|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-247 |
3.25e-107 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 310.10 E-value: 3.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHY----DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----TETKHHPVG 74
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 155 EPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTLTERIVPLDHNRTRKDLYKPEVLA 234
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPEFAA 243
|
250
....*....|...
gi 447179532 235 LKDELLSMLQRQV 247
Cdd:COG1116 244 LRAEILDLLREEA 256
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-218 |
1.12e-104 |
|
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: 302.08 E-value: 1.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETK----HHPVGYMPQ 78
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvtgpGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 159 ALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTLTERIVPL 218
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-246 |
1.44e-68 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 212.03 E-value: 1.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPV-------GY 75
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL---DGVPVtgpgadrGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 156 PFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPittltERIV---PLDHNR-------TRK 225
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP-----GRIVerlELDFSRrflagedARA 235
|
250 260
....*....|....*....|.
gi 447179532 226 DLYKPEVLALKDELLSMLQRQ 246
Cdd:COG4525 236 IKSDPAFIALREELLDIIFAQ 256
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-206 |
3.87e-62 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 198.40 E-value: 3.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-----TETKHH--PVGY 75
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvTGLPPEkrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 156 PFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV-----VEQQ 206
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVmndgrIEQV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-208 |
1.36e-60 |
|
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: 190.04 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-----TETKHH--PVGYMPQK 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvTGVPPErrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-248 |
1.71e-55 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 178.35 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETkhhPV-------GYMPQ 78
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVegpgaerGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 159 ALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPiTTLTERIvPLDHNR-------TRKDLYKPE 231
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGP-GRVVERL-PLNFARrfvagesSRSIKSDPQ 235
|
250
....*....|....*....
gi 447179532 232 VLALKDELLSML--QRQVL 248
Cdd:PRK11248 236 FIAMREYVLSRVfeQREAF 254
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-205 |
7.03e-55 |
|
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: 177.07 E-value: 7.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 22 IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTETKHHPVGYMPQKDMLLPWRTI 88
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaamsrkELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 89 IENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASL 168
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190
....*....|....*....|....*....|....*..
gi 447179532 169 QEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-205 |
9.11e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 179.19 E-value: 9.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----TETKHHP----VGYMPQ 78
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdLFTNLPPrerrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 159 ALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ 209
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-200 |
3.41e-54 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 178.76 E-value: 3.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 10 HNVSFhydekpiihelnaSIHEKE-FVsIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYMPQKDM------- 81
Cdd:COG4175 44 NDASF-------------DVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPTAGEVLI---DGEDITKLSKKELrelrrkk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 ---------LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:COG4175 107 msmvfqhfaLLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRV 200
Cdd:COG4175 187 MDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRI 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-243 |
1.29e-52 |
|
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: 170.34 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 22 IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVG----YMPQKDMLLPWRTIIENAALPLE 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpdrmVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 98 C--QGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQ 175
Cdd:TIGR01184 81 RvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 176 WQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTLTERI-VPLDHNRTRKDLYK-PEVLALKDELLSML 243
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILeVPFPRPRDRLEVVEdPSYYDLRNEALYFL 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-205 |
7.34e-51 |
|
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: 164.95 E-value: 7.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 8 QFHNVSFHYD--EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP-------VGYM 76
Cdd:cd03225 1 ELKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgKDLTKLSlkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQ--KDMLLPwRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:cd03225 81 FQnpDDQFFG-PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 155 EPFSALDALTKASLQEWLfEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03225 160 EPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-208 |
2.09e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.88 E-value: 2.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----TETKHHPVGYM 76
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLlpwrtiieNAALPLECQGV--------------QKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIR 142
Cdd:COG1121 81 PQRAEV--------DWDFPITVRDVvlmgrygrrglfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 143 TLLTGGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-205 |
7.75e-50 |
|
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: 162.66 E-value: 7.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTETK 69
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 HHPVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 150 ILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEAlFLSNRVLVVEQ 205
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRD 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-202 |
2.76e-49 |
|
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: 161.64 E-value: 2.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHH--PVGYMPQK 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkDITNLPPHkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAV 203
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-204 |
8.86e-49 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.21 E-value: 8.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYD----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELT 66
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 67 ETKHHPVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLT 146
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 147 GGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDvEEALFLSNRVLVVE 204
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLR 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-205 |
1.49e-48 |
|
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: 158.12 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-----------TETKHHPVGY 75
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPWRTIIENAALPLecqgvqkkeaqvkakellykfglqgyetkhpkdlSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447179532 156 PFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-205 |
1.94e-48 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 159.77 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL-----EKVSIGKIELTETKhhPV------G 74
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLieptsGEIFIDGEDIREQD--PVelrrkiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGL--QGYETKHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-205 |
5.88e-48 |
|
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: 158.26 E-value: 5.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP-------VGYM 76
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgKDITKKNlrelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQ--KDMLL-PwrTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:COG1122 81 FQnpDDQLFaP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447179532 154 DEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG1122 159 DEPTAGLDPRGRRELLE-LLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-215 |
6.44e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 6.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL---------TETKHHpVGYMP 77
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpAEVRRR-IGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 158 SALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLV------VEQQPITTLTERI 215
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIidkgriVADGTPDELKARL 222
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-202 |
8.66e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 159.87 E-value: 8.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 8 QFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHPV-------GYMP 77
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIdgEDIRDLDPvelrrriGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGL--QGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 156 PFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAV 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-205 |
2.70e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTE---TKHHP------VGYMP 77
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplSAMPPpewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLlpWR-TIIENAALPLecQGVQKKEAQVKAKELLYKFGLQ-GYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:COG4619 81 QEPAL--WGgTVRDNLPFPF--QLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447179532 156 PFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-205 |
6.35e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 156.39 E-value: 6.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-------TETKHHPVGYMPQK 79
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV-----VEQ 205
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVmndgrIQQ 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-208 |
2.11e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 151.15 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 8 QFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----TETKHHPVGYMPQKDmLL 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpLEKERKRIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWR---TIIENAALPLE-----CQGVQKKEAQvKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:cd03235 80 DRDfpiSVRDVVLMGLYghkglFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447179532 156 PFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:cd03235 159 PFAGVDPKTQEDIYE-LLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-205 |
3.61e-45 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 151.34 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTE---TKHHP----VGYMPQK 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedaTDVPVqernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKK--EAQVKAK--ELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRSERppEAEIRAKvhELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447179532 156 PFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-205 |
1.44e-44 |
|
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: 149.58 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEK----PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI------------ELTETK 69
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 HHPVGYMPQKDM--LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYET---KHPKDLSGGMRQRVSFIRTL 144
Cdd:cd03257 81 RKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 145 LTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQ 205
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVmyagkiVEE 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-208 |
