRTVLFVTHDVDEAVYLAGRVVV 250
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDP---QGVKEILeiFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
46-236 |
7.42e-26 |
|
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: 101.96 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 46 KISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSG---GEVLVDGVPV-RGPGPDR 121
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRkPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -GVVFQQYALFPWLTVRGNVEFG--LRLTRL-PAAERRRR-ADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDP 196
Cdd:cd03234 83 vAYVRQDDILLPGLTVRETLTYTaiLRLPRKsSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154143773 197 AVLLMDEPFGALDALTrVRSQEQLLATWTRERRTVLFVTH 236
Cdd:cd03234 163 KVLILDEPTSGLDSFT-ALNLVSTLSQLARRNRIVILTIH 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
47-251 |
1.23e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGV----PVRGPGPDR- 121
Cdd:PRK13644 2 IRLENVSYSYP---DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdFSKLQGIRKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -GVVFQQ-YALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:PRK13644 79 vGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 200 LMDEPFGALDALTRVRSQEQlLATWTRERRTVLFVTHDVDEaVYLAGRVVVM 251
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLER-IKKLHEKGKTIVYITHNLEE-LHDADRIIVM 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
61-257 |
1.63e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-----GVVFQQYALFPwLT 135
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrqqvSYCAQTPTLFG-DT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFglrltrlPAAERRRRADHAIGLVGLGDFadALPRT--------LSGGMKQRCALARAYAVDPAVLLMDEPFGA 207
Cdd:PRK10247 97 VYDNLIF-------PWQIRNQQPDPAIFLDDLERF--ALPDTiltkniaeLSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 208 LDALTRvRSQEQLLATWTRERR-TVLFVTHDVDEAVYlAGRVVVMAARPGR 257
Cdd:PRK10247 168 LDESNK-HNVNEIIHRYVREQNiAVLWVTHDKDEINH-ADKVITLQPHAGE 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
47-249 |
1.91e-25 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 101.15 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVS-RHHPvkggAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---- 121
Cdd:cd03253 1 IEFENVTfAYDP----GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -GVVFQQYALFPwLTVRGNVEFGlrltRLPAAERRRRAdhAIGLVGLGDFADALP---RT--------LSGGMKQRCALA 189
Cdd:cd03253 77 iGVVPQDTVLFN-DTIGYNIRYG----RPDATDEEVIE--AAKAAQIHDKIMRFPdgyDTivgerglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 190 RAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTH------DVDEAVYLA-GRVV 249
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRD--VSKGRTTIVIAHrlstivNADKIIVLKdGRIV 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
60-263 |
2.31e-25 |
|
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: 105.54 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 60 GGAFTALDRLSLDIAEGEFVAVVGPSGCGKS----TLLNLAAGLDAPSGGEVLVDGVP-----------VRGpgpDR-GV 123
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllglserelrrIRG---NRiAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 VFQQ--YALFPWLTVRGNVEFGLRL-TRLPAAERRRRADHAIGLVGLGDFA---DALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:COG4172 97 IFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 198 VLLMDEPFGALDaltrVRSQEQ---LLATWTRERRT-VLFVTHD---VDEavyLAGRVVVMaaRPGrvhRVVE 263
Cdd:COG4172 177 LLIADEPTTALD----VTVQAQildLLKDLQRELGMaLLLITHDlgvVRR---FADRVAVM--RQG---EIVE 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
47-251 |
2.34e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.75 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-----RGPGPDR 121
Cdd:PRK13648 8 IVFKNVSFQY--QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQ-YALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLL 200
Cdd:PRK13648 86 GIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 201 MDEPFGALDALTRvRSQEQLLATWTRERR-TVLFVTHDVDEAVYlAGRVVVM 251
Cdd:PRK13648 166 LDEATSMLDPDAR-QNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVM 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
45-251 |
2.65e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.58 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR--- 121
Cdd:PRK13537 6 APIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLL 200
Cdd:PRK13537 82 vGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 201 MDEPFGALDALTRVRSQEQLLATWTRErRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARG-KTILLTTHFMEEAERLCDRLCVI 211
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
65-258 |
2.78e-25 |
|
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: 100.91 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKST----LLNLAAGLDAPSGGEVLVDGVPVRGP---GPDRGVVFQ--QYALFPWLT 135
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLsirGRHIATIMQnpRTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADAL---PRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALT 212
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154143773 213 RVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRI 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-258 |
3.68e-25 |
|
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: 99.55 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 44 RAKISFRE--VSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSG--GEVLVDGVPVRGPGP 119
Cdd:cd03213 1 GVTLSFRNltVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 120 DR--GVVFQQYALFPWLTVRGNVEFGLRLtrlpaaerrrradhaiglvglgdfadalpRTLSGGMKQRCALARAYAVDPA 197
Cdd:cd03213 81 RKiiGYVPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 198 VLLMDEPFGALDAltrvRSQEQLLATWTRER---RTVLFVTHDV-DEAVYLAGRVVVMAarPGRV 258
Cdd:cd03213 132 LLFLDEPTSGLDS----SSALQVMSLLRRLAdtgRTIICSIHQPsSEIFELFDKLLLLS--QGRV 190
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
67-236 |
3.99e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 99.49 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 67 DRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDrgvvFQQYALF--------PWLTVRG 138
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQDLLYlghqpgikTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 139 NVEFGLRLTRLPAAERRRradHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAlTRVRSQE 218
Cdd:PRK13538 94 NLRFYQRLHGPGDDEALW---EALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK-QGVARLE 169
|
170
....*....|....*...
gi 1154143773 219 QLLATWTRERRTVLFVTH 236
Cdd:PRK13538 170 ALLAQHAEQGGMVILTTH 187
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
61-258 |
8.25e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRgvVFQQYALFPW------- 133
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLALLPQhhltpeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 134 LTVRGNVEFGlrltRLP--------AAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:PRK11231 91 ITVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 206 GALDaltrVRSQEQLLATwTRERR----TVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:PRK11231 167 TYLD----INHQVELMRL-MRELNtqgkTVVTVLHDLNQASRYCDHLVVLAN--GHV 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
64-251 |
1.23e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGV---------PVRGPGpdrGVVFQQyalfP-- 132
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsdeenlwDIRNKA---GMVFQN----Pdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 ---WLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:PRK13633 97 qivATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154143773 210 ALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYlAGRVVVM 251
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVM 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
65-247 |
1.27e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLL---NLAAGL--DAPSGGEVLVDGVPVRGPGPDR-------GVVFQQYALFP 132
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYSPRTDTvdlrkeiGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 wLTVRGNVEFGLRLTrlpAAERRRRADHAI--GLVGLGDFADALPR------TLSGGMKQRCALARAYAVDPAVLLMDEP 204
Cdd:PRK14239 100 -MSIYENVVYGLRLK---GIKDKQVLDEAVekSLKGASIWDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154143773 205 FGALDALTRVRSQEQLLAtwTRERRTVLFVTHDVDEAVYLAGR 247
Cdd:PRK14239 176 TSALDPISAGKIEETLLG--LKDDYTMLLVTRSMQQASRISDR 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
58-259 |
1.80e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-----RGPGPDRGVVFQQYALFP 132
Cdd:PRK09536 11 VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 WLTVRGNVEFGL--RLTRL-PAAERRRRA-DHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGAL 208
Cdd:PRK09536 91 EFDVRQVVEMGRtpHRSRFdTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 209 DALTRVRSQEqLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRVH 259
Cdd:PRK09536 171 DINHQVRTLE-LVRRLVDDGKTAVAAIHDLDLAARYCDELVLLAD--GRVR 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
47-251 |
2.83e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.15 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV----RGPGPDR- 121
Cdd:PRK13636 6 LKVEELNYNYS---DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 --GVVFQQ--YALFPwLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPA 197
Cdd:PRK13636 83 svGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 198 VLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
64-209 |
2.84e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.18 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV----------RGPG--PdrgvvfQQYALF 131
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarLGIGylP------QEASIF 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 132 PWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:COG1137 91 RKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
41-251 |
3.54e-24 |
|
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: 97.54 E-value: 3.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 41 APD--RAKISFREVSRHHPVKGgAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVrgPG 118
Cdd:cd03248 4 APDhlKGIVKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI--SQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 119 PDR-------GVVFQQYALFPwLTVRGNVEFGLR---LTRLPAAERRRRADHAIGLVGLGDFADALPR--TLSGGMKQRC 186
Cdd:cd03248 81 YEHkylhskvSLVGQEPVLFA-RSLQDNIAYGLQscsFECVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 187 ALARAYAVDPAVLLMDEPFGALDALTRVRSQeQLLATWTrERRTVLFVTHDVdEAVYLAGRVVVM 251
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQ-QALYDWP-ERRTVLVIAHRL-STVERADQILVL 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
47-251 |
4.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.94 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVS-RHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVdGVPVRGPG------- 118
Cdd:PRK13634 3 ITFQKVEhRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 119 PDR---GVVFQ--QYALFPwLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALARAY 192
Cdd:PRK13634 82 PLRkkvGIVFQfpEHQLFE-ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 193 AVDPAVLLMDEPFGALDAltrvRSQEQLLATWTRERR----TVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDP----KGRKEMMEMFYKLHKekglTTVLVTHSMEDAARYADQIVVM 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
61-210 |
5.53e-24 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 96.27 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV--RGPGPDRGVVF--QQYALFPWLTV 136
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENILYlgHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 137 RGNVEFglrLTRLPAAErRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDA 210
Cdd:TIGR01189 91 LENLHF---WAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
47-236 |
6.43e-24 |
|
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: 95.84 E-value: 6.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----G 122
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 VVFQQYALFPwLTVRGNVefGLRltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVLLMD 202
Cdd:cd03247 79 VLNQRPYLFD-TTLRNNL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154143773 203 EPFGALDALTrvrsQEQLLATWTR--ERRTVLFVTH 236
Cdd:cd03247 124 EPTVGLDPIT----ERQLLSLIFEvlKDKTLIWITH 155
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
61-237 |
7.11e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVlvdgvpVRGPGPDRGVVFQQYALFPWLTVRGNV 140
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------SIPKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGLRltRLPAAERRRR------------------------------ADHAIG--LVGLG---DFADALPRTLSGGMKQR 185
Cdd:COG0488 83 LDGDA--ELRALEAELEeleaklaepdedlerlaelqeefealggweAEARAEeiLSGLGfpeEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 186 CALARAYAVDPAVLLMDEPFGALDALTRvrsqeQLLATWTRERR-TVLFVTHD 237
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESI-----EWLEEFLKNYPgTVLVVSHD 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
65-258 |
1.02e-23 |
|
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: 95.19 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP----DRGVVF-----QQYALFPWLT 135
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdaiRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVefglrltrlpaaerrrradhaiglvglgdfadALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVR 215
Cdd:cd03215 95 VAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154143773 216 SQEQLLATwTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:cd03215 143 IYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
47-251 |
1.41e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.18 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAftALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL---DAPSGGEVLVDGVP--------VR 115
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITltaktvwdIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 116 gpgpDR-GVVFQ----QyalFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALAR 190
Cdd:PRK13640 84 ----EKvGIVFQnpdnQ---FVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVyLAGRVVVM 251
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVL 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
47-241 |
1.65e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.58 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGpDRGVVFQ 126
Cdd:NF033858 2 ARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR-HRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 127 QYA---------LFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQR----CALARaya 193
Cdd:NF033858 77 RIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlglcCALIH--- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 194 vDPAVLLMDEPFGALDALTRvRSQEQLLATwTRERR---TVLFVTHDVDEA 241
Cdd:NF033858 154 -DPDLLILDEPTTGVDPLSR-RQFWELIDR-IRAERpgmSVLVATAYMEEA 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
65-258 |
1.70e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.62 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL---DAPSGGEVLVDGVPVRGPG----------PDRGVVFQQYALF 131
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlardirksrANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 PWLTVRGNVEFGlRLTRLP---------AAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMD 202
Cdd:PRK09984 99 NRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 203 EPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVvmAARPGRV 258
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV--ALRQGHV 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
64-258 |
2.21e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 96.31 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV-RGPGPDR----GVVFQQYAL--FPWLTV 136
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRakyiGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 ---------RGNVeFGLRLtRLPAAERRRRADH--AIGLvGLGDFADALPRTLSGGmkQRCALARAYAV--DPAVLLMDE 203
Cdd:COG1101 100 eenlalayrRGKR-RGLRR-GLTKKRRELFRELlaTLGL-GLENRLDTKVGLLSGG--QRQALSLLMATltKPKLLLLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 204 PFGALD--------ALTRVRSQEQLLatwtrerrTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:COG1101 175 HTAALDpktaalvlELTEKIVEENNL--------TTLMVTHNMEQALDYGNRLIMMHE--GRI 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
47-238 |
2.25e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.33 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG------PGPD 120
Cdd:PRK10908 2 IRFEHVSKAYL---GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 R--GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:PRK10908 79 RqiGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154143773 199 LLMDEPFGALD-ALTrvRSQEQLLATWTRERRTVLFVTHDV 238
Cdd:PRK10908 159 LLADEPTGNLDdALS--EGILRLFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
66-251 |
2.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---------GVVFQ--QYALFPwL 134
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrkkvSLVFQfpEAQLFE-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTR 213
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 214 vRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13641 182 -KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-253 |
4.39e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 14 DRTREKTREETREKSREETGAPLTRTPAPdrAKISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLL 93
Cdd:PRK13536 11 PRRLELSPIERKHQGISEAKASIPGSMST--VAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 94 NLAAGLDAPSGGEVLVDGVPVrgPGPDR------GVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGL 167
Cdd:PRK13536 85 RMILGMTSPDAGKITVLGVPV--PARARlarariGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 168 GDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRErRTVLFVTHDVDEAVYLAGR 247
Cdd:PRK13536 163 ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAERLCDR 241
|
....*.