3.34e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 149.44 E-value: 3.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHHpVGYMPQKDM 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaPLAEARED-TRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 LLPWRTIIENAALPLecqgvqKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:PRK11247 92 LLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 162 ALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-207 |
4.44e-44 |
|
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: 155.06 E-value: 4.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY-----DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP------ 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdgKDLTKLSrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 ----VGYMPQkD---MLLPWRTIIENAALPLECQGVQ-KKEAQVKAKELLYKFGLQ-GYETKHPKDLSGGMRQRVSFIRT 143
Cdd:COG1123 340 lrrrVQMVFQ-DpysSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447179532 144 LLTGGEILLLDEPFSALDALTKASLQEwLFEQWQ-EWEKTILFITHDVEEALFLSNRVLV------VEQQP 207
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILN-LLRDLQrELGLTYLFISHDLAVVRYIADRVAVmydgriVEDGP 488
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-202 |
8.53e-44 |
|
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: 147.02 E-value: 8.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-------TETKHHPVGYMPQK 79
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdvtdLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAV 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-202 |
2.62e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 147.79 E-value: 2.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-------TETKHHPV 73
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdgqdithVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447179532 154 DEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVV 217
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-208 |
2.22e-41 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 141.48 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELT---ETKHHP----VGYMPQK 79
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNgqdATRVHArdrkIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-216 |
4.76e-41 |
|
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: 140.76 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI---------ELTETKHHpVGYMP 77
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrkEPREARRQ-IGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 158 SALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVL------VVEQQPITTLTERIV 216
Cdd:COG4555 161 NGLDVMARRLLRE-ILRALKKEGKTVLFSSHIMQEVEALCDRVVilhkgkVVAQGSLDELREEIG 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-194 |
4.96e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 139.92 E-value: 4.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG-LE---KVSiGKIEL---------TETKHhpV 73
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSpafSAS-GEVLLngrrltalpAEQRR--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQKDMLLPWRTIIENA--ALPlecQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEIL 151
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447179532 152 LLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEAL 194
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-207 |
1.28e-40 |
|
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: 145.82 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL--------EKVSIGKIELTETKHHP--- 72
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphggrisGEVLLDGRDLLELSEALrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 -VGYMPQKDM--LLPWrTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:COG1123 84 rIGMVFQDPMtqLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 150 ILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQQP 207
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVmddgriVEDGP 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-205 |
1.39e-40 |
|
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: 139.34 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYMPQKDmL 82
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV---DGQDITGLSEKE-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 83 LPWR----------------TIIENAALPL-ECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLL 145
Cdd:COG1127 78 YELRrrigmlfqggalfdslTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-205 |
2.92e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.26 E-value: 2.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTEtkhHPVGYMPQKDM--- 81
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG---QDLSRLKRREIpyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 ------------LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:COG2884 78 rrrigvvfqdfrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 150 ILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDveEALF--LSNRVLVVEQ 205
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIME-LLEEINRRGTTVLIATHD--LELVdrMPKRVLELED 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-205 |
3.89e-40 |
|
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: 136.37 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL---------TETKHHpVGYMP 77
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkepEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPWRTIIENAalplecqgvqkkeaqvkakellykfglqgyetkhpkDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447179532 158 SALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03230 124 SGLDPESRREFWE-LLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-204 |
2.71e-39 |
|
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: 135.50 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 23 HELNASIH-EKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-------TETKHH------PVGYMPQKDMLLPWRTI 88
Cdd:cd03297 13 FTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdSRKKINlppqqrKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 89 IENAALPLecQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASL 168
Cdd:cd03297 93 RENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 447179532 169 QEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVE 204
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-205 |
8.02e-39 |
|
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: 132.37 E-value: 8.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 8 QFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETK---------HHPVGYMPQ 78
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDiaklpleelRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 kdmllpwrtiienaalplecqgvqkkeaqvkakellykfglqgyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 159 ALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd00267 110 GLDPASRERLLE-LLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-208 |
1.76e-38 |
|
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: 133.78 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----------TETKHHP--VG 74
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedisglseAELYRLRrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENAALPL-ECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 154 DEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-211 |
3.64e-38 |
|
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: 133.39 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY----DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETkhhPVGYMPQKDM- 81
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAFr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 -------------LLPWRTIIENAALPLECQGVQKKEAQVKakELLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLLTG 147
Cdd:COG1124 79 rrvqmvfqdpyasLHPRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 148 GEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTL 211
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVmqngriVEELTVADL 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-203 |
4.89e-38 |
|
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: 132.24 E-value: 4.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVS--FHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL------TETKHHP--VGYM 76
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysirTDRKAARqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEP 156
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 157 FSALDALTKASLqeWLFEQWQEWEKTILFITHDVEEALFLSNRVLVV 203
Cdd:cd03263 161 TSGLDPASRRAI--WDLILEVRKGRSIILTTHSMDEAEALCDRIAIM 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-205 |
1.34e-37 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 130.68 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--------TETKHHPVGYMPQ 78
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirdaREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRTIIENAALPLECQGVQKKEAQVKakELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREAID--EALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 159 ALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLsnRVLVVEQ 205
Cdd:COG4133 161 ALDAAGVALLAE-LIAAHLARGGAVLLTTHQPLELAAA--RVLDLGD 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-205 |
1.68e-37 |
|
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: 131.16 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEK----PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTET 68
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltllsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 69 KHHpVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGG 148
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 149 EILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-203 |
1.89e-37 |
|
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: 131.30 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 24 ELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTET-------KHHPVGYMPQKDMLLPWRTIIENAALPL 96
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppEKRDISYVPQNYALFPHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 97 ECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQW 176
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180
....*....|....*....|....*..
gi 447179532 177 QEWEKTILFITHDVEEALFLSNRVLVV 203
Cdd:cd03299 177 KEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-205 |
2.07e-37 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 129.04 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD--EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL---------TETKHHPVGY 75
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdlrdldLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPwRTIIENAalplecqgvqkkeaqvkakellykfglqgyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:cd03228 81 VPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447179532 156 PFSALDALTKASLQEwLFEQWQEwEKTILFITHDVEEALfLSNRVLVVEQ 205
Cdd:cd03228 123 ATSALDPETEALILE-ALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-208 |
2.82e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 134.08 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKhhpvgy 75
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgeDVTHRS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDM--------LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTG 147
Cdd:PRK11432 75 IQQRDIcmvfqsyaLFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447179532 148 GEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-202 |
5.89e-37 |
|
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: 132.62 E-value: 5.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 37 IIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHH--PVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVK 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSImldgeDVTNVPPHlrHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 110 AKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHD 189
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|...
gi 447179532 190 VEEALFLSNRVLV 202
Cdd:TIGR01187 161 QEEAMTMSDRIAI 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-205 |
1.04e-36 |
|
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: 128.80 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHH------PVGY 75
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglKLTDDKKNinelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPWRTIIENAAL-PLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447179532 155 EPFSALDA-LTKASLQewLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03262 161 EPTSALDPeLVGEVLD--VMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-161 |
1.82e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 128.96 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHHP------VG 74
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgeDLTDSKKDInklrrkVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENAAL-PLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
....*...
gi 447179532 154 DEPFSALD 161
Cdd:COG1126 161 DEPTSALD 168
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-205 |
2.09e-36 |
|
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: 127.99 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIihELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKH-------HPVGYMPQK 79
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaappadRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-205 |
5.57e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 5.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIihELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHH--PVGYMPQK 79
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqDLTALPPAerPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALplecqGVQKK-----EAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:COG3840 80 NNLFPHLTVAQNIGL-----GLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 155 EPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-204 |
7.90e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 130.53 E-value: 7.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTET-------KHHPVGYMPQKDMLL 83
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL 163
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447179532 164 TKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVE 204
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLD 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-204 |
8.38e-36 |
|
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: 126.91 E-value: 8.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLE----------KVSIGKIELTETKHHP---- 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgapdegEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 --VGYMPQKDMLLPwRTIIENAALPLECQGVQ-KKEAQVKAKELLYKFGLQGYETK--HPKDLSGGMRQRVSFIRTLLTG 147
Cdd:cd03260 81 rrVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 148 GEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVEEALFLSNRVLVVE 204
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLL 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-205 |
7.53e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 127.12 E-value: 7.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVS--FHYDEKPII--HELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTET 68
Cdd:COG1135 1 MIELENLSktFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgvdltalserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 69 KHHpVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGG 148
Cdd:COG1135 81 RRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 149 EILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHD---VEEalfLSNRVLVVEQ 205
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvVRR---ICDRVAVLEN 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-205 |
7.60e-35 |
|
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: 125.16 E-value: 7.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP-------VGYM 76
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgRDLASLSrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQ----------KDMLL----PWRTIIenaalplecqGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIR 142
Cdd:COG1120 81 PQeppapfgltvRELVAlgryPHLGLF----------GRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447179532 143 TLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-158 |
1.36e-34 |
|
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: 121.22 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 22 IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEK-----VSIGKIELTETKHHP----VGYMPQKDMLLPWRTIIENA 92
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSptegtILLDGQDLTDDERKSlrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 93 ALPLECQGVQKKEAQVKAKELLYKFGLQGYETKH----PKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-193 |
1.42e-34 |
|
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: 123.70 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYD--EKP--IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP------ 72
Cdd:COG4181 5 SAPIIELRGLTKTVGtgAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 -------VGYMPQKDMLLPWRTIIENAALPLECQGVqkKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLL 145
Cdd:COG4181 85 arlrarhVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEA 193
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-205 |
2.25e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 122.77 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE-----LTETKHHPVGYMPQKDM 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447179532 162 ALTKASLQEWLFEQwQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03269 161 PVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-208 |
2.35e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 126.35 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTET-------KHHPVGYMPQKDMLL 83
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhaRDRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRTIIENAALPLECQGVQKK--EAQVKAK--ELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:PRK10851 87 RHMTVFDNIAFGLTVLPRRERpnAAAIKAKvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-205 |
5.89e-34 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 121.59 E-value: 5.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYD-EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHPVGYMP----- 77
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIagEDVNRLRGRQLPllrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 -----QKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLqgyETKH---PKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:TIGR02673 81 igvvfQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGL---EHKAdafPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 150 ILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILD-LLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-205 |
6.94e-34 |
|
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: 128.80 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEK----------VSIGKIELTETKHHpVG 74
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEptsgrilidgIDLRQIDPASLRRQ-IG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPwRTIIENAAL-----PLEcqgvqkkeaqvKAKELLYKFGL--------QGYETK---HPKDLSGGMRQRV 138
Cdd:COG2274 553 VVLQDVFLFS-GTIRENITLgdpdaTDE-----------EIIEAARLAGLhdfiealpMGYDTVvgeGGSNLSGGQRQRL 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 139 SFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDvEEALFLSNRVLVVEQ 205
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHR-LSTIRLADRIIVLDK 684
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-205 |
7.40e-34 |
|
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: 120.23 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 10 HNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTEtkhHPVGYMPQKDMLlpwRTIi 89
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG---KDLASLSPKELA---RKI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 90 enAALPlecqgvqkkeaQVkakelLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQ 169
Cdd:cd03214 76 --AYVP-----------QA-----LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 447179532 170 EWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03214 138 ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-209 |
1.12e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIG-------KIELTETKHHPV----G 74
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENAAL-PLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 154 DEPFSALDALTKaslQEWL--FEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPIT 209
Cdd:PRK09493 161 DEPTSALDPELR---HEVLkvMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-201 |
1.22e-33 |
|
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: 120.44 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 10 HNVSFHYDEKP-IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP------VGYMPQK-DM 81
Cdd:cd03226 3 ENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkerrksIGYVMQDvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 LLPWRTIIENAALPLEcqgvQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:cd03226 83 QLFTDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447179532 162 ALTKASLQEWlFEQWQEWEKTILFITHDVEEALFLSNRVL 201
Cdd:cd03226 159 YKNMERVGEL-IRELAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-204 |
1.98e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.76 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 22 IHELNASIHEKEFVSIIGPSGCGKSTLFRL-------------ITGLEKVSIGKIELTETKHHPVGYMPQKDMLLPWRTI 88
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLlnrlieptrgqvlIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 89 IENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASL 168
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 447179532 169 QEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVE 204
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-205 |
2.37e-33 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 120.15 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKP----IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTET 68
Cdd:TIGR02211 1 LLKCENLGKRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVlfngqslsklssnERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 69 KHHPVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGG 148
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 149 EILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSnRVLVVEQ 205
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLD-RVLEMKD 216
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-191 |
2.56e-33 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 119.64 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPV-------------GYMP 77
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnskkaskfrreklGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190
....*....|....*....|....*....|....
gi 447179532 158 SALDALTKASLQEWLFEQWQEwEKTILFITHDVE 191
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPE 195
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-209 |
1.62e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 124.10 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHHP----VGYM 76
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvDLSDLDPASwrrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPWrTIIEN--------------AALplecqgvqkkeAQVKAKELLYKFGlQGYETK---HPKDLSGGMRQRVS 139
Cdd:COG4988 417 PQNPYLFAG-TIRENlrlgrpdasdeeleAAL-----------EAAGLDEFVAALP-DGLDTPlgeGGRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 140 FIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHDvEEALFLSNRVLVVEQQPIT 209
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIV 550
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
7-211 |
1.81e-32 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 117.65 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIihELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKH-------HPVGYMPQK 79
Cdd:TIGR01277 1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHtglapyqRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:TIGR01277 79 NNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447179532 160 LDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTL 211
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-204 |
2.35e-31 |
|
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: 114.81 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP----------V 73
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVngQDVSDLRgraipylrrkI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 154 DEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVE 204
Cdd:cd03292 161 DEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-229 |
2.78e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.62 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 21 IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLE-----KVSIGKIELTETKH------------HPVGYMPQKDMLL 83
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEqpeagTIRVGDITIDTARSlsqqkglirqlrQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRTIIENAAL-PLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDA 162
Cdd:PRK11264 98 PHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 163 -LTKASLQEwlFEQWQEWEKTILFITHDVEEALFLSNRVL------VVEQQPITTLterIVPLDHNRTRKDLYK 229
Cdd:PRK11264 178 eLVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDVADRAIfmdqgrIVEQGPAKAL---FADPQQPRTRQFLEK 246
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-201 |
5.31e-31 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 114.70 E-value: 5.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTETKHH 71
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtditklrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 72 pVGYMPQKDMLLPWRTIIEN------AALPL--ECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRT 143
Cdd:TIGR02315 81 -IGMIFQHYNLIERLTVLENvlhgrlGYKPTwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 144 LLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVL 201
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIV 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-224 |
8.56e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 117.24 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-------TETKHHPVGYMPQ 78
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdgvdlshVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 159 ALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTLTERIVPLDHNRTR 224
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-201 |