gi 1154143773 248 VVVMAA 253
Cdd:PRK13536 242 LCVLEA 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-258 |
1.01e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 38 RTPAPDRAKISFREVSRHHPVKGgaftaldrLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGP 117
Cdd:COG1129 248 RAAAPGEVVLEVEGLSVGGVVRD--------VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 118 GP----DRGVVF-----QQYALFPWLTVRGNVEFGL--RLTR---LPAAERRRRADHAIGLVGL--GDfADALPRTLSGG 181
Cdd:COG1129 320 SPrdaiRAGIAYvpedrKGEGLVLDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRIktPS-PEQPVGNLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 182 MKQRCALARAYAVDPAVLLMDEPfgaldalTR---VRS-QE--QLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRP 255
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEP-------TRgidVGAkAEiyRLIRELAAEGKAVIVISSELPELLGLSDRILVM--RE 469
|
...
gi 1154143773 256 GRV 258
Cdd:COG1129 470 GRI 472
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
61-263 |
1.14e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.46 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLL-------NLAAGLDAPsgGEVLVDGVPVRGPGPDR-------GVVFQ 126
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVE--GKVTFHGKNLYAPDVDPvevrrriGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 127 QYALFPwLTVRGNVEFGLRLTRLPA-----AERR-RRAdhaiglvGLGD-FADALPRT---LSGGMKQRCALARAYAVDP 196
Cdd:PRK14243 99 KPNPFP-KSIYDNIAYGARINGYKGdmdelVERSlRQA-------ALWDeVKDKLKQSglsLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 197 AVLLMDEPFGALDALTRVRSQEqlLATWTRERRTVLFVTHDVDEavylAGRVVVMAA--------RPGRVHRVVE 263
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEE--LMHELKEQYTIIIVTHNMQQ----AARVSDMTAffnvelteGGGRYGYLVE 239
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
61-258 |
2.87e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 93.07 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGvpvRGpgpdrGVVFQQYAL---------- 130
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM---RD-----GQLRDLYALseaerrrllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 131 FPWLTVRGNVEFGLRLT---------RLPAA-ER-----RRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALARAYAV 194
Cdd:PRK11701 89 TEWGFVHQHPRDGLRMQvsaggnigeRLMAVgARhygdiRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 195 DPAVLLMDEPFGALDALTRVRSQEqLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLD-LLRGLVRELGlAVVIVTHDLAVARLLAHRLLVM--KQGRV 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
37-260 |
2.91e-22 |
|
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: 96.36 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 37 TRTPAPdRAKISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG 116
Cdd:COG4618 322 MPLPRP-KGRLSVENLTVVPP--GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 117 PGPDR-----GVVFQQYALFPWlTVRGNVefglrlTRLPAAERRRRADHAIgLVGLGDFADALP-----------RTLSG 180
Cdd:COG4618 399 WDREElgrhiGYLPQDVELFDG-TIAENI------ARFGDADPEKVVAAAK-LAGVHEMILRLPdgydtrigeggARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 181 GMKQRCALARAYAVDPAVLLMDEPFGALD-----ALTRvrsqeqLLATWTRERRTVLFVTHDVdEAVYLAGRVVVMaaRP 255
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaALAA------AIRALKARGATVVVITHRP-SLLAAVDKLLVL--RD 541
|
....*
gi 1154143773 256 GRVHR 260
Cdd:COG4618 542 GRVQA 546
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
53-248 |
4.13e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.60 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 53 SRHHPVKGgaftaldrLSLDIAEGEFVAVVGPSGCGKSTLLN-----LAAGLDAPSGGEVLVDGVPVRGPGPDR------ 121
Cdd:PRK14267 15 GSNHVIKG--------VDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPievrre 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -GVVFQQYALFPWLTVRGNVEFGLRLTRL--PAAERRRRADHAIGLVGLGD-FADAL---PRTLSGGMKQRCALARAYAV 194
Cdd:PRK14267 87 vGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDeVKDRLndyPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 195 DPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTHDVDEAVYLAGRV 248
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFE--LKKEYTIVLVTHSPAQAARVSDYV 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
46-251 |
5.09e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 46 KISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRG--- 122
Cdd:PRK10619 5 KLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 ---------------VVFQQYALFPWLTVRGNV-EFGLRLTRLPAAERRRRADHAIGLVGLGDFA-DALPRTLSGGMKQR 185
Cdd:PRK10619 81 vadknqlrllrtrltMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 186 CALARAYAVDPAVLLMDEPFGALDA--LTRVRSQEQLLAtwtRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPelVGEVLRIMQQLA---EEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
47-258 |
6.24e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHH----PVKGgafTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR- 121
Cdd:PRK13649 3 INLQNVSYTYqagtPFEG---RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 --------GVVFQ--QYALFPWlTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALAR 190
Cdd:PRK13649 80 ikqirkkvGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTRvRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAArpGRV 258
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGR-KELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEK--GKL 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
47-251 |
6.68e-22 |
|
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: 91.78 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHpvKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:cd03252 1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlrrqv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPwLTVRGNVEfglrLTRlPAAErRRRADHAIGLVGLGDFADALPR-----------TLSGGMKQRCALAR 190
Cdd:cd03252 79 GVVLQENVLFN-RSIRDNIA----LAD-PGMS-MERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTR---VRSQEQLLATwtrerRTVLFVTHDVdEAVYLAGRVVVM 251
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEhaiMRNMHDICAG-----RTVIIIAHRL-STVKNADRIIVM 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
66-253 |
7.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.46 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPG-----PDRGVVFQQY-ALFPWLTVRGN 139
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 VEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQ 219
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....
gi 1154143773 220 LLATWTRERRTVLFVTHDVDEAVYlAGRVVVMAA 253
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKA 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
61-253 |
7.97e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.58 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVrGPGpD----RGVVF--QQYALFPWL 134
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAG-DiatrRRVGYmsQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRV 214
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 215 RSQeQLLATWTRERRTVLFV-THDVDEA-----VYL--AGRVVVMAA 253
Cdd:NF033858 435 MFW-RLLIELSREDGVTIFIsTHFMNEAercdrISLmhAGRVLASDT 480
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-236 |
1.34e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 35 PLTRTPAPDRAKISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV 114
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 115 RGPGPDR-----GVVFQQYALFPwLTVRGNvefgLRLTRLPAAERRRRAdhAIGLVGLGDFADALP----------RTLS 179
Cdd:PRK11160 405 ADYSEAAlrqaiSVVSQRVHLFS-ATLRDN----LLLAAPNASDEALIE--VLQQVGLEKLLEDDKglnawlgeggRQLS 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 180 GGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvRSQEQLLATWTRErRTVLFVTH 236
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE-RQILELLAEHAQN-KTVLMITH 532
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-249 |
2.83e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 93.73 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 26 EKSREETGAPLTRTPAPDRAKISFREVSRHHpvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGG 105
Cdd:COG5265 337 DQPPEVADAPDAPPLVVGGGEVRFENVSFGY---DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSG 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 106 EVLVDGVPVRGPGPD--R---GVVFQQYALFPwLTVRGNVEFGlrltRLPA--AERRRRADHAiglvGLGDFADALP--- 175
Cdd:COG5265 414 RILIDGQDIRDVTQAslRaaiGIVPQDTVLFN-DTIAYNIAYG----RPDAseEEVEAAARAA----QIHDFIESLPdgy 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 176 RT--------LSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQL--LAtwtrERRTVLFVTH------DVD 239
Cdd:COG5265 485 DTrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALreVA----RGRTTLVIAHrlstivDAD 560
|
250
....*....|.
gi 1154143773 240 EAVYL-AGRVV 249
Cdd:COG5265 561 EILVLeAGRIV 571
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
46-251 |
2.91e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 46 KISFREVSRHHPvKGGAF--TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-- 121
Cdd:PRK13646 2 TIRFDNVSYTYQ-KGTPYehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -------GVVFQ--QYALFPwLTVRGNVEFGLRLTRLPAAERRRRADHAigLVGLG---DFADALPRTLSGGMKQRCALA 189
Cdd:PRK13646 81 rpvrkriGMVFQfpESQLFE-DTVEREIIFGPKNFKMNLDEVKNYAHRL--LMDLGfsrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 190 RAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-278 |
4.94e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTL---LNLAAGLDapsgGEVLVDG--------VPVRGPGPDR-----GVVFQQYA 129
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELE----SEVRVEGrveffnqnIYERRVNLNRlrrqvSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 130 LFPwLTVRGNVEFGLRLTRL-PAAERRRRADHAIGLVGLGD-FADALPRT---LSGGMKQRCALARAYAVDPAVLLMDEP 204
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDeIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 205 FGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPGRVHRVVEVPLPR--------PRTEELRL 276
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTKkifnsphdSRTREYVL 257
|
..
gi 1154143773 277 SR 278
Cdd:PRK14258 258 SR 259
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
69-236 |
6.64e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 6.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVF--QQYALFPWLTVRGNVEFGLRL 146
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlgHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 147 trlpAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVRSQEqLLATWTR 226
Cdd:PRK13539 101 ----LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD----AAAVA-LFAELIR 171
|
170
....*....|....
gi 1154143773 227 ERR----TVLFVTH 236
Cdd:PRK13539 172 AHLaqggIVIAATH 185
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
47-257 |
7.76e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 7.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGgafTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR----- 121
Cdd:PRK13657 335 VEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrrni 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQQYALFPwLTVRGNvefgLRLTRLPA--AERRRRADHAIGLvglgDFADALP-----------RTLSGGMKQRCAL 188
Cdd:PRK13657 412 AVVFQDAGLFN-RSIEDN----IRVGRPDAtdEEMRAAAERAQAH----DFIERKPdgydtvvgergRQLSGGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 189 ARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTH------DVDEAVYL-AGRVVVM------AARP 255
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDE--LMKGRTTFIIAHrlstvrNADRILVFdNGRVVESgsfdelVARG 560
|
..
gi 1154143773 256 GR 257
Cdd:PRK13657 561 GR 562
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
51-282 |
8.94e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.57 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 51 EVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKS-TLLNLAAGLDAPsgGEVLVDGVPVRGP------------ 117
Cdd:PRK11022 8 KLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQdlqrisekerrn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 118 --GPDRGVVFQQ--YALFPWLTVRGNVEFGLRLTRLPA-AERRRRADHAIGLVGLGDFA---DALPRTLSGGMKQRCALA 189
Cdd:PRK11022 86 lvGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNkKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 190 RAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAA----RPGRVHRVVEVP 265
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAgqvvETGKAHDIFRAP 245
|
250
....*....|....*...