8.84e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 114.38 E-value: 8.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHHP------- 72
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIlvdgqDVTALRGRAlrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VGYMPQKDMLLPWRTIIEN-------------AALPLecqgvQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVS 139
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrlgrtstwrSLLGL-----FPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 140 FIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVL 201
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-216 |
9.42e-31 |
|
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: 114.20 E-value: 9.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTET-------------KHHp 72
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlRRQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VGYMPQKDMLLPWRTIIEN------AALPL--ECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTL 144
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENvlsgrlGRRSTwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 145 LTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVL------VVEQQPITTLTERIV 216
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVglkdgrIVFDGPPAELTDEVL 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-205 |
9.86e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.44 E-value: 9.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 8 QFHNVSFHYDE-KPIIHEL---NASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTETKH 70
Cdd:PRK11153 3 ELKNISKVFPQgGRTIHALnnvSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltalsekELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 71 HpVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEI 150
Cdd:PRK11153 83 Q-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 151 LLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-192 |
1.14e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.21 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHHPVGYMPQ-- 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgePLDPEDRRRIGYLPEer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 ---KDMllpwrTIIEN----AALplecQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEIL 151
Cdd:COG4152 81 glyPKM-----KVGEQlvylARL----KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447179532 152 LLDEPFSALDALTKASLQEWLFEQwQEWEKTILFITHD---VEE 192
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQmelVEE 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-205 |
2.27e-30 |
|
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: 118.33 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDE--KPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP-------VGY 75
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggVDLRDLDeddlrrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQK----DMllpwrTIIENaaLPLECQGVQkkEAQVKAkeLLYKFGL--------QGYETK---HPKDLSGGMRQRVSF 140
Cdd:COG4987 414 VPQRphlfDT-----TLREN--LRLARPDAT--DEELWA--ALERVGLgdwlaalpDGLDTWlgeGGRRLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 141 IRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHDvEEALFLSNRVLVVEQ 205
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVLED 544
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-205 |
4.39e-30 |
|
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: 111.53 E-value: 4.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPI--IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEK----------VSIGKIELTETKHHpVG 74
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKptsgsvlldgTDIRQLDPADLRRN-IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQkDMLLPWRTIIENAALPLecqGVQKKEAQVKAKELLykfGLQGYETKHPK-----------DLSGGMRQRVSFIRT 143
Cdd:cd03245 82 YVPQ-DVTLFYGTLRDNITLGA---PLADDERILRAAELA---GVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 144 LLTGGEILLLDEPFSALDaltkASLQEWLFEQWQEW--EKTILFITHDVeEALFLSNRVLVVEQ 205
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD----MNSEERLKERLRQLlgDKTLIIITHRP-SLLDLVDRIIVMDS 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-204 |
7.07e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHhpVGYMPQK-DML 82
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK--IGYFDQHqEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 83 LPWRTIIENAalplecQGVQKKEAQVKAKELLYKFGLQGYE-TKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:COG0488 391 DPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447179532 162 ALTKASLQEWLfeqwQEWEKTILFITHDVEealFLS---NRVLVVE 204
Cdd:COG0488 465 IETLEALEEAL----DDFPGTVLLVSHDRY---FLDrvaTRILEFE 503
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-205 |
7.09e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 7.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD-EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP-------VGYM 76
Cdd:COG1132 340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgVDIRDLTleslrrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPwRTIIEN--------------AALplecqgvqkKEAQvkAKELLYKFGlQGYET-------KhpkdLSGGMR 135
Cdd:COG1132 420 PQDTFLFS-GTIRENirygrpdatdeeveEAA---------KAAQ--AHEFIEALP-DGYDTvvgergvN----LSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447179532 136 QRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHD---VEEAlflsNRVLVVEQ 205
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRlstIRNA----DRILVLDD 549
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-205 |
8.27e-30 |
|
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: 112.14 E-value: 8.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD--EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE-----------LTETKHHpV 73
Cdd:TIGR04520 1 IEVENVSFSYPesEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldtldeenLWEIRKK-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALfLSNRVLVVEQ 205
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNK 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-200 |
1.08e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 111.06 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDE----KPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL------------- 65
Cdd:PRK11629 2 NKILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngqpmsklssaak 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 66 TETKHHPVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLL 145
Cdd:PRK11629 82 AELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRV 200
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-205 |
4.05e-29 |
|
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: 112.12 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 37 IIGPSGCGKSTLFRLITGLEKVSIGKIEL-------TETKHH------PVGYMPQKDMLLPWRTIIENaalpLE-----C 98
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdSARGIFlpphrrRIGYVFQEARLFPHLSVRGN----LLygrkrA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 99 QGVQKKEAQVKAKELLykfGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLfEQWQE 178
Cdd:COG4148 106 PRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL-ERLRD 181
|
170 180
....*....|....*....|....*...
gi 447179532 179 WEKT-ILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG4148 182 ELDIpILYVSHSLDEVARLADHVVLLEQ 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-210 |
4.95e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.01 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 9 FHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELteTKHHPVGYMPQKDMLLPWRTI 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--PKGLRIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 89 IENA------------------ALPLECQGVQKK--------------EAQVKAKELLYKFGLQGYETKHP-KDLSGGMR 135
Cdd:COG0488 79 LDTVldgdaelraleaeleeleAKLAEPDEDLERlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPvSELSGGWR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 136 QRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLfeqwQEWEKTILFITHDVEealFL---SNRVLVVEQQPITT 210
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDRY---FLdrvATRILELDRGKLTL 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
7-203 |
3.24e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.98 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKefVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHH-------PVGYMPQK 79
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFDLTVERGER--VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTttppsrrPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAAL---P-LECQGVQKKEAQVKAKellyKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:PRK10771 80 NNLFSHLTVAQNIGLglnPgLKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447179532 156 PFSALD-ALTKASLQewLFEQ-WQEWEKTILFITHDVEEALFLSNRVLVV 203
Cdd:PRK10771 156 PFSALDpALRQEMLT--LVSQvCQERQLTLLMVSHSLEDAARIAPRSLVV 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-194 |
3.45e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.78 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 16 YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGkiELTETKHHPVGYMPQK---DMLLPwRTIIENA 92
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG--TVRRAGGARVAYVPQRsevPDSLP-LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 93 AL----PLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASL 168
Cdd:NF040873 79 AMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|....*.
gi 447179532 169 QEwLFEQWQEWEKTILFITHDVEEAL 194
Cdd:NF040873 159 IA-LLAEEHARGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-205 |
4.01e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 4.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYD---EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTET----KHH 71
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdLLTEEnvwdIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 72 PVGYMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEI 150
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 151 LLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEaLFLSNRVLVVEQ 205
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKN 215
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
18-219 |
8.05e-28 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 105.87 E-value: 8.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 18 EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIG-------------KIELTETKHHpVGYMPQKDMLLP 84
Cdd:TIGR02982 17 RKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGslkvlgqelhgasKKQLVQLRRR-IGYIFQAHNLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 85 WRTIIENAALPLECQ-GVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL 163
Cdd:TIGR02982 96 FLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSK 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 164 TKASLQEWLFEQWQEWEKTILFITHDveealflsNRVLVVeqqpittlTERIVPLD 219
Cdd:TIGR02982 176 SGRDVVELMQKLAKEQGCTILMVTHD--------NRILDV--------ADRILQME 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
16-203 |
1.45e-27 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 105.32 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 16 YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHPV--------GYMPQKDMLLPW 85
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgQDITKLPMhkrarlgiGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 RTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTK 165
Cdd:cd03218 90 LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 447179532 166 ASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVV 203
Cdd:cd03218 170 QDIQK-IIKILKDRGIGVLITDHNVRETLSITDRAYII 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-206 |
1.65e-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: 103.45 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL---TETKHHP------VGY 75
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgaDISQWDPnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPwRTIIENAalplecqgvqkkeaqvkakellykfglqgyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:cd03246 81 LPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 156 PFSALDALTKASLQEwLFEQWQEWEKTILFITHDvEEALFLSNRVLVVEQQ 206
Cdd:cd03246 123 PNSHLDVEGERALNQ-AIAALKAAGATRIVIAHR-PETLASADRILVLEDG 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-202 |
2.67e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.84 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTetkhhpvGYMPQKD 80
Cdd:PRK13632 4 KSVMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID-------GITISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 MLLPWRTII-----------------ENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRT 143
Cdd:PRK13632 77 NLKEIRKKIgiifqnpdnqfigatveDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 144 LLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALfLSNRVLV 202
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIV 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-214 |
3.13e-27 |
|
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: 106.68 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHN--VSFHYDEKPI--IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEK---VSIGKIELtetKHHPVGYMPQ 78
Cdd:COG0444 1 LLEVRNlkVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILF---DGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDM------------------LLPWRTIIENAALPLE-CQGVQKKEAQVKAKELLYKFGLQGYET---KHPKDLSGGMRQ 136
Cdd:COG0444 78 KELrkirgreiqmifqdpmtsLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLPDPERrldRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 137 RVSFIRTLLTGGEILLLDEPFSALDALTKA-------SLQEwlfeqwqEWEKTILFITHDVEEALFLSNRVLV------V 203
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAqilnllkDLQR-------ELGLAILFITHDLGVVAEIADRVAVmyagriV 230
|
250
....*....|.