gi 1154143773 266 LpRPRTEEL-RLSREFAE 282
Cdd:PRK11022 246 R-HPYTQALlRALPEFAQ 262
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
66-258 |
8.95e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.68 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV----RGPGPDR---GVVFQ--QYALFpWLTV 136
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLALRqqvATVFQdpEQQIF-YTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVrs 216
Cdd:PRK13638 96 DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT-- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 217 qeQLLATWTR---ERRTVLFVTHDVD------EAVYLAGRVVVMAA-RPGRV 258
Cdd:PRK13638 174 --QMIAIIRRivaQGNHVIISSHDIDliyeisDAVYVLRQGQILTHgAPGEV 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
63-252 |
1.25e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 63 FTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLV----------DGVPVRGPGPDR----------- 121
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKiknfkelrrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 GVVFQ--QYALFPwLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGD-FADALPRTLSGGMKQRCALARAYAVDPAV 198
Cdd:PRK13631 119 SMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 199 LLMDEPFGALDALTRvRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:PRK13631 198 LIFDEPTAGLDPKGE-HEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
64-258 |
1.29e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD---RGVVF--QQYALFPWLTVRG 138
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYlpQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 139 NVEFGlrltRLP--------AAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDa 210
Cdd:PRK10575 105 LVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 211 ltrVRSQEQLLA---TWTRER-RTVLFVTHDVDEAVYLAGRVVvmAARPGRV 258
Cdd:PRK10575 180 ---IAHQVDVLAlvhRLSQERgLTVIAVLHDINMAARYCDYLV--ALRGGEM 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
63-251 |
1.72e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 63 FTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVD--GVP--------VRGPGPDRGVVFQ--QYAL 130
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPanlkkikeVKRLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 131 FPwLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:PRK13645 104 FQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154143773 210 AltrvRSQEQLLATWTR----ERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13645 183 P----KGEEDFINLFERlnkeYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
61-251 |
3.14e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVP-----VRGPGPDRGVVFQQY--ALFPw 133
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenIREVRKFVGLVFQNPddQIFS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 134 LTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTR 213
Cdd:PRK13652 94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 214 VRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
47-251 |
4.33e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.87 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVS-RHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR---- 121
Cdd:PRK13643 2 IKFEKVNyTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 -----GVVFQ--QYALFPWlTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLG-DFADALPRTLSGGMKQRCALARAYA 193
Cdd:PRK13643 82 vrkkvGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 194 VDPAVLLMDEPFGALDALTRVRSQeQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-259 |
5.01e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 14 DRTREKTREETREKSREETGAPLTRTPAPDR---AKISFREVSR--------HHPVKG-GAFTALDRLSLDIAEGEFVAV 81
Cdd:COG0488 267 RRFRAKARKAKQAQSRIKALEKLEREEPPRRdktVEIRFPPPERlgkkvlelEGLSKSyGDKTLLDDLSLRIDRGDRIGL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 82 VGPSGCGKSTLLNLAAGLDAPSGGEVlvdgvpVRGPGPDRGVVFQQYALF-PWLTVRGNVEfglrltrlPAAERRRRAdH 160
Cdd:COG0488 347 IGPNGAGKSTLLKLLAGELEPDSGTV------KLGETVKIGYFDQHQEELdPDKTVLDELR--------DGAPGGTEQ-E 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 161 AIGLVGL----GDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvRSQEQLLATWTrerRTVLFVTH 236
Cdd:COG0488 412 VRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL-EALEEALDDFP---GTVLLVSH 487
|
250 260
....*....|....*....|....*
gi 1154143773 237 DvdeaVYLAGRVV--VMAARPGRVH 259
Cdd:COG0488 488 D----RYFLDRVAtrILEFEDGGVR 508
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
61-251 |
7.84e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.58 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG-PG---PDRGVV--FQQYALFPWL 134
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGhqiARMGVVrtFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGN--------VEFGL--RLTRLPA---AERR--RRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:PRK11300 96 TVIENllvaqhqqLKTGLfsGLLKTPAfrrAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 200 LMDEPFGALDAlTRVRSQEQLLATWTRERR-TVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11300 176 MLDEPAAGLNP-KETKELDELIAELRNEHNvTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
69-240 |
1.28e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdAPSGGEVLVDGVPVRGPGPD--RgvvfQQYAlfpWL---------TVR 137
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPEswR----KHLS---WVgqnpqlphgTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 GNVefglRLTRLPAAErrRRADHAIGLVGLGDFADALPR-----------TLSGGMKQRCALARAYAVDPAVLLMDEPFG 206
Cdd:PRK11174 441 DNV----LLGNPDASD--EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154143773 207 ALDAltrvRSQEQLLATWTR--ERRTVLFVTHDVDE 240
Cdd:PRK11174 515 SLDA----HSEQLVMQALNAasRRQTTLMVTHQLED 546
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-259 |
1.77e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.92 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 16 TREKTREETREKSREETGAPltrtPAPDRAKISFREvsRHHP--VKGGAFT------------ALDRLSLDIAEGEFVAV 81
Cdd:TIGR01257 888 TREERALEKTEPLTEEMEDP----EHPEGINDSFFE--RELPglVPGVCVKnlvkifepsgrpAVDRLNITFYENQITAF 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 82 VGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVR----GPGPDRGVVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRR 157
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 158 ADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRvRSQEQLLATWtRERRTVLFVTHD 237
Cdd:TIGR01257 1042 MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR-RSIWDLLLKY-RSGRTIIMSTHH 1119
|
250 260
....*....|....*....|..
gi 1154143773 238 VDEAVYLAGRVVVMAArpGRVH 259
Cdd:TIGR01257 1120 MDEADLLGDRIAIISQ--GRLY 1139
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
61-258 |
1.78e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.81 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD----RGVVFQQYALFPW-LT 135
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevarRIGLLAQNATTPGdIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVEFGlRLTRLPAAERRRRADH-----AIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDA 210
Cdd:PRK10253 98 VQELVARG-RYPHQPLFTRWRKEDEeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154143773 211 LTRVRSQEqLLATWTRER-RTVLFVTHDVDEAVYLAGRVVvmAARPGRV 258
Cdd:PRK10253 177 SHQIDLLE-LLSELNREKgYTLAAVLHDLNQACRYASHLI--ALREGKI 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
75-263 |
2.96e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 75 EGEFVAVVGPSGCGKSTLLNLAAGLDAPS---GGEVLVDGVPVRGPGPDR--GVVFQQYALFPWLTVRGNVEFG--LRLT 147
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHLMFQahLRMP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 148 R-LPAAERRRRADHAIGLVGLGDFADAL------PRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVRSQEQL 220
Cdd:TIGR00955 130 RrVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM-AYSVVQV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 221 LATWTRERRTVLFVTHD--------VDEAVYLA-GRVVVMaarpGRVHRVVE 263
Cdd:TIGR00955 209 LKGLAQKGKTIICTIHQpsselfelFDKIILMAeGRVAYL----GSPDQAVP 256
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-236 |
5.62e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.19 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 44 RAKISFREVSrhhpVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL-----DAPSGGEVLVDG-----VP 113
Cdd:PRK14247 1 MNKIEIRDLK----VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGqdifkMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 114 VRGPGPDRGVVFQQYALFPWLTVRGNVEFGLRLTRL--PAAERRRRADHAIGLVGL----GDFADALPRTLSGGMKQRCA 187
Cdd:PRK14247 77 VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154143773 188 LARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTH 236
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLE--LKKDMTIVLVTH 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
65-251 |
5.86e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVR-GPGPDRG----VVFQ--QYALFPWLTVR 137
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRSqrirMIFQdpSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 GNVEFGLRL-TRLPAAERRRRADHAIGLVGL-GDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDalTRVR 215
Cdd:PRK15112 108 QILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD--MSMR 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154143773 216 SQEQLLATWTRERRTV--LFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK15112 186 SQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVM 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
64-243 |
8.31e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.47 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSG--GEVLVDGVPVRGPGPDR-GVVFQQYALFPWLTVRGNV 140
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFgLRLTRLPAA----ERRRRADHAIGLVGLGD-----FADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAL 211
Cdd:PLN03211 162 VF-CSLLRLPKSltkqEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190
....*....|....*....|....*....|..
gi 1154143773 212 TRVRSQeQLLATWTRERRTVLFVTHDVDEAVY 243
Cdd:PLN03211 241 AAYRLV-LTLGSLAQKGKTIVTSMHQPSSRVY 271
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
69-275 |
2.65e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKStlLNLAAGLD-APSG-----GEVLVDGVPVrGPGPDRG----VVFQ--QYALFPWLTV 136
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKS--LTCAAALGiLPAGvrqtaGRVLLDGKPV-APCALRGrkiaTIMQnpRSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGN-VEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVR 215
Cdd:PRK10418 99 HTHaRETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 216 SQEqLLATWTRERRT-VLFVTHDVDEAVYLAGRVVVMAArpGRV--HRVVEVPLPRPRTEELR 275
Cdd:PRK10418 179 ILD-LLESIVQKRALgMLLVTHDMGVVARLADDVAVMSH--GRIveQGDVETLFNAPKHAVTR 238
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
64-245 |
2.87e-18 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 81.68 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVP-VRGPGPDRGVVFQQYALFPWLTVRGNVEF 142
Cdd:TIGR03740 14 TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKDLHKIGSLIESPPLYENLTARENLKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 143 GLRLTRLPAAerrrRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVRSQEQLLA 222
Cdd:TIGR03740 94 HTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIG-IQELRELIR 168
|
170 180
....*....|....*....|...
gi 1154143773 223 TWTRERRTVLFVTHDVDEAVYLA 245
Cdd:TIGR03740 169 SFPEQGITVILSSHILSEVQQLA 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
64-251 |
3.48e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP----DRGVVF-----QQYALFPWL 134
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerrRLGVAYipedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGL----RLTRLPAAERRRRADHAIGLVglGDF------ADALPRTLSGGMKQRCALARAYAVDPAVLLMDEP 204
Cdd:COG3845 352 SVAENLILGRyrrpPFSRGGFLDRKAIRAFAEELI--EEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154143773 205 FGALD--ALTRVRsqEQLLAtwTRERRT-VLFVTHDVDEAVYLAGRVVVM 251
Cdd:COG3845 430 TRGLDvgAIEFIH--QRLLE--LRDAGAaVLLISEDLDEILALSDRIAVM 475
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
59-272 |
3.84e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 59 KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP--------DRGVVFQQ--Y 128
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewravrsDIQMIFQDplA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 129 ALFPWLTVRGNVEFGLRL--TRLPAAERRRRADHAIGLVGL-GDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:PRK15079 110 SLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 206 GALDaltrVRSQEQ---LLATWTRERRTVL-FVTHDVDEAVYLAGRVVVM----AARPGRVHRVVE-------------V 264
Cdd:PRK15079 190 SALD----VSIQAQvvnLLQQLQREMGLSLiFIAHDLAVVKHISDRVLVMylghAVELGTYDEVYHnplhpytkalmsaV 265
|
....*...