gi 447179532 204 EQQPITTLTER 214
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-213 |
3.80e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.78 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL------EKVSI-----GKIELTETKHHpVG 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygNDVRLfgerrGGEDVWELRKR-IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YM-PQKDMLLPWRTIIENAAL---------PLECQGVQKKeaqvKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTL 144
Cdd:COG1119 82 LVsPALQLRFPRDETVLDVVLsgffdsiglYREPTDEQRE----RARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 145 LTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEAL-FLSNRVL-----VVEQQPIT-TLTE 213
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPpGITHVLLlkdgrVVAAGPKEeVLTS 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-205 |
8.91e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.08 E-value: 8.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEK-PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKhhpVGYMPQKD----M 81
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV---VNELEPADrdiaM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 ------LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:PRK11650 81 vfqnyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 156 PFSALDALTKAS-------LQEWLfeqwqewEKTILFITHDVEEALFLSNRVLV-----VEQ 205
Cdd:PRK11650 161 PLSNLDAKLRVQmrleiqrLHRRL-------KTTSLYVTHDQVEAMTLADRVVVmnggvAEQ 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-192 |
9.79e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.26 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELT---------ETKHH 71
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgedistlkpEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 72 PVGYMPQKDMLLPwRTIIENAALPLECQGVQKKEAQVKAKelLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLLTGGEI 150
Cdd:PRK10247 82 QVSYCAQTPTLFG-DTVYDNLIFPWQIRNQQPDPAIFLDD--LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447179532 151 LLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEE 192
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-205 |
1.20e-26 |
|
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: 105.58 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 23 HELNAS--IHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-------------TETKHHPVGYMPQKDMLLPWRT 87
Cdd:TIGR02142 12 FSLDADftLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsrkgifLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 88 IIENaaLPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKAS 167
Cdd:TIGR02142 92 VRGN--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 447179532 168 LQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-206 |
2.10e-26 |
|
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: 99.83 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHhpVGYMPQkdmllpwr 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK--IGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 87 tiienaalplecqgvqkkeaqvkakellykfglqgyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKA 166
Cdd:cd03221 71 -------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447179532 167 SLQEWLfeqwQEWEKTILFITHDVEealFLS---NRVLVVEQQ 206
Cdd:cd03221 108 ALEEAL----KEYPGTVILVSHDRY---FLDqvaTKIIELEDG 143
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-205 |
2.21e-26 |
|
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: 101.89 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVsIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP------VGYMPQ 78
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIdgQDVLKQPqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRTIIEN----AALplecQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:cd03264 80 EFGVYPNFTVREFldyiAWL----KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 155 EPFSALDALTKASLQEWLFEQWQewEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-241 |
2.60e-26 |
|
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: 103.62 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 15 HYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGK--------IELTETKHHPVGYMPQK---DMLL 83
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTarvagydvVREPRKVRRSIGIVPQYasvDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRtiiENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL 163
Cdd:TIGR01188 82 TGR---ENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 164 TKASLqeW-LFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITT------LTERI---VPLDHNRTRKDLyKPEVL 233
Cdd:TIGR01188 159 TRRAI--WdYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAegtpeeLKRRLgkdTLESRPRDIQSL-KVEVS 235
|
....*...
gi 447179532 234 ALKDELLS 241
Cdd:TIGR01188 236 MLIAELGE 243
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-205 |
2.65e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLE------------------KVSIGKIELTET 68
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLEtpdsgqlniaghqfdfsqKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 69 KhhpVGYMPQKDMLLPWRTIIEN-AALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTG 147
Cdd:COG4161 83 K---VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 148 GEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVE-IIRELSQTGITQVIVTHEVEFARKVASQVVYMEK 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-198 |
5.08e-26 |
|
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: 100.08 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDE--KPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVGYMPQKDMllp 84
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 85 wrtiienaalplecqGVQKKEAQVKAKELLYKFGLQgyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALT 164
Cdd:cd03247 78 ---------------SVLNQRPYLFDTTLRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447179532 165 KASLQEWLFEQWQewEKTILFITH------DVEEALFLSN 198
Cdd:cd03247 134 ERQLLSLIFEVLK--DKTLIWITHhltgieHMDKILFLEN 171
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-208 |
5.45e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETK----HHP---------- 72
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsKTPsdkairelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 -VGYMPQKDMLLPWRTIIEN-AALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEI 150
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 151 LLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVS-IIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-189 |
6.36e-26 |
|
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: 105.40 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHhpVGYMPQ-KDMLL 83
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK--LAYVDQsRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRTIIENAALPLECQGVQKKEaqVKAKELLYKFGLQGYET-KHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDA 162
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKRE--IPSRAYVGRFNFKGSDQqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
170 180
....*....|....*....|....*..
gi 447179532 163 LTKASLQEWLfeqwQEWEKTILFITHD 189
Cdd:TIGR03719 477 ETLRALEEAL----LNFAGCAVVISHD 499
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-211 |
1.09e-25 |
|
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: 101.42 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY---------DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYM 76
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF---RGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDM-----------------LLPWRTIIENAALPLE-CQGVQKKEAQVKAKELLYKFGLQG-YETKHPKDLSGGMRQR 137
Cdd:TIGR02769 79 DRKQRrafrrdvqlvfqdspsaVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 138 VSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTL 211
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVmdkgqiVEECDVAQL 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-188 |
1.83e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 99.99 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 8 QFHNVSFHYDEK-PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI--------ELTE-TKHHPVGYMP 77
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirDISRkSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPwRTIIENAAL--PLECQGVQKKEAQVKAKELLYKFGLQGYET---KHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:cd03254 84 QDTFLFS-GTIMENIRLgrPNATDEEVIEAAKEAGAHDFIMKLPNGYDTvlgENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQewEKTILFITH 188
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
28-202 |
1.89e-25 |
|
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: 99.82 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYMP-------------QKDMLLPWRTIIENAAL 94
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF---DGEDITGLPpheiarlgigrtfQIPRLFPELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 95 PLECQGV----------QKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALT 164
Cdd:cd03219 99 AAQARTGsglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 447179532 165 KASLQEWLfEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:cd03219 179 TEELAELI-RELRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-203 |
3.32e-25 |
|
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: 98.98 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 16 YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI---------ELTETKHHpVGYMPQKDMLLPWR 86
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdvvrEPREVRRR-IGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 87 TIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKA 166
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 447179532 167 SLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVV 203
Cdd:cd03265 169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-205 |
3.76e-25 |
|
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: 99.73 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYMP-------- 77
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF---DGRDITGLPphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 -----QKDMLLPWRTIIENAALPLECQG---------------VQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQR 137
Cdd:COG0411 81 iartfQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 138 VSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
28-214 |
3.84e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 100.96 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYMPQKDM-----------------LLPWRTIIE 90
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF---DGQDITGLSGRELrplrrrmqmvfqdpyasLNPRMTVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 91 NAALPLECQGVQ-KKEAQVKAKELLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDaltkASL 168
Cdd:COG4608 117 IIAEPLRIHGLAsKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD----VSI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 169 QEW---LFEQWQEwEK--TILFITHD---VEealFLSNRVLV------VEQQPITTLTER 214
Cdd:COG4608 193 QAQvlnLLEDLQD-ELglTYLFISHDlsvVR---HISDRVAVmylgkiVEIAPRDELYAR 248
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-188 |
3.95e-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: 99.23 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD-EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE-----LTETKHHP----VGYM 76
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdIREVTLDSlrraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQkDMLLPWRTIIENAAL-PLECQGVQKKEAQVKAK--ELLYKFGlQGYETKHPK---DLSGGMRQRVSFIRTLLTGGEI 150
Cdd:cd03253 81 PQ-DTVLFNDTIGYNIRYgRPDATDEEVIEAAKAAQihDKIMRFP-DGYDTIVGErglKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 447179532 151 LLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITH 188
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
33-203 |
5.15e-25 |
|
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: 98.21 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 33 EFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELT--ETKHHP------VGYMPQKDMLLPWRTIIENAALPLECQGVQKK 104
Cdd:cd03266 32 EVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPaearrrLGFVSDSTGLYDRLTARENLEYFAGLYGLKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 105 EAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLfEQWQEWEKTIL 184
Cdd:cd03266 112 ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI-RQLRALGKCIL 190
|
170
....*....|....*....