gi 1154143773 265 PLPRPRTE 272
Cdd:PRK15079 266 PIPDPDLE 273
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-258 |
4.15e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 30 EETGAPLtrtPAPDRAK--ISFREVSRHHPVKGGAF-------TALDRLSLDIAEGEFVAVVGPSGCGKST----LLNLA 96
Cdd:PRK15134 260 EPSGDPV---PLPEPASplLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 97 AgldapSGGEVLVDGVPVRGPGPDR--------GVVFQ--QYALFPWLTVRGNVEFGLRLTR--LPAAERRRRADHAIGL 164
Cdd:PRK15134 337 N-----SQGEIWFDGQPLHNLNRRQllpvrhriQVVFQdpNSSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 165 VGLG-DFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrvRS-QEQLLATW----TRERRTVLFVTHDV 238
Cdd:PRK15134 412 VGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-----KTvQAQILALLkslqQKHQLAYLFISHDL 486
|
250 260
....*....|....*....|
gi 1154143773 239 DEAVYLAGRVVVMaaRPGRV 258
Cdd:PRK15134 487 HVVRALCHQVIVL--RQGEV 504
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
61-236 |
4.72e-18 |
|
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: 80.61 E-value: 4.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD--RGVVF--QQYALFPWLTV 136
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYlgHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEFGLRLTRLPAAERrrradhAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAlTRVRS 216
Cdd:cd03231 91 LENLRFWHADHSDEQVEE------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK-AGVAR 163
|
170 180
....*....|....*....|
gi 1154143773 217 QEQLLATWTRERRTVLFVTH 236
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
69-258 |
5.74e-18 |
|
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: 81.42 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEV---LVDGVPV---RGPGPDRgvvfQQYALFPWLTVRGNVEF 142
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyiMRSGAELelyQLSEAER----RRLMRTEWGFVHQNPRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 143 GLRLTRLPAAERRRRAdHAIGLVGLGDF-----------------ADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:TIGR02323 98 GLRMRVSAGANIGERL-MAIGARHYGNIrataqdwleeveidptrIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 206 GALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:TIGR02323 177 GGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRV 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
45-257 |
1.59e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHP-VKggaftALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP---- 119
Cdd:PRK11288 3 PYLSFDGIGKTFPgVK-----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtaal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 120 DRGV--VFQQYALFPWLTVRGNvefgLRLTRLPAA-----ERRRRADHAIGLVGLGDFADalPRT----LSGGMKQRCAL 188
Cdd:PRK11288 78 AAGVaiIYQELHLVPEMTVAEN----LYLGQLPHKggivnRRLLNYEAREQLEHLGVDID--PDTplkyLSIGQRQMVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 189 ARAYAVDPAVLLMDEPFGALDAltrvRSQEQLLATWTRER---RTVLFVTHDVDEAVYLAGRVVVMaaRPGR 257
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSA----REIEQLFRVIRELRaegRVILYVSHRMEEIFALCDAITVF--KDGR 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-265 |
1.75e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 26 EKSREETGAPLTRTPAPDRAkISFREVSRHHPvKGGAFtaLDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL------ 99
Cdd:COG4178 343 EAADALPEAASRIETSEDGA-LALEDLTLRTP-DGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsg 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 100 --DAPSGGEVLVdgVPvrgpgpdrgvvfqQYALFPWLTVRGNVEFGLRLTRLPAAERRrradHAIGLVGLGDFADAL--- 174
Cdd:COG4178 419 riARPAGARVLF--LP-------------QRPYLPLGTLREALLYPATAEAFSDAELR----EALEAVGLGHLAERLdee 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 175 ---PRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAltrvRSQEQLLATWTRERR--TVLFVTHDVDEAVYlAGRVV 249
Cdd:COG4178 480 adwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE----ENEAALYQLLREELPgtTVISVGHRSTLAAF-HDRVL 554
|
250
....*....|....*.
gi 1154143773 250 VMAARPGRVHRVVEVP 265
Cdd:COG4178 555 ELTGDGSWQLLPAEAP 570
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
69-252 |
1.76e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP----DRGVVF-----QQYALFPWLTVRGN 139
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 VeFGLRLTRL-----PAAERRR--RADHAIGlVGLGDfADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALT 212
Cdd:PRK15439 362 V-CALTHNRRgfwikPARENAVleRYRRALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154143773 213 RVrSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:PRK15439 439 RN-DIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMH 477
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-270 |
2.33e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 82.15 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 29 REETGAPLTRTPAPDRAKISFREVS-RHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEV 107
Cdd:COG4615 310 EPAAADAAAPPAPADFQTLELRGVTyRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 108 LVDGVPVRGPGPDR-----GVVFQQYALFPwltvrgnvefglRLTRLPAAERRRRADHAIGLVGLGD---FAD-ALPRT- 177
Cdd:COG4615 390 LLDGQPVTADNREAyrqlfSAVFSDFHLFD------------RLLGLDGEADPARARELLERLELDHkvsVEDgRFSTTd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 178 LSGGMKQRCALARAYAVDPAVLLMDEpfGALDaltrvrsQ---------EQLLATWTRERRTVLFVTHDvDEAVYLAGRV 248
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDE--WAAD-------QdpefrrvfyTELLPELKARGKTVIAISHD-DRYFDLADRV 527
|
250 260
....*....|....*....|..
gi 1154143773 249 VVMAArpGRVHRVVEVPLPRPR 270
Cdd:COG4615 528 LKMDY--GKLVELTGPAALAAS 547
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
66-237 |
2.36e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.91 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVlvdgvpVRGPGPDRGVVFQQYALFPWLTVRGNVEFGLR 145
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA------RPQPGIKVGYLPQEPQLDPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 146 -----LTRLPA---------------AERRRRADHAIGLVGLGDF-------ADAL--P------RTLSGGMKQRCALAR 190
Cdd:TIGR03719 95 eikdaLDRFNEisakyaepdadfdklAAEQAELQEIIDAADAWDLdsqleiaMDALrcPpwdadvTKLSGGERRRVALCR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTrVRSQEQLLATWTrerRTVLFVTHD 237
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAES-VAWLERHLQEYP---GTVVAVTHD 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
64-250 |
3.26e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.75 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL-DAPSG----GEVLVDGVPV---RGPGPDR---GVVFQQYALFP 132
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSIfnyRDVLEFRrrvGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 wLTVRGNVEFGLRLTRL-PAAERRRRADHAIGLVGLGD-FADAL---PRTLSGGMKQRCALARAYAVDPAVLLMDEPFGA 207
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDaVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154143773 208 LDALTRVRSQEQLLAtwTRERRTVLFVTHDVDEAVYLAGRVVV 250
Cdd:PRK14271 194 LDPTTTEKIEEFIRS--LADRLTVIIVTHNLAQAARISDRAAL 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
47-251 |
4.00e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.98 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPvkGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD----RG 122
Cdd:TIGR01257 1938 LRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDvhqnMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 123 VVFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMD 202
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154143773 203 EPFGALDALTRvRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:TIGR01257 2096 EPTTGMDPQAR-RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
66-237 |
6.92e-17 |
|
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: 75.95 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGpgpdrgvVFQQyalfpwltvrgnvefglr 145
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------YFEQ------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 146 ltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVRSQEQLLATWT 225
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIEALEEALK 114
|
170
....*....|..
gi 1154143773 226 RERRTVLFVTHD 237
Cdd:cd03221 115 EYPGTVILVSHD 126
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
43-236 |
1.01e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.06 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 43 DRAK--ISFREVSRHHPVKGGAftALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRgpgpD 120
Cdd:PRK11176 336 ERAKgdIEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR----D 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 R---------GVVFQQYALFPwLTVRGNVEF--GLRLTRlPAAERRRRADHAIglvglgDFADALPR-----------TL 178
Cdd:PRK11176 410 YtlaslrnqvALVSQNVHLFN-DTIANNIAYarTEQYSR-EQIEEAARMAYAM------DFINKMDNgldtvigengvLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 179 SGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLAtwTRERRTVLFVTH 236
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE--LQKNRTSLVIAH 537
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
65-253 |
1.40e-16 |
|
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: 77.09 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVD----GVPVRGPGPDR---------GVVFQQYALF 131
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREilalrrrtiGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 PWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGD-FADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDA 210
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 211 LTR--VRsqeQLLATWTRERRTVLFVTHDVD--EAVylAGRVVVMAA 253
Cdd:COG4778 186 ANRavVV---ELIEEAKARGTAIIGIFHDEEvrEAV--ADRVVDVTP 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
69-236 |
4.23e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQY--ALFPWLTVRGNVEFglrL 146
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKADLSTLENLHF---L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 147 TRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaLTRVRSQEQLLATWTR 226
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMISAHLR 185
|
170
....*....|
gi 1154143773 227 ERRTVLFVTH 236
Cdd:PRK13543 186 GGGAALVTTH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-251 |
6.12e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 6.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL------DAPSGGEVL--------VDGVPVRgpgPDRGVVFQQYALF 131
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLyfgkdifqIDAIKLR---KEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 PWLTVRGNVEFGLRLTRLPAA-ERRRRADHAIGLVGLG----DFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFG 206
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154143773 207 ALDAltrVRSQE-QLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK14246 183 MIDI---VNSQAiEKLITELKNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
72-256 |
6.76e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 75.52 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 72 DIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVR-GPgpdrgvvfqQY--ALFPwLTVRgnvEFGLRLTR 148
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKP---------QYikADYE-GTVR---DLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 149 LPAAERRRRADHAIGLvGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRER 228
Cdd:cd03237 88 DFYTHPYFKTEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|....*...
gi 1154143773 229 RTVLFVTHDVDEAVYLAGRVVVMAARPG 256
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
58-236 |
9.49e-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: 74.67 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAFT------ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQYALF 131
Cdd:cd03290 3 VTNGYFSwgsglaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 -----PWL---TVRGNVEFGLrltrlPAAERRRRA-------DHAIGLVGLGDFADALPR--TLSGGMKQRCALARAYAV 194
Cdd:cd03290 83 yaaqkPWLlnaTVEENITFGS-----PFNKQRYKAvtdacslQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154143773 195 DPAVLLMDEPFGALDA-LTRVRSQEQLLATWTRERRTVLFVTH 236
Cdd:cd03290 158 NTNIVFLDDPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTH 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
58-285 |
9.73e-16 |
|
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: 77.15 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDA--PSGGEVLV----------------DGVPVRGPG- 118
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYhvalcekcgyverpskVGEPCPVCGg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 119 -----------PDR----------GVVFQQ-YALFPWLTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPR 176
Cdd:TIGR03269 88 tlepeevdfwnLSDklrrrirkriAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 177 TLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTH-------DVDEAVYLAGRVV 249
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpeviedLSDKAIWLENGEI 247
|
250 260 270
....*....|....*....|....*....|....*...
gi 1154143773 250 VMAARPGRVHRVV--EVPLPRpRTEELRLSREFAEVRN 285
Cdd:TIGR03269 248 KEEGTPDEVVAVFmeGVSEVE-KECEVEVGEPIIKVRN 284
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
46-258 |
4.11e-15 |
|
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: 72.91 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 46 KISFREVS-RHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR--- 121
Cdd:cd03244 2 DIEFKNVSlRYRP---NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 --GVVFQQYALFPWlTVRGNVEFglrLTRLPAAERRRradhAIGLVGLGDFADALP-----------RTLSGGMKQRCAL 188
Cdd:cd03244 79 riSIIPQDPVLFSG-TIRSNLDP---FGEYSDEELWQ----ALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154143773 189 ARAYAVDPAVLLMDEPFGALDALTRVRSQEQLlatwtRER---RTVLFVTH------DVDeavylagRVVVMAArpGRV 258
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTI-----REAfkdCTVLTIAHrldtiiDSD-------RILVLDK--GRV 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
66-253 |
6.75e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdAPSGGEVLVDGVPVRG-PGPD----RGVVFQQYALFPWLTVrgnv 140
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwSAAElarhRAYLSQQQSPPFAMPV---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 eFG-LRLtRLPAAERRRRADHAIG-LVGLGDFADALPR---TLSGGMKQRCALARAYA-VDPAV------LLMDEPFGAL 208
Cdd:COG4138 87 -FQyLAL-HQPAGASSEAVEQLLAqLAEALGLEDKLSRpltQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154143773 209 DaltrVRSQ---EQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAA 253
Cdd:COG4138 165 D----VAQQaalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-239 |
1.69e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 37 TRTPAPDRAkisfREVSRHHPVKGGA--FTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAG--LDAPSGGEVLVDGV 112
Cdd:COG2401 19 SVLDLSERV----AIVLEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 113 PVrgpGPDRGVVFQQYALFPWLTVrgnVEFglrltrlpaaerrrradhaIGLVGLGD--FADALPRTLSGGMKQRCALAR 190
Cdd:COG2401 95 QF---GREASLIDAIGRKGDFKDA---VEL-------------------LNAVGLSDavLWLRRFKELSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154143773 191 AYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVD 239
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
65-251 |
2.26e-14 |
|
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: 73.24 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPgpDRGVVFQQYALFPW--LTVRGNVEF 142
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFINYLPQepYIFSGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 143 GLRLTRLPAAERRRrADHAIGLVGLGDFADALPR-----------TLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAL 211
Cdd:TIGR01193 567 NLLLGAKENVSQDE-IWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154143773 212 TRVRSQEQLLATwtrERRTVLFVTHDVDEAvYLAGRVVVM 251
Cdd:TIGR01193 646 TEKKIVNNLLNL---QDKTIIFVAHRLSVA-KQSDKIIVL 681
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
81-237 |
2.77e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 81 VVGPSGCGKSTLLNLAAGLDAPSGGEVlvdgvpVRGPGPDRGVVFQQYALFPWLTVRGNVEFGLR-----LTRLPA---- 151
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEA------RPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAevkaaLDRFNEiyaa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 152 -----------AERRRRADHAIGLVGLGDF-------ADAL--P------RTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:PRK11819 112 yaepdadfdalAAEQGELQEIIDAADAWDLdsqleiaMDALrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
170 180 190
....*....|....*....|....*....|..