gi 447179532 185 FITHDVEEALFLSNRVLVV 203
Cdd:cd03266 191 FSTHIMQEVERLCDRVVVL 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-206 |
9.68e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.93 E-value: 9.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEK----PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----------- 65
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 66 --TETKHHPVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLqGYETKH-PKDLSGGMRQRVSFIR 142
Cdd:PRK10584 81 arAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGL-GKRLDHlPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 143 TLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQ 206
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-202 |
1.09e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.93 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDE--KPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL-----EKVSIGKIELTETK----HHP 72
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLllpeaGTITVGGMVLSEETvwdvRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VGYMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEIL 151
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 152 LLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFlSNRVLV 202
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIV 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-199 |
1.11e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVsIGKIELTET---KHHPVgYMPQK 79
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDL-NPEVTITGSivyNGHNI-YSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DML---------------LPWrTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETK---HPK--DLSGGMRQRVS 139
Cdd:PRK14239 80 DTVdlrkeigmvfqqpnpFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKdrlHDSalGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 140 FIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVEEALFLSNR 199
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDR 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-245 |
1.18e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELT-----ETKHHP---VG 74
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCgepvpSRARHArqrVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 155 EPFSALDALTKASLQEWLfEQWQEWEKTILFITHDVEEALFLSNRVLVVE------QQPITTLTERIVPLDhnrtRKDLY 228
Cdd:PRK13537 164 EPTTGLDPQARHLMWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVIEegrkiaEGAPHALIESEIGCD----VIEIY 238
|
250
....*....|....*..
gi 447179532 229 KPEVLALKDELLSMLQR 245
Cdd:PRK13537 239 GPDPVALRDELAPLAER 255
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-215 |
1.93e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.80 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFR-------LITGLeKVSiGKIEL---------- 65
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGA-RVE-GEILLdgediydpdv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 66 ---TETKHhpVGYMPQKDMLLPWrTIIENAALPLECQGVQKKEA----------------QVKAKelLYKFGLqgyetkh 126
Cdd:COG1117 86 dvvELRRR--VGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSEldeiveeslrkaalwdEVKDR--LKKSAL------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 127 pkDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVEEALFLSNRVL----- 201
Cdd:COG1117 154 --GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAffylg 229
|
250
....*....|....*
gi 447179532 202 -VVEQQPittlTERI 215
Cdd:COG1117 230 eLVEFGP----TEQI 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-194 |
2.40e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI----------ELTET 68
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 69 KHHpVGYMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTG 147
Cdd:PRK13648 82 RKH-IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 148 GEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEAL 194
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-203 |
3.34e-24 |
|
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: 100.44 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL-----EKVSIGKIELTETKHHP----VGYM 76
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvdpteGSIAVNGVPLADADADSwrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPwRTIIENAALplecqgvQKKEAQVKA-KELLYKFGL--------QGYETK---HPKDLSGGMRQRVSFIRTL 144
Cdd:TIGR02857 402 PQHPFLFA-GTIAENIRL-------ARPDASDAEiREALERAGLdefvaalpQGLDTPigeGGAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 145 LTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHDVEEALfLSNRVLVV 203
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-189 |
4.91e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.18 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 21 IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTETKHHPVGYMPQKDMLLPWRT 87
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagqdvatldadALAQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 88 IIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKAS 167
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180
....*....|....*....|..
gi 447179532 168 LQEWLfEQWQEWEKTILFITHD 189
Cdd:PRK10535 183 VMAIL-HQLRDRGHTVIIVTHD 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-170 |
1.04e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.48 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETK--HHP--------VGY 75
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDitHLPmhkrarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQ-----KDMllpwrTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQgyetkHPKD-----LSGGMRQRVSFIRTLL 145
Cdd:COG1137 83 LPQeasifRKL-----TVEDNILAVLELRKLSKKEREERLEELLEEFGIT-----HLRKskaysLSGGERRRVEIARALA 152
|
170 180
....*....|....*....|....*
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQE 170
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQK 177
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-204 |
2.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL--------EKVSIGKIELTETK--- 69
Cdd:PRK13640 2 KDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTvwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 -HHPVGYMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTG 147
Cdd:PRK13640 82 iREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 148 GEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALfLSNRVLVVE 204
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLD 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-208 |
2.79e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNA---SIHEKEFVSIIGPSGCGKSTLFRLITGL--EKVSIGKIELTETKHHPVGYMPQK- 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGvsfSITKGEWVSIIGQNGSGKSTTARLIDGLfeEFEGKVKIDGELLTAENVWNLRRKi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 -------DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:PRK13642 84 gmvfqnpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFlSNRVLVVEQQPI 208
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-209 |
4.00e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.37 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHY---------DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETkhhPVGY 75
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE---PLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MP-------QKDMLL----------PWRTIIENAALPLE-CQGVQKKEAQVKAKELLYKFGLQ-GYETKHPKDLSGGMRQ 136
Cdd:PRK10419 79 LNraqrkafRRDIQMvfqdsisavnPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 137 RVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQQPIT 209
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVmdngqiVETQPVG 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-208 |
4.28e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.27 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPV----GYMPQ 78
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KD----MLLPWR--------------TIIENA-ALPLECQGVQKKEAQVKAKELLYKFGLQGY-ETKHPKDLSGGMRQRV 138
Cdd:PRK10619 82 ADknqlRLLRTRltmvfqhfnlwshmTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447179532 139 SFIRTLLTGGEILLLDEPFSALDA-LTKASLQewLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPeLVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-210 |
4.36e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 93.38 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP----VGYMPQK-----DMLLPWRTIIENAAL---- 94
Cdd:TIGR03771 2 SADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKgwrhIGYVPQRhefawDFPISVAHTVMSGRTghig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 95 PLECQGVQKKEAQVKAkelLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEwLFE 174
Cdd:TIGR03771 82 WLRRPCVADFAAVRDA---LRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE-LFI 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 447179532 175 QWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITT 210
Cdd:TIGR03771 158 ELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIAD 193
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-172 |
5.46e-23 |
|
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: 93.37 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 9 FHNVSFHYDEKP---IIHELNASIHEKEFVSIIGPSGCGKSTLFRLI-------TG---LEKVSIGKIELTETKHHpVGY 75
Cdd:cd03249 3 FKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGeilLDGVDIRDLNLRWLRSQ-IGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPwRTIIENAALPLEcQGVQKKEAQVKAKELLYKF--GL-QGYET---KHPKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:cd03249 82 VSQEPVLFD-GTIAENIRYGKP-DATDEEVEEAAKKANIHDFimSLpDGYDTlvgERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180
....*....|....*....|...
gi 447179532 150 ILLLDEPFSALDALTKASLQEWL 172
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEAL 182
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-188 |
9.54e-23 |
|
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: 91.84 E-value: 9.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL---EKVSiGKIELTETKHHP------VG 74
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtgLGVS-GEVLINGRPLDKrsfrkiIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENaalplecqgvqkkeaqvkakeLLYKFGLQGyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:cd03213 86 YVPQDDILHPTLTVRET---------------------LMFAAKLRG--------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190
....*....|....*....|....*....|....
gi 447179532 155 EPFSALDALTKASLQEwLFEQWQEWEKTILFITH 188
Cdd:cd03213 137 EPTSGLDSSSALQVMS-LLRRLADTGRTIICSIH 169
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-208 |
2.61e-22 |
|
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: 91.52 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE----------LTETKHHpVG 74
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytLASLRRQ-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQkDMLLPWRTIIENAALPLEcqGVQKKEA-----QVKAKELLYKFGlQGYETK---HPKDLSGGMRQRVSFIRTLLT 146
Cdd:cd03251 80 LVSQ-DVFLFNDTVAENIAYGRP--GATREEVeeaarAANAHEFIMELP-EGYDTVigeRGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 147 GGEILLLDEPFSALDALTKASLQEWLfEQWQEwEKTILFITH---DVEEAlflsNRVLVVEQQPI 208
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAAL-ERLMK-NRTTFVIAHrlsTIENA----DRIVVLEDGKI 214
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-205 |
3.72e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 94.72 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 18 EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELT---------ETKHHPVGYMPQKDMLLPwRTI 88
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDgadlkqwdrETFGKHIGYLPQDVELFP-GTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 89 IENAALPLECQGVQKKEAQVK---AKELLYKFGlQGYETKHPKD---LSGGMRQRVSFIRTLLTGGEILLLDEPFSALDA 162
Cdd:TIGR01842 409 AENIARFGENADPEKIIEAAKlagVHELILRLP-DGYDTVIGPGgatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447179532 163 LTKASLQEWLfEQWQEWEKTILFITHDVeEALFLSNRVLVVEQ 205
Cdd:TIGR01842 488 EGEQALANAI-KALKARGITVVVITHRP-SLLGCVDKILVLQD 528
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-202 |
4.87e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.30 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 17 DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYMPQ-----------KDMLL-- 83
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI---DGKDVTKLPEykrakyigrvfQDPMMgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 -PWRTIIENAAL--------PLEcQGVQKKEAQvKAKELLYKFGLqGYEtKHPKD----LSGGMRQRVSFIRTLLTGGEI 150
Cdd:COG1101 94 aPSMTIEENLALayrrgkrrGLR-RGLTKKRRE-LFRELLATLGL-GLE-NRLDTkvglLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447179532 151 LLLDEPFSALDALTKASLQEwLFEQWQEWEK-TILFITHDVEEALFLSNRVLV 202
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLE-LTEKIVEENNlTTLMVTHNMEQALDYGNRLIM 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-189 |
5.98e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.03 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHhpVGYMPQ-KDMLL 83
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK--LAYVDQsRDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRTIIENAALPLECQGVQKKEAQVKAkellY--KFGLQGYE-TKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSAL 160
Cdd:PRK11819 401 PNKTVWEEISGGLDIIKVGNREIPSRA----YvgRFNFKGGDqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170 180
....*....|....*....|....*....