gi 1154143773 206 GALDALTrVRSQEQLLATWTrerRTVLFVTHD 237
Cdd:PRK11819 192 NHLDAES-VAWLEQFLHDYP---GTVVAVTHD 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
64-252 |
3.25e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDG-----VPVRGPGpDRGVVF--QQYALFPWLTV 136
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARA-RRGIGYlpQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNVEFGLRLTR-LPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVR 215
Cdd:PRK10895 96 YDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS-VI 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154143773 216 SQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMA 252
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVS 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
64-238 |
3.95e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRGVVFQQYA-----LFPWLtVRG 138
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSeevdwSFPVL-VED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 139 NVEFG----LRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRV 214
Cdd:PRK15056 100 VVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|....
gi 1154143773 215 RSQEqLLATWTRERRTVLFVTHDV 238
Cdd:PRK15056 180 RIIS-LLRELRDEGKTMLVSTHNL 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
66-210 |
4.08e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAG-LDAPSGGEVLVdgvpvrgpgpdRGVVfqqyALFP---WL---TVRG 138
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI-----------RGTV----AYVPqvsWIfnaTVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 139 NVEFGLRLTrlpaAERRRRA------DHAIGLVGLGDFADALPR--TLSGGMKQRCALARAYAVDPAVLLMDEPFGALDA 210
Cdd:PLN03130 698 NILFGSPFD----PERYERAidvtalQHDLDLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
61-251 |
4.14e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR------GVVFQQYALFPWL 134
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaaqlgiGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVRGNVEFGLRLTR-------LPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGA 207
Cdd:PRK09700 96 TVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 208 LDAltrvRSQEQLLATWTR---ERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK09700 176 LTN----KEVDYLFLIMNQlrkEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
59-274 |
7.19e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 59 KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKS-TLLNLAAGLDApSGGEVLVDGVPVRGP-------------------G 118
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRRsrqvielseqsaaqmrhvrG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 119 PDRGVVFQQ--YALFPWLTVRGNVEFGLRLTR-LPAAERRRRADHAIGLVGLGDFADAL---PRTLSGGMKQRCALARAY 192
Cdd:PRK10261 104 ADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 193 AVDPAVLLMDEPFGALDALTRVRSQeQLLATWTRERRT-VLFVTHDVDEAVYLAGRVVVM----AARPGRVHRVVEVPlP 267
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQIL-QLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMyqgeAVETGSVEQIFHAP-Q 261
|
....*..
gi 1154143773 268 RPRTEEL 274
Cdd:PRK10261 262 HPYTRAL 268
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
58-260 |
1.37e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.13 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAFT-------ALDRLSLDIAEGEFVAVVGPSGCGKSTLLN-LAAGLDAPSGgEVLVDGVPVRGPgpdrgvvfqQYA 129
Cdd:TIGR00957 639 VHNATFTwardlppTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEG-HVHMKGSVAYVP---------QQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 130 LFPWLTVRGNVEFGLRLTRlpaaERRRRADHAIGLvgLGDFaDALP---RT--------LSGGMKQRCALARAYAVDPAV 198
Cdd:TIGR00957 709 WIQNDSLRENILFGKALNE----KYYQQVLEACAL--LPDL-EILPsgdRTeigekgvnLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 199 LLMDEPFGALDA------LTRVRSQEQLLATWTRerrtvLFVTH------DVDEAVYLA-GRVVVMAARPGRVHR 260
Cdd:TIGR00957 782 YLFDDPLSAVDAhvgkhiFEHVIGPEGVLKNKTR-----ILVTHgisylpQVDVIIVMSgGKISEMGSYQELLQR 851
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
69-253 |
1.57e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdAPSGGEVLVDGVPVRG-PGPD----RGVVFQQ------YALFPWLTVr 137
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwSAAElarhRAYLSQQqtppfaMPVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 gnvefglrltRLPAAERRRRADHAI----GLVGLGDFadaLPR---TLSGGMKQRCALARAY-AVDPAV------LLMDE 203
Cdd:PRK03695 93 ----------HQPDKTRTEAVASALnevaEALGLDDK---LGRsvnQLSGGEWQRVRLAAVVlQVWPDInpagqlLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154143773 204 PFGALDaLTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAA 253
Cdd:PRK03695 160 PMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
66-236 |
1.63e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD---RGV-VFQQYALFPWLTVRGNVE 141
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlrQGVaMVQQDPVVLADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 142 FGLRLTrlpaaerRRRADHAIGLVGLGDFADALP-----------RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDA 210
Cdd:PRK10790 437 LGRDIS-------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180
....*....|....*....|....*.
gi 1154143773 211 LTRVRSQEQLLAtwTRERRTVLFVTH 236
Cdd:PRK10790 510 GTEQAIQQALAA--VREHTTLVVIAH 533
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
66-249 |
2.55e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDA--PSGGEVLVDGVPVRGPGPD----RGV--VFQQYALFPWLTVR 137
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDerarAGIflAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 gnvEF------GLRLTRLPAAERRRRADHAIGLVGLG-DFAD-ALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:COG0396 96 ---NFlrtalnARRGEELSAREFLKLLKEKMKELGLDeDFLDrYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154143773 210 --ALTRVRSQ-EQLLatwtRERRTVLFVTH--------DVDEA-VYLAGRVV 249
Cdd:COG0396 173 idALRIVAEGvNKLR----SPDRGILIITHyqrildyiKPDFVhVLVDGRIV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
39-251 |
2.94e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 39 TPAPDRAKISFREVSRHHPVKGGAFT-------ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDG 111
Cdd:PRK10261 306 TVVDGEPILQVRNLVTRFPLRSGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 112 -----------VPVRgpgPDRGVVFQQ-YA-LFPWLTVRGNVEFGLRLTRL-PAAERRRRADHAIGLVGL-GDFADALPR 176
Cdd:PRK10261 386 qridtlspgklQALR---RDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPH 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 177 TLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
70-258 |
3.65e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 70 SLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGP----DRGVVF-----QQYALFPWLTVRGNV 140
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdaiRAGIMLcpedrKAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 141 EFGLRLTRLPA------AERRRRADHAIGLVGLGD-FADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTR 213
Cdd:PRK11288 353 NISARRHHLRAgclinnRWEAENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154143773 214 vrsQE--QLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:PRK11288 433 ---HEiyNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM--REGRI 474
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
66-249 |
9.11e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 65.63 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDA--PSGGEVLVDGVpvrgpgpdrgvvfqqyalfpwltvrgnvefg 143
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGE------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 144 lRLTRLPAAERRRRadhAIGL----------VGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaLTR 213
Cdd:cd03217 65 -DITDLPPEERARL---GIFLafqyppeipgVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154143773 214 VRSQEQLLATWTRERRTVLFVTH-----DVDEA----VYLAGRVV 249
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHyqrllDYIKPdrvhVLYDGRIV 184
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
59-238 |
1.69e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.99 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 59 KGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGvpvrgpgpDRGVVFQQYALFPWLTVRG 138
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 139 NVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEpfgALDALTRVRSQE 218
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQK 181
|
170 180
....*....|....*....|..
gi 1154143773 219 QL--LATWTRERRTVLFVTHDV 238
Cdd:PRK13546 182 CLdkIYEFKEQNKTIFFVSHNL 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
42-269 |
2.36e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 42 PDRAKISFREVSRHHPVKGGAFTALDrLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVD------GVPVR 115
Cdd:PTZ00265 378 KDIKKIQFKNVRFHYDTRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 116 GPGPDRGVVFQQYALFPwLTVRGNVEFGL-RLTRLPAAE-----------------RRRRADHAIGL------------- 164
Cdd:PTZ00265 457 WWRSKIGVVSQDPLLFS-NSIKNNIKYSLySLKDLEALSnyynedgndsqenknkrNSCRAKCAGDLndmsnttdsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 165 --------------------VGLGDFADALP-----------RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTR 213
Cdd:PTZ00265 536 emrknyqtikdsevvdvskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 214 VRSQEQLLATWTRERRTVLFVTHDVDEAVYlAGRVVVMAARPGRVHRVVEVPLPRP 269
Cdd:PTZ00265 616 YLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
76-251 |
2.51e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 76 GEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDRG------VVFQQYALFPWLTVRGNVEFGlrLTRL 149
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiyLVPQEPLLFPNLSVKENILFG--LPKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 150 PAAERRRRAdhAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGAL-----DAL-TRVRSqeqLLAT 223
Cdd:PRK15439 115 QASMQKMKQ--LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLtpaetERLfSRIRE---LLAQ 189
|
170 180
....*....|....*....|....*...
gi 1154143773 224 WTrerrTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK15439 190 GV----GIVFISHKLPEIRQLADRISVM 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
61-257 |
4.46e-12 |
|
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: 66.00 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdAPSG---GEVLVDGVPVRGPG----PDRGVVF--QQYALF 131
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNirdtERAGIVIihQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 PWLTVRGNVEFGLRLT----RLPAAERRRRADHAIGLVGLGDFADALP-RTLSGGMKQRCALARAYAVDPAVLLMDEPFG 206
Cdd:TIGR02633 91 PELSVAENIFLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 207 ALdaltrVRSQEQLLATWTRE--RRTV--LFVTHDVDEAVYLAGRVVVMaaRPGR 257
Cdd:TIGR02633 171 SL-----TEKETEILLDIIRDlkAHGVacVYISHKLNEVKAVCDTICVI--RDGQ 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
47-210 |
5.67e-12 |
|
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: 63.42 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 47 ISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAG--LDAPSGGEVLVDGVPVRGPGPDR-GV 123
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRStGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 124 VFQQYALFPWLTVRGNVEFGLRLTRLPAAERRRRadhAIGlVGLgdfadalprtlsggmkqrcalarayAVDPAVLLMDE 203
Cdd:cd03232 84 VEQQDVHSPNLTVREALRFSALLRGLSVEQRKRL---TIG-VEL-------------------------AAKPSILFLDE 134
|
....*..
gi 1154143773 204 PFGALDA 210
Cdd:cd03232 135 PTSGLDS 141
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
44-251 |
6.54e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 44 RAKISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR-- 121
Cdd:PRK11614 3 KVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKim 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 122 ----GVVFQQYALFPWLTVRGNVEF-GLRLTRLPAAERRRRAdhaiglvglgdfADALPR----------TLSGGMKQRC 186
Cdd:PRK11614 79 reavAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWV------------YELFPRlherriqragTMSGGEQQML 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 187 ALARAYAVDPAVLLMDEPFGALDALTRVR---SQEQLlatwTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQifdTIEQL----REQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
66-252 |
8.01e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAG----LDAPSG----GEVLVDGVPVRGPGPD-----RGVVFQQYALFP 132
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAIDAPrlarlRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 WLTVRGNVEFGlrltRLPAAER--------RRRADHAIGLVGlgdfADALPR----TLSGGMKQRCALARAYA------- 193
Cdd:PRK13547 97 AFSAREIVLLG----RYPHARRagalthrdGEIAWQALALAG----ATALVGrdvtTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 194 --VDPAVLLMDEPFGALDaltrVRSQEQLLATWTRERRT----VLFVTHDVDEAVYLAGRVVVMA 252
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALD----LAHQHRLLDTVRRLARDwnlgVLAIVHDPNLAARHADRIAMLA 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
34-251 |
8.54e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 34 APLTRTPA-PDRAKISFREVSRHHPvkGGAFtALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGV 112
Cdd:PRK10522 309 AEFPRPQAfPDWQTLELRNVTFAYQ--DNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 113 PVRGPGPDR-----GVVFQQYALFPWLTVRGNVE-----FGLRLTRLPAAERRRRADHAIGLVglgdfadalprTLSGGM 182
Cdd:PRK10522 386 PVTAEQPEDyrklfSAVFTDFHLFDQLLGPEGKPanpalVEKWLERLKMAHKLELEDGRISNL-----------KLSKGQ 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 183 KQRCALARAYAVDPAVLLMDEPFGALDALTRvRSQEQLLATWTRER-RTVLFVTHDvDEAVYLAGRVVVM 251
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFR-REFYQVLLPLLQEMgKTIFAISHD-DHYFIHADRLLEM 522
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
44-212 |
1.08e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.67 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 44 RAKISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSG---GEVLVDGVPVRGPG-- 118
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 119 PDRGVVF--QQYALFPWLTVRGNVEFGLRLTrlpaaerrrradhaiglvglgdfADALPRTLSGGMKQRCALARAYAVDP 196
Cdd:cd03233 81 YPGEIIYvsEEDVHFPTLTVRETLDFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVSRA 137
|
170
....*....|....*.
gi 1154143773 197 AVLLMDEPFGALDALT 212
Cdd:cd03233 138 SVLCWDNSTRGLDSST 153
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
44-212 |
1.69e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 44 RAKISFREVSRHHPVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLN-LAAGLDAP--SGGEVLVDGVPVRGPGPD 120
Cdd:TIGR00956 757 EDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTGviTGGDRLVNGRPLDSSFQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 R-GVVFQQYALFPWLTVRGNVEFGLRLtRLPA----AERRRRADHAIGLVGLGDFADALPRTLSGGM----KQRCALARA 191
Cdd:TIGR00956 837 SiGYVQQQDLHLPTSTVRESLRFSAYL-RQPKsvskSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVE 915
|
170 180
....*....|....*....|..
gi 1154143773 192 YAVDPAVLL-MDEPFGALDALT 212
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQT 937
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
58-238 |
1.84e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVlvdgvpVRGPGPDRGVVFQQYALFPW--LT 135
Cdd:PRK09544 12 VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDTTlpLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRgnvefglRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVR 215
Cdd:PRK09544 86 VN-------RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD----VN 154
|
170 180
....*....|....*....|....*..
gi 1154143773 216 SQEQLLATWTRERRT----VLFVTHDV 238
Cdd:PRK09544 155 GQVALYDLIDQLRREldcaVLMVSHDL 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-242 |
1.97e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 8 TRDASRDRTREKTREETREKsREETG-APLTRTPAPDRAKISF--REVSRHHPVKggafTALDRLSLDIAEGEFVAVVGP 84
Cdd:PRK11147 279 TRNEGRVRALKALRRERSER-REVMGtAKMQVEEASRSGKIVFemENVNYQIDGK----QLVKDFSAQVQRGDKIALIGP 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 85 SGCGKSTLLNLAAGLDAPSGGEVLVdgvpvrgpGPDRGVV-FQQY--ALFPWLTVRGNVEFGLRLTRLPAAERrrradHA 161
Cdd:PRK11147 354 NGCGKTTLLKLMLGQLQADSGRIHC--------GTKLEVAyFDQHraELDPEKTVMDNLAEGKQEVMVNGRPR-----HV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 162 IGLvgLGDF------ADALPRTLSGGMKQRCALARAYaVDPAVLL-MDEPFGALDALTrVRSQEQLLATWTrerRTVLFV 234
Cdd:PRK11147 421 LGY--LQDFlfhpkrAMTPVKALSGGERNRLLLARLF-LKPSNLLiLDEPTNDLDVET-LELLEELLDSYQ---GTVLLV 493
|
250
....*....|.
gi 1154143773 235 THD---VDEAV 242
Cdd:PRK11147 494 SHDrqfVDNTV 504
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
65-240 |
3.37e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGvpvrgpgpDRGVVFQQYALFPWLTVRGNVEFGL 144
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------SAALIAISSGLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 145 RLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQlLATW 224
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK-MNEF 189
|
170
....*....|....*.
gi 1154143773 225 TRERRTVLFVTHDVDE 240
Cdd:PRK13545 190 KEQGKTIFFISHSLSQ 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
64-258 |
5.27e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKS-TLLNLAAGLDAPS----GGEVLVDGVPV--------RGPGPDR-GVVFQQ-- 127
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaseqtlRGVRGNKiAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 128 YALFPWLTVRGNVEFGLRLTRlpaaERRRRADHAIGL-----VGLGDFADAL---PRTLSGGMKQRCALARAYAVDPAVL 199
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHR----GMRREAARGEILncldrVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 200 LMDEPFGALDalTRVRSQ-EQLLATWTRE-RRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:PRK15134 179 IADEPTTALD--VSVQAQiLQLLRELQQElNMGLLFITHNLSIVRKLADRVAVM--QNGRC 235
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
72-256 |
5.87e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.28 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 72 DIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVrgpgpdrgVVFQQYAlfpwltvrgnvefglrltrlpa 151
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP--------VYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 152 aerrrradhaiglvglgdfadalprTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTV 231
Cdd:cd03222 71 -------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|....*
gi 1154143773 232 LFVTHDVDEAVYLAGRVVVMAARPG 256
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-237 |
5.88e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 40 PAPDRAK----ISFREVSRHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLvdgvpvR 115
Cdd:PLN03073 498 PTPDDRPgppiISFSDASFGYP---GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------R 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 116 GPGPdRGVVFQQYalfpwltvrgNVEfGLRLTRLP----------AAERRRRADhaIGLVGL-GDFADALPRTLSGGMKQ 184
Cdd:PLN03073 569 SAKV-RMAVFSQH----------HVD-GLDLSSNPllymmrcfpgVPEQKLRAH--LGSFGVtGNLALQPMYTLSGGQKS 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 185 RCALARAYAVDPAVLLMDEPFGALDaLTRVRSQEQLLATWtreRRTVLFVTHD 237
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLD-LDAVEALIQGLVLF---QGGVLMVSHD 683
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
65-212 |
7.95e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPDR------GVVFQQYALFPWLTVRG 138
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagiGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 139 NV----EFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPfgaLDALT 212
Cdd:PRK10762 99 NIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDALT 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-226 |
8.19e-11 |
|
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: 61.41 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 23 ETREKSREETGApltRTPAPDRAKISFREVSRH-HPVkggaftaLDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDA 101
Cdd:cd03291 19 ELLEKAKQENND---RKHSSDDNNLFFSNLCLVgAPV-------LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 102 PSGGEVLVDGvpvrgpgpdRGVVFQQYALFPWLTVRGNVEFGLRLTrlpaaERRRRAdhAIGLVGLGDFADALPR----- 176
Cdd:cd03291 89 PSEGKIKHSG---------RISFSSQFSWIMPGTIKENIIFGVSYD-----EYRYKS--VVKACQLEEDITKFPEkdntv 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 177 ------TLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQE----QLLATWTR 226
Cdd:cd03291 153 lgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscvcKLMANKTR 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
66-212 |
1.04e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRgpgPDRgVVFQQYALF--------PWLTVR 137
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---KDL-CTYQKQLCFvghrsginPYLTLR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 138 GNVEFGLRLTrlpaaERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALT 212
Cdd:PRK13540 93 ENCLYDIHFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
66-226 |
1.15e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGpdrgvvfqqyalFPWL---TVRGNVEF 142
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWImpgTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 143 GLR------------------LTRLPAAERRRRADHAIglvglgdfadalprTLSGGMKQRCALARAYAVDPAVLLMDEP 204
Cdd:TIGR01271 510 GLSydeyrytsvikacqleedIALFPEKDKTVLGEGGI--------------TLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180
....*....|....*....|....*.
gi 1154143773 205 FGALDALTRVRSQE----QLLATWTR 226
Cdd:TIGR01271 576 FTHLDVVTEKEIFEsclcKLMSNKTR 601
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
76-240 |
3.53e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 76 GEFVAVVGPSGCGKSTLLNLAAG-LDAPSGGEVLVDGvpvrgpgpdrgvvfqqyalfpwltvrgnvefglrlTRLPAAER 154
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG-----------------------------------EDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 155 RRRADHAIGLVGLGdfadalprtLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQE-----QLLATWTRERR 229
Cdd:smart00382 47 DQLLLIIVGGKKAS---------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKSEKNL 117
|
170
....*....|.
gi 1154143773 230 TVLFVTHDVDE 240
Cdd:smart00382 118 TVILTTNDEKD 128
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
64-236 |
4.46e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.11 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 64 TALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRGPGPD--RG---VVFQQYALFPwLTVRG 138
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSrlaVVSQTPFLFS-DTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 139 NVEFGLrltrlPAAERRRrADHAIGLVGLGDFADALPR-----------TLSGGMKQRCALARAYAVDPAVLLMDEPFGA 207
Cdd:PRK10789 408 NIALGR-----PDATQQE-IEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190
....*....|....*....|....*....|..
gi 1154143773 208 LDAltrvRSQEQL---LATWtRERRTVLFVTH 236
Cdd:PRK10789 482 VDG----RTEHQIlhnLRQW-GEGRTVIISAH 508
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
61-257 |
8.84e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdAPSG---GEVLVDGVPVRGPG----PDRGVV--FQQYALF 131
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQASNirdtERAGIAiiHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 132 PWLTVRGNVEFGLRLT---RLPAAERRRRADHAIGLVGLgDFADALP-RTLSGGMKQRCALARAYAVDPAVLLMDEPFGA 207
Cdd:PRK13549 95 KELSVLENIFLGNEITpggIMDYDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 208 LDAltrvrSQEQLLATWTRERR----TVLFVTHDVDEAVYLAGRVVVMaaRPGR 257
Cdd:PRK13549 174 LTE-----SETAVLLDIIRDLKahgiACIYISHKLNEVKAISDTICVI--RDGR 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
39-258 |
1.30e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 39 TPAPDRAKISFREVSRHHPVKGGAFTALD------RLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDgv 112
Cdd:PTZ00243 643 TGGGHEATPTSERSAKTPKMKTDDFFELEpkvllrDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 113 pvrgpgpdRGVVF--QQyalfPWL---TVRGNVEF--GLRLTRLPAAER--RRRADHAIGLVGLGDFADALPRTLSGGMK 183
Cdd:PTZ00243 721 --------RSIAYvpQQ----AWImnaTVRGNILFfdEEDAARLADAVRvsQLEADLAQLGGGLETEIGEKGVNLSGGQK 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 184 QRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLfVTHDVdEAVYLAGRVVVMAArpGRV 258
Cdd:PTZ00243 789 ARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVL-ATHQV-HVVPRADYVVALGD--GRV 859
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
66-236 |
1.62e-09 |
|
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: 56.01 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGL--------DAPSGGEVLVdgVPVR---GPGPDRGVVfqqyaLFPWL 134
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGEDLLF--LPQRpylPLGTLREQL-----IYPWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 135 TVrgnvefglrltrlpaaerrrradhaiglvglgdfadalprtLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrV 214
Cdd:cd03223 90 DV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----E 124
|
170 180
....*....|....*....|..