gi 447179532 161 DALTKASLQEWLfeqwQEWEKTILFITHD 189
Cdd:PRK11819 477 DVETLRALEEAL----LEFPGCAVVISHD 501
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-203 |
8.57e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.91 E-value: 8.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPVGYmpQKDMLLP 84
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI---KGEPIKY--DKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 85 WR-----------------TIIENAAL-PLECqGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLT 146
Cdd:PRK13639 76 VRktvgivfqnpddqlfapTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 147 GGEILLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVV 203
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVM 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-234 |
1.58e-21 |
|
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: 89.47 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL----------EKVSIGKIELTETKHHpVG 74
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyvpengrvlvDGHDLALADPAWLRRQ-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPwRTIIENAALPLECQGVQKKEAQVK---AKELLYKFGLqGYET---KHPKDLSGGMRQRVSFIRTLLTGG 148
Cdd:cd03252 80 VVLQENVLFN-RSIRDNIALADPGMSMERVIEAAKlagAHDFISELPE-GYDTivgEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 149 EILLLDEPFSALDaltkaslqewlfeqwQEWEKTILFITHDVeealfLSNRVLVVEQQPITTL--TERIVPLDHNRTRKD 226
Cdd:cd03252 158 RILIFDEATSALD---------------YESEHAIMRNMHDI-----CAGRTVIIIAHRLSTVknADRIIVMEKGRIVEQ 217
|
....*...
gi 447179532 227 LYKPEVLA 234
Cdd:cd03252 218 GSHDELLA 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-161 |
2.50e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.40 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP-------VGYMP 77
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLngRPLAAWSpwelarrRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QK-DMLLPWrTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLL-------TGGE 149
Cdd:COG4559 82 QHsSLAFPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170
....*....|..
gi 447179532 150 ILLLDEPFSALD 161
Cdd:COG4559 161 WLFLDEPTSALD 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-205 |
2.67e-21 |
|
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: 88.43 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTE---TKHHP----VGYMPQK 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyQKNIEalrrIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQvkakELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447179532 160 LDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03268 157 LDPDGIKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
33-205 |
2.83e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.78 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 33 EFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHHPV-------GYMPQKDMLLPWRTIIENAALPLECQG 100
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLKNREVpflrrqiGMIFQDHHLLMDRTVYDNVAIPLIIAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 101 VQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD-ALTKASLQewLFEQWQEW 179
Cdd:PRK10908 109 ASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdALSEGILR--LFEEFNRV 186
|
170 180
....*....|....*....|....*.
gi 447179532 180 EKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK10908 187 GVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-189 |
3.76e-21 |
|
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: 91.65 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHE-LNASIHEKEFVSIIGPSGCGKSTLFRLITGL-----EKVSIGKIELTETKHHP----VGYM 76
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDgVSLDLPPGERVAILGPSGSGKSTLLATLAGLldplqGEVTLDGVPVSSLDQDEvrrrVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPwRTIIENaaLPLECQGVQKKEAQvkakELLYKFGL--------QGYETK---HPKDLSGGMRQRVSFIRTLL 145
Cdd:TIGR02868 415 AQDAHLFD-TTVREN--LRLARPDATDEELW----AALERVGLadwlralpDGLDTVlgeGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHD 189
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-204 |
4.96e-21 |
|
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: 87.52 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEK-----PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG-LEKVSiGKIELtetkHHPVGYMPQKd 80
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLS-GSVSV----PGSIAYVSQE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 mllPW---RTIIEN--AALPLEcqgVQKKEAQVKAKELLykfglqgyetkhpKD------------------LSGGMRQR 137
Cdd:cd03250 75 ---PWiqnGTIRENilFGKPFD---EERYEKVIKACALE-------------PDleilpdgdlteigekginLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 138 VSFIRTLLTGGEILLLDEPFSALDALTKAslqeWLFEQ-----WQEwEKTILFITHDVeEALFLSNRVLVVE 204
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGR----HIFENcilglLLN-NKTRILVTHQL-QLLPHADQIVVLD 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-204 |
5.24e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--------TETKHHPVGYMPQ 78
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvparARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447179532 159 ALDALTKASLQEWLfEQWQEWEKTILFITHDVEEALFLSNRVLVVE 204
Cdd:PRK13536 202 GLDPHARHLIWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVLE 246
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-205 |
5.82e-21 |
|
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: 87.49 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP--------VGYM 76
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgRDITGLPpheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPWRTIIEN---AALPLECQGVQKKEAQVKA-----KELLYKFGlqgyetkhpKDLSGGMRQRVSFIRTLLTGG 148
Cdd:cd03224 81 PEGRRIFPELTVEENlllGAYARRRAKRKARLERVYElfprlKERRKQLA---------GTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 149 EILLLDEP------------FSALDALTKASLqewlfeqwqewekTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03224 152 KLLLLDEPseglapkiveeiFEAIRELRDEGV-------------TILLVEQNARFALEIADRAYVLER 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-168 |
1.66e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVS-FHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHhpVGYMPQKDMlLPW 85
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR--VLFLPQRPY-LPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 RTIIENAALPLECQGVqkKEAQVkaKELLYKFGLQGYETKH------PKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:COG4178 440 GTLREALLYPATAEAF--SDAEL--REALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
....*....