gi 1154143773 215 RSQEQLLATWTRERRTVLFVTH 236
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH 146
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
61-257 |
2.65e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSG---GEVLVDG-----VPVRGPGPDRG----VVFQQ- 127
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGreilnLPEKELNKLRAeqisMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 128 -YALFPWLTVRGNVEFGLRL-------------------TRLPAAERRRRAdhaiglvglgdfadaLPRTLSGGMKQRCA 187
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLhkgmskaeafeesvrmldaVKMPEARKRMKM---------------YPHEFSGGMRQRVM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 188 LARAYAVDPAVLLMDEPFGALDaltrVRSQEQ---LLATWTRERRT-VLFVTHDVDEAVYLAGRVVVMAArpGR 257
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALD----VTVQAQimtLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYA--GR 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
66-210 |
3.15e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAG-LDAPSGGEVLVDGVPVRGPGpdrgvvfqqyalFPWL---TVRGNVE 141
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAYVPQ------------VSWIfnaTVRENIL 700
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154143773 142 FGLRLTrlpaAERRRRA------DHAIGLVGLGDFADALPR--TLSGGMKQRCALARAYAVDPAVLLMDEPFGALDA 210
Cdd:PLN03232 701 FGSDFE----SERYWRAidvtalQHDLDLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
44-251 |
4.55e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 44 RAKISFREVSRHHpvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLnLAAGLDAPSGGE--------VLVDGVPVR 115
Cdd:NF000106 11 RNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrpwrf*twCANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 116 GPGPDRGVVFQQYALFpwlTVRGNVEFGLRLTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVD 195
Cdd:NF000106 86 TIG*HRPVR*GRRESF---SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 196 PAVLLMDEPFGALDALTRVRSQEQlLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATVLLTTQYMEEAEQLAHELTVI 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
65-208 |
4.86e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdAPSG---GEVLVDGVPVRGPG----PDRGVVF--QQYALFPWLT 135
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGEVCRFKDirdsEALGIVIihQELALIPYLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 136 VRGNVEFGLRLTRLPAAERRRRADHAIGL---VGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGAL 208
Cdd:NF040905 95 IAENIFLGNERAKRGVIDWNETNRRARELlakVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
50-251 |
6.67e-09 |
|
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: 56.37 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 50 REVSRHHPVKGgAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLN-LAAGLDAPSGGEVLVDGVPVRGPGPDR----GVV 124
Cdd:TIGR02633 261 RNLTCWDVINP-HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQairaGIA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 125 F-----QQYALFPWLTVRGNVEFGL-----RLTRLPAAERRRRADHAIGLVGLGDFADALPRT-LSGGMKQRCALARAYA 193
Cdd:TIGR02633 340 MvpedrKRHGIVPILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGrLSGGNQQKAVLAKMLL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 194 VDPAVLLMDEPFGALDALTRVRSQeQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:TIGR02633 420 TNPRVLILDEPTRGVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-241 |
1.01e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 31 ETGAPLTRTP-APDRAKISFREVSrhhpVKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGlDAPSG--GEV 107
Cdd:PRK10938 244 EPDEPSARHAlPANEPRIVLNNGV----VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysNDL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 108 LVDGVPvRGPGP-------DRGVVFQQYALFPWL--TVRGNVEFG----LRLTRLPAAERRRRADHAIGLVGLGD-FADA 173
Cdd:PRK10938 319 TLFGRR-RGSGEtiwdikkHIGYVSSSLHLDYRVstSVRNVILSGffdsIGIYQAVSDRQQKLAQQWLDILGIDKrTADA 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 174 LPRTLSGGmKQRCAL-ARAYAVDPAVLLMDEPFGALDALTR--VRS-QEQLLAtwtrERRT-VLFVTHDVDEA 241
Cdd:PRK10938 398 PFHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNRqlVRRfVDVLIS----EGETqLLFVSHHAEDA 465
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-251 |
1.12e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 22 EETREKSREETGAPL----TRTPA--PDRAKISFREVS-RHHPvkgGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLN 94
Cdd:TIGR00957 1254 ERLKEYSETEKEAPWqiqeTAPPSgwPPRGRVEFRNYClRYRE---DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTL 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 95 LAAGLDAPSGGEVLVDGVPVRGPGPDR-----GVVFQQYALFPWlTVRGNVE-FGlrltrlpaaerrRRADH----AIGL 164
Cdd:TIGR00957 1331 GLFRINESAEGEIIIDGLNIAKIGLHDlrfkiTIIPQDPVLFSG-SLRMNLDpFS------------QYSDEevwwALEL 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 165 VGLGDFADALP-----------RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrvrsqEQLLATWTR---ERRT 230
Cdd:TIGR00957 1398 AHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET-----DNLIQSTIRtqfEDCT 1472
|
250 260
....*....|....*....|.
gi 1154143773 231 VLFVTHDVDeAVYLAGRVVVM 251
Cdd:TIGR00957 1473 VLTIAHRLN-TIMDYTRVIVL 1492
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
66-237 |
1.75e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGldapsggEVLVDgvpvrgpgpDRGVVFQQYALF------PWLTVRGN 139
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-------EVLLD---------DGRIIYEQDLIVarlqqdPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 V-EF---GL-----------RLTRLPAAERRRRA-----------DHAIG----------LVGLGDFADALPRTLSGGMK 183
Cdd:PRK11147 83 VyDFvaeGIeeqaeylkryhDISHLVETDPSEKNlnelaklqeqlDHHNLwqlenrinevLAQLGLDPDAALSSLSGGWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 184 QRCALARAYAVDPAVLLMDEPFGALDALTrVRSQEQLLATWtreRRTVLFVTHD 237
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIET-IEWLEGFLKTF---QGSIIFISHD 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
75-256 |
4.97e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 75 EGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVlvdgvpvrGPGPDRGVVFQQYA---LFPWLT---------------- 135
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRgteLQDYFKklangeikvahkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 ------VRGNVEfglrlTRLPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:COG1245 170 dlipkvFKGTVR-----ELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154143773 210 ALTRVRSQeQLLATWTRERRTVLFVTHDVdeAV--YLAGRVVVMAARPG 256
Cdd:COG1245 245 IYQRLNVA-RLIRELAEEGKYVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
74-265 |
6.27e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 74 AEGEFVAVVGPSGCGKSTLLNLAAGL---------DAPSGGEVLVDgvpVRGP-----------GPDRGVVFQQYA-LFP 132
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKlkpnlgkfdDPPDWDEILDE---FRGSelqnyftklleGDVKVIVKPQYVdLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 133 wLTVRGNVefGLRLTRlpaAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALT 212
Cdd:cd03236 101 -KAVKGKV--GELLKK---KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 213 RVrSQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPGrVHRVVEVP 265
Cdd:cd03236 175 RL-NAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG-AYGVVTLP 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
66-221 |
6.70e-08 |
|
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: 53.40 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVdgvpvrGPGPDRGVVFQQY-ALFPWLTVRGNVEFGL 144
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYVDQSRdALDPNKTVWEEISGGL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 145 RLTRLPAAERRRRAdhaigLVGLGDF--ADALPRT--LSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTrVRSQEQL 220
Cdd:TIGR03719 412 DIIKLGKREIPSRA-----YVGRFNFkgSDQQKKVgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET-LRALEEA 485
|
.
gi 1154143773 221 L 221
Cdd:TIGR03719 486 L 486
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
61-274 |
1.28e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 52.22 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPS----------GGEVLVDGVPV---RGPGPDRGVVFQ- 126
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLKLSPRerrKIIGREIAMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 127 -QYALFPWLTVRGNVEFGLRLTRLPAAERRR---RADHAIGL---VGLGDFAD---ALPRTLSGGMKQRCALARAYAVDP 196
Cdd:COG4170 98 pSSCLDPSAKIGDQLIEAIPSWTFKGKWWQRfkwRKKRAIELlhrVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 197 AVLLMDEPFGALDALTrvrsQEQ---LLATWTRERRT-VLFVTHDVDEAVYLAGRVVVM----AARPGRVHRVVEVPLpR 268
Cdd:COG4170 178 RLLIADEPTNAMESTT----QAQifrLLARLNQLQGTsILLISHDLESISQWADTITVLycgqTVESGPTEQILKSPH-H 252
|
....*.
gi 1154143773 269 PRTEEL 274
Cdd:COG4170 253 PYTKAL 258
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
105-238 |
2.43e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 105 GEVLVDGVPV-----RGPGPDRGVVFQQYALFPwLTVRGNVEFGLRLTRLPAAERrrradhAIGLVGLGDFADALP---- 175
Cdd:PTZ00265 1277 GKILLDGVDIcdynlKDLRNLFSIVSQEPMLFN-MSIYENIKFGKEDATREDVKR------ACKFAAIDEFIESLPnkyd 1349
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 176 -------RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDALTRVRSQEQLLATWTRERRTVLFVTHDV 238
Cdd:PTZ00265 1350 tnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
60-251 |
5.01e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 60 GGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAP----SGGEVLVDGVPV---------RGPGPDRGVVFQ 126
Cdd:PRK15093 17 DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLlrlsprerrKLVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 127 --QYALFPWLTVrgnvefGLRLTR-LPAAE-----------RRRRADHAIGLVGLGDFADAL---PRTLSGGMKQRCALA 189
Cdd:PRK15093 97 epQSCLDPSERV------GRQLMQnIPGWTykgrwwqrfgwRKRRAIELLHRVGIKDHKDAMrsfPYELTEGECQKVMIA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 190 RAYAVDPAVLLMDEPFGALDALTrvrsQEQLLATWTR----ERRTVLFVTHDVDEAVYLAGRVVVM 251
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTT----QAQIFRLLTRlnqnNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
75-256 |
5.83e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 75 EGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEvlvdgvPVRGPGPD------RGVVFQQYalFPWLT------------- 135
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD------YEEEPSWDevlkrfRGTELQNY--FKKLYngeikvvhkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 ------VRGNVEFGLRltrlpAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:PRK13409 170 dlipkvFKGKVRELLK-----KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154143773 210 ALTRVRS----QEqlLAtwtrERRTVLFVTHDVdeAV--YLAGRVVVMAARPG 256
Cdd:PRK13409 245 IRQRLNVarliRE--LA----EGKYVLVVEHDL--AVldYLADNVHIAYGEPG 289
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
83-203 |
5.90e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 83 GPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVRG-PGPDRGVVFQQYALFPWLTVRGNVEFGLRL----TRLPAaerrrr 157
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSEIynsaETLYA------ 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1154143773 158 adhAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDE 203
Cdd:PRK13541 107 ---AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
76-210 |
5.96e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 76 GEFVAVVGPSGCGKSTLLNLAAGldAPSGG----EVLVDGVPVRGPGPDR--GVVFQQYALFPWLTVRGNVEFGLRLtRL 149
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGyiegDIRISGFPKKQETFARisGYCEQNDIHSPQVTVRESLIYSAFL-RL 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 150 PAA----ERRRRADHAIGLVGLGDFADA---LPRT--LSGGMKQRCALARAYAVDPAVLLMDEPFGALDA 210
Cdd:PLN03140 983 PKEvskeEKMMFVDEVMELVELDNLKDAivgLPGVtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
66-258 |
8.36e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPV--RGP--GPDRGVVF-----QQYALFPWLTV 136
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPqdGLANGIVYisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 137 RGNvefgLRLTRLPAAERRR-RADHAIGLVGLGDF----------ADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPF 205
Cdd:PRK10762 348 KEN----MSLTALRYFSRAGgSLKHADEQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 206 GALDaltrVRSQE---QLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMaaRPGRV 258
Cdd:PRK10762 424 RGVD----VGAKKeiyQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM--HEGRI 473
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
61-212 |
1.58e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEV-LVDGVPVRgpgpdrgvVFQQYALfpwltvrgn 139
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLG--------YFAQHQL--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 vEFgLR--------LTRLPAAERRRRADHAIGLVGL-GDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD- 209
Cdd:PRK10636 386 -EF-LRadesplqhLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDl 463
|
....*..
gi 1154143773 210 ----ALT 212
Cdd:PRK10636 464 dmrqALT 470
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
73-257 |
1.71e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 73 IAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDgvpVRgpgpdrgVVFQ-QYaLFPwlTVRGNVEFGLRLTRLPA 151
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LK-------ISYKpQY-IKP--DYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 152 AERRRRADHAIGLvGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDAltrvrsqEQLLAT------WT 225
Cdd:PRK13409 429 GSSYYKSEIIKPL-QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV-------EQRLAVakairrIA 500
|
170 180 190
....*....|....*....|....*....|...
gi 1154143773 226 RERR-TVLFVTHDVDEAVYLAGRVVVMAARPGR 257
Cdd:PRK13409 501 EEREaTALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
72-267 |
2.92e-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: 48.63 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 72 DIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDgvpVRgpgpdrgVVFQ-QY--ALFPwltvrGNVEFGLRLTR 148
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LK-------ISYKpQYisPDYD-----GTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 149 LPAAERRRRADHAIGLVGLGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrvrSQEQLLAT----- 223
Cdd:COG1245 427 TDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD------VEQRLAVAkairr 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154143773 224 WTRER-RTVLFVTHDV---DeavYLAGRVVVMAARPGrVHRVVEVPLP 267
Cdd:COG1245 501 FAENRgKTAMVVDHDIyliD---YISDRLMVFEGEPG-VHGHASGPMD 544
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
58-237 |
3.05e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 58 VKGGAF-TALDRLSLDIAEGEFVAVVGPSGCGKSTLLN---LAAGLDAPSGGevlvdgvpvRGPGPDRGVVfqqyalfpw 133
Cdd:cd03227 2 IVLGRFpSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATR---------RRSGVKAGCI--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 134 ltvRGNVEFGLRLTRLpaaerrrradhaiglvglgdfadalprTLSGGMKQRCALA-----RAYAVDPAVLLmDEPFGAL 208
Cdd:cd03227 64 ---VAAVSAELIFTRL---------------------------QLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGL 112
|
170 180 190
....*....|....*....|....*....|...
gi 1154143773 209 DALTRVRsqeqlLATWTRERR----TVLFVTHD 237
Cdd:cd03227 113 DPRDGQA-----LAEAILEHLvkgaQVIVITHL 140
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
61-212 |
6.26e-06 |
|
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: 46.77 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 61 GAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdAPSGGEVLVDGV-----PVRGPGPDRGVVFQQYALFPWlT 135
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVswnsvPLQKWRKAFGVIPQKVFIFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNVE-FGlrltRLPAAERRRRADHaiglVGLGDFADALPR-----------TLSGGMKQRCALARAYAVDPAVLLMDE 203
Cdd:cd03289 93 FRKNLDpYG----KWSDEEIWKVAEE----VGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
....*....
gi 1154143773 204 PFGALDALT 212
Cdd:cd03289 165 PSAHLDPIT 173
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
69-249 |
9.32e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEV-LVDGVPVRGPGPDRGVVFQQ-YALFPWLT----------- 135
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDHAYDFENdLTLFDWMSqwrqegddeqa 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 136 VRGNvefglrLTRLpaaerrrradhaigLVGlGDFADALPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVR 215
Cdd:PRK15064 418 VRGT------LGRL--------------LFS-QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD----ME 472
|
170 180 190
....*....|....*....|....*....|....
gi 1154143773 216 SQEQLLATWTRERRTVLFVTHDVDEAVYLAGRVV 249
Cdd:PRK15064 473 SIESLNMALEKYEGTLIFVSHDREFVSSLATRII 506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
45-251 |
1.50e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 45 AKISFREVSRHHPVKggAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAA----GLDAPSGGEVLVDGVPvrgpgPD 120
Cdd:TIGR00956 58 LTRGFRKLKKFRDTK--TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT-----PE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 121 ------RGVVF---QQYALFPWLTVRGNVEFGLRLtRLPA---------AERRRRADHAIGLVGL---------GDFAda 173
Cdd:TIGR00956 131 eikkhyRGDVVynaETDVHFPHLTVGETLDFAARC-KTPQnrpdgvsreEYAKHIADVYMATYGLshtrntkvgNDFV-- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 174 lpRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALD---ALTRVRSqeqlLATWTRERRTVLFVT--HDVDEAVYLAGRV 248
Cdd:TIGR00956 208 --RGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDsatALEFIRA----LKTSANILDTTPLVAiyQCSQDAYELFDKV 281
|
...
gi 1154143773 249 VVM 251
Cdd:TIGR00956 282 IVL 284
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-251 |
1.69e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 34 APLT----RTPA--PDRAKISFREVSRHH-----PVkggaftaLDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAP 102
Cdd:PLN03130 1219 APLViennRPPPgwPSSGSIKFEDVVLRYrpelpPV-------LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 103 SGGEVLVDGVPVRGPG-----PDRGVVFQQYALFPWlTVRGNVE-FG----------LRLTRLPAAERRrradHAIGLVg 166
Cdd:PLN03130 1292 ERGRILIDGCDISKFGlmdlrKVLGIIPQAPVLFSG-TVRFNLDpFNehndadlwesLERAHLKDVIRR----NSLGLD- 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 167 lGDFADAlPRTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaltrVRSQEQLLATWTRERR--TVLFVTH------DV 238
Cdd:PLN03130 1366 -AEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEATAAVD----VRTDALIQKTIREEFKscTMLIIAHrlntiiDC 1439
|
250
....*....|....
gi 1154143773 239 DEAVYL-AGRVVVM 251
Cdd:PLN03130 1440 DRILVLdAGRVVEF 1453
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
176-236 |
1.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154143773 176 RTLSGGMKQRCALARAYAVDPAVLLMDEPFGALDaLTRVRSQEQLLATWTrerRTVLFVTH 236
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-LHAVLWLETYLLKWP---KTFIVVSH 399
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
68-203 |
2.09e-05 |
|
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: 45.90 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 68 RLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLdapsggevlvdgVPVRGP---GPDRGVVF--QQYALFPWLTVRGNV-- 140
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGEL------------WPVYGGrltKPAKGKLFyvPQRPYMTLGTLRDQIiy 537
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154143773 141 --------EFGLRLTRLPAAERRRRADHAI----GLVGLGDFADalprTLSGGMKQRCALARAYAVDPAVLLMDE 203
Cdd:TIGR00954 538 pdssedmkRRGLSDKDLEQILDNVQLTHILeregGWSAVQDWMD----VLSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
66-239 |
2.17e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDG------VPVRGPGPDRGVVfqQYalfpwlTVRGN 139
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawVNQETPALPQPAL--EY------VIDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 VEFGLRLTRLPAAERRRRAdHAIGLV---------------------GLGDFADALPR---TLSGGMKQRCALARAYAVD 195
Cdd:PRK10636 89 REYRQLEAQLHDANERNDG-HAIATIhgkldaidawtirsraasllhGLGFSNEQLERpvsDFSGGWRMRLNLAQALICR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154143773 196 PAVLLMDEPFGALDaLTRVRSQEQLLATWTrerRTVLFVTHDVD 239
Cdd:PRK10636 168 SDLLLLDEPTNHLD-LDAVIWLEKWLKSYQ---GTLILISHDRD 207
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
63-256 |
4.57e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.80 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 63 FTALDrlsldiaEGEFVAVVGPSGCGKSTLLnlaaglDAPS---GGEVLVDGVPVrgpgpDRGVVFQQYALFPWLTVrgn 139
Cdd:cd03279 22 FTGLD-------NNGLFLICGPTGAGKSTIL------DAITyalYGKTPRYGRQE-----NLRSVFAPGEDTAEVSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 140 vEFGLRlTRLPAAERRRRADH----AIGLVGLGDFADALPR---TLSGGMKQRCALARAYAVDPAV----------LLMD 202
Cdd:cd03279 81 -TFQLG-GKKYRVERSRGLDYdqftRIVLLPQGEFDRFLARpvsTLSGGETFLASLSLALALSEVLqnrggarleaLFID 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154143773 203 EPFGALD--ALTRVrsqEQLLATWTRERRTVLFVTHDVDEAVYLAGRVVVMAARPG 256
Cdd:cd03279 159 EGFGTLDpeALEAV---ATALELIRTENRMVGVISHVEELKERIPQRLEVIKTPGG 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
65-208 |
4.60e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 65 ALDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLVDGVPVR----GPGPDRGV--VFQQYALFPWLTVRG 138
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkssKEALENGIsmVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154143773 139 NVEFGLRLTRLPAAERRRRADHAIGLVGLGDFaDALPR----TLSGGMKQRCALARAYAVDPAVLLMDEPFGAL 208
Cdd:PRK10982 93 NMWLGRYPTKGMFVDQDKMYRDTKAIFDELDI-DIDPRakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
66-236 |
1.30e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLD--APSGGEVLVDGVPVRGPGP-DRG-----VVFQQYALFPWLTVR 137
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPeDRAgegifMAFQYPVEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 138 gnveFGLRlTRLPAAeRRRRADHAIGLVGLGDF-----------ADALPRTL----SGGMKQRCALARAYAVDPAVLLMD 202
Cdd:PRK09580 97 ----FFLQ-TALNAV-RSYRGQEPLDRFDFQDLmeekiallkmpEDLLTRSVnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154143773 203 EPFGAL--DALTRVrsqEQLLATWTRERRTVLFVTH 236
Cdd:PRK09580 171 ESDSGLdiDALKIV---ADGVNSLRDGKRSFIIVTH 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
67-109 |
1.80e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1154143773 67 DRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPSGGEVLV 109
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
66-237 |
7.52e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 66 LDRLSL-------DIAEGEF----VAVVGPSGCGKSTL---LNLA-AGLDAPSGgevlvdgvpvRGPGPDRGVVFQQyal 130
Cdd:cd03240 1 IDKLSIrnirsfhERSEIEFfsplTLIVGQNGAGKTTIieaLKYAlTGELPPNS----------KGGAHDPKLIREG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 131 fpwlTVRGNVEFGLRLT--RLPAAERRRRA-DHAIgLVGLGDFADALPR---TLSGGMKQ------RCALARAYAVDPAV 198
Cdd:cd03240 68 ----EVRAQVKLAFENAngKKYTITRSLAIlENVI-FCHQGESNWPLLDmrgRCSGGEKVlasliiRLALAETFGSNCGI 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154143773 199 LLMDEPFGALDAlTRVRSQeqlLATWTRERRT-----VLFVTHD 237
Cdd:cd03240 143 LALDEPTTNLDE-ENIEES---LAEIIEERKSqknfqLIVITHD 182
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
73-252 |
7.68e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.28 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 73 IAEGEFVAVVGPSGCGKSTL----LNLAAGLDapsgGEVLVDGV-----PVRGPGPDRGVVFQQYALFpwltvRGNVEFG 143
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIdisklPLHTLRSRLSIILQDPILF-----SGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 144 LRltrlpaAERRRRAD---HAIGLVGLGDFADALPRTL-----------SGGMKQRCALARAYAVDPAVLLMDEPFGALD 209
Cdd:cd03288 115 LD------PECKCTDDrlwEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154143773 210 ALTRVRSQEQLLATWTreRRTVLFVTHDVdEAVYLAGRVVVMA 252
Cdd:cd03288 189 MATENILQKVVMTAFA--DRTVVTIAHRV-STILDADLVLVLS 228
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
65-101 |
2.84e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.62 E-value: 2.84e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1154143773 65 ALDRLSLDIAEGE-FVAVVGPSGCGKSTLLN-LAAGLDA 101
Cdd:COG3267 31 ALARLEYALAQGGgFVVLTGEVGTGKTTLLRrLLERLPD 69
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
66-111 |
3.34e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.47 E-value: 3.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLNLAAGLDAPS--GGEVLVDG 111
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKG 70
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
58-100 |
5.16e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 5.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1154143773 58 VKGGAFTALDRLSLDIAEGEFVAVVGPSGCGKSTLLN--LAAGLD 100
Cdd:TIGR00630 616 LKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALA 660
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
187-277 |
5.92e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 37.68 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 187 ALARAYAvdPAVLLMDEpfgaLDALTRVRSQEQllaTWTRERRTVlfvthdvdeAVYLA--------GRVVVMAA----- 253
Cdd:COG1222 165 ELAREKA--PSIIFIDE----IDAIAARRTDDG---TSGEVQRTV---------NQLLAeldgfesrGDVLIIAAtnrpd 226
|
90 100 110
....*....|....*....|....*....|.
gi 1154143773 254 -------RPGRVHRVVEVPLPrprTEELRLS 277
Cdd:COG1222 227 lldpallRPGRFDRVIEVPLP---DEEAREE 254
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
66-94 |
7.94e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.21 E-value: 7.94e-03
10 20
....*....|....*....|....*....
gi 1154143773 66 LDRLSLDIAEGEFVAVVGPSGCGKSTLLN 94
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
67-204 |
9.22e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.60 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154143773 67 DRLSLDIAEGEFVAVVGPSGCGKSTLLN-LAAGLDAPSGGEVLVDGVPVRGPGP----DRGVVF-----QQYALFPWLTV 136
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPqqaiAQGIAMvpedrKRDGIVPVMGV 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154143773 137 RGNVEfglrLTRLPAAERRRRADHAIGLVGLGDFADALP-RT---------LSGGMKQRCALARAYAVDPAVLLMDEP 204
Cdd:PRK13549 359 GKNIT----LAALDRFTGGSRIDDAAELKTILESIQRLKvKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
69-94 |
9.45e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 9.45e-03
10 20
....*....|....*....|....*.
gi 1154143773 69 LSLDIAEGEFVAVVGPSGCGKSTLLN 94
Cdd:PRK00349 628 VDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| |