gi 447179532 160 LDALTKASL 168
Cdd:COG4178 516 LDEENEAAL 524
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-204 |
2.65e-20 |
|
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: 85.95 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVS--F---HYDEK--PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI--------------- 63
Cdd:COG4778 4 LLEVENLSktFtlhLQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 64 --ELTETKHHPVGYMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLqgyetkhPKDL--------SGG 133
Cdd:COG4778 84 prEILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447179532 134 MRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVE--EAlfLSNRVLVVE 204
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVE-LIEEAKARGTAIIGIFHDEEvrEA--VADRVVDVT 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-205 |
3.23e-20 |
|
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: 89.69 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 19 KPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----TETK----HHPVGYMPQKDMLLPWRTIIE 90
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggkdIETNldavRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 91 NAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQE 170
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*
gi 447179532 171 WLFEQWQewEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:TIGR01257 1103 LLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQ 1135
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-205 |
3.38e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI----------ELTETKHHPVGY 75
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPWRTIIENAALPLEC-QGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 155 EPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK10895 163 EPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQ 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-205 |
5.85e-20 |
|
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: 88.27 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RSKNILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP----- 72
Cdd:COG4618 326 RPKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgADLSQWDreelg 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 --VGYMPQKDMLLPwRTIIEN--------------AAlplecqgvqkKEAQVkaKELLYKFGlQGYETK-----HPkdLS 131
Cdd:COG4618 406 rhIGYLPQDVELFD-GTIAENiarfgdadpekvvaAA----------KLAGV--HEMILRLP-DGYDTRigeggAR--LS 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 132 GGMRQRVSFIRTLLTGGEILLLDEPFSALD-----ALTKAslqewlFEQWQEWEKTILFITHDVeEALFLSNRVLVVEQ 205
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaALAAA------IRALKARGATVVVITHRP-SLLAAVDKLLVLRD 541
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-205 |
1.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD-----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELT------ETKHHPVGY 75
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLL---PWRTIIENAAL------PLECqGVQKKEAQVKAKELLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLL 145
Cdd:PRK13641 83 LRKKVSLVfqfPEAQLFENTVLkdvefgPKNF-GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEH 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-214 |
1.75e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.08 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY---DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHH----PVG 74
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvPLVQYDHHylhrQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPwRTIIENAALPL---ECQGVQKKEAQVKAKELLYKFGlQGYET---KHPKDLSGGMRQRVSFIRTLLTGG 148
Cdd:TIGR00958 559 LVGQEPVLFS-GSVRENIAYGLtdtPDEEIMAAAKAANAHDFIMEFP-NGYDTevgEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 149 EILLLDEPFSALDALTKASLQEWLFEQwqewEKTILFITH------DVEEALFLsNRVLVVEQQPITTLTER 214
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRSRA----SRTVLLIAHrlstveRADQILVL-KKGSVVEMGTHKQLMED 703
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-205 |
2.37e-19 |
|
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: 83.35 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 16 YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVGYMP--QKDMllpwrTIIENAA 93
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGgfNPEL-----TGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 94 LPLECQGVQKKEAQVKAKElLYKF-GLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWL 172
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDE-IIEFsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190
....*....|....*....|....*....|...
gi 447179532 173 FEQWQEwEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-203 |
2.77e-19 |
|
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: 82.09 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIihelNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----------TETKHHPV 73
Cdd:cd03215 2 EPVLEVRGLSVKGAVRDV----SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrspRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMP---QKDMLLPWRTIIENAALPLEcqgvqkkeaqvkakellykfglqgyetkhpkdLSGGMRQRVSFIRTLLTGGEI 150
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447179532 151 LLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVV 203
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVM 177
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-161 |
3.31e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.67 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPV------------G 74
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL---NGRPLadwspaelarrrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDML-LPW--RTIIENAALPLecqGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLL------ 145
Cdd:PRK13548 80 VLPQHSSLsFPFtvEEVVAMGRAPH---GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170
....*....|....*.
gi 447179532 146 TGGEILLLDEPFSALD 161
Cdd:PRK13548 157 GPPRWLLLDEPTSALD 172
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-220 |
4.72e-19 |
|
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: 85.95 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD-EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG----------LEKVSIGKIELTETKHHpVGY 75
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGffqarsgeilLNGFSLKDIDRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPwRTIIENAAL----PLECQGVQKKEAQVKAKELLYKFGlQGYETK---HPKDLSGGMRQRVSFIRTLLTGG 148
Cdd:TIGR01193 553 LPQEPYIFS-GSILENLLLgakeNVSQDEIWAACEIAEIKDDIENMP-LGYQTElseEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447179532 149 EILLLDEPFSALDALT-KASLQEWLFEQwqewEKTILFITHdveealflsnRVLVVEQqpittlTERIVPLDH 220
Cdd:TIGR01193 631 KVLILDESTSNLDTITeKKIVNNLLNLQ----DKTIIFVAH----------RLSVAKQ------SDKIIVLDH 683
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-205 |
7.44e-19 |
|
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: 85.26 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD-EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI--------ELTETK-HHPVGYM 76
Cdd:COG5265 358 VRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirDVTQASlRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQkDMLLPWRTI---------------IENAAlplecqgvqkKEAQvkakelLYKF--GL-QGYET-------KhpkdLS 131
Cdd:COG5265 438 PQ-DTVLFNDTIayniaygrpdaseeeVEAAA----------RAAQ------IHDFieSLpDGYDTrvgerglK----LS 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 132 GGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITH------DVEEALFLSNRVlVVEQ 205
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivDADEILVLEAGR-IVER 573
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-205 |
9.65e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 9 FHNVSFHYD-----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEK-----VSIGKIELTETKHhpvgympQ 78
Cdd:PRK13634 5 FQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQptsgtVTIGERVITAGKK-------N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDmLLPWR-----------------TIIENAALPLECQGVQKKEAQVKAKELLYKFGL-QGYETKHPKDLSGGMRQRVSF 140
Cdd:PRK13634 78 KK-LKPLRkkvgivfqfpehqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 141 IRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHK 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-212 |
1.01e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFhydekpiihelnaSIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTEtkhHPVGYMP--- 77
Cdd:PRK11300 13 MRFGGLLAVNNVNL-------------EVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG---QHIEGLPghq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 ----------QKDMLLPWRTIIENAalpLECQGVQKK------------------EAQVKAKELLYKFGLQGYETKHPKD 129
Cdd:PRK11300 77 iarmgvvrtfQHVRLFREMTVIENL---LVAQHQQLKtglfsgllktpafrraesEALDRAATWLERVGLLEHANRQAGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 130 LSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ-QPI 208
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQgTPL 233
|
....
gi 447179532 209 TTLT 212
Cdd:PRK11300 234 ANGT 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-208 |
1.42e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----------ELTETKHhPV 73
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRK-LV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:PRK13644 80 GIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 153 LDEPFSALDALTKASLQEWLfEQWQEWEKTILFITHDVEEaLFLSNRVLVVEQQPI 208
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERI-KKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-205 |
2.15e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.60 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL---EKVSIGKIEL--------------- 65
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELlgrtvqregrlardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 66 TETKHHpVGYMPQKDMLLPWRTIIENAAL------PL--ECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQR 137
Cdd:PRK09984 82 RKSRAN-TGYIFQQFNLVNRLSVLENVLIgalgstPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 138 VSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-162 |
2.42e-18 |
|
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: 80.10 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVGYMPQKDML-LPW 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 RTIIENAALPLE--------CQGvqkkeAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:TIGR01189 81 LPGLKPELSALEnlhfwaaiHGG-----AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*
gi 447179532 158 SALDA 162
Cdd:TIGR01189 156 TALDK 160
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-202 |
3.27e-18 |
|
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: 79.01 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVGympqkdmllPWR 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---------PRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 87 tiienaalplecqgvqkkeaqvkAKELlykfglqGYETKHpkDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDaltkA 166
Cdd:cd03216 72 -----------------------ARRA-------GIAMVY--QLSVGERQMVEIARALARNARLLILDEPTAALT----P 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 447179532 167 SLQEWLFE---QWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:cd03216 116 AEVERLFKvirRLRAQGVAVIFISHRLDEVFEIADRVTV 154
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-200 |
3.99e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL----------EKVSIGKIELTETKHHP- 72
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneearveGEVRLFGRNIYSPDVDPi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 -----VGYMPQKDMLLPWRTIIENAALPLECQGV--QKKEAQVKAKELLYKFGLQGyETK-----HPKDLSGGMRQRVSF 140
Cdd:PRK14267 82 evrreVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWD-EVKdrlndYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 141 IRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVEEALFLSNRV 200
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYV 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-205 |
4.56e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYD-----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETK------HHPVG 74
Cdd:PRK13637 7 NLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvDITDKKvklsdiRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQ-KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGL--QGYETKHPKDLSGGMRQRVSFIRTLLTGGEIL 151
Cdd:PRK13637 87 LVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447179532 152 LLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNK 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-208 |
6.96e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 6.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI--------ELTETKHHP 72
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 V----GYMPQKDMLLPWRTIIENAALPLEcQGVQKKEAQVKAKEL--LYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLT 146
Cdd:PRK11831 82 VrkrmSMLFQSGALFTDMNVFDNVAYPLR-EHTQLPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 147 GGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-205 |
7.80e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.46 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 24 ELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTET--------------KHHpVGYMPQKDMLLPWRTII 89
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppeKRR-IGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 90 ENAalpleCQGVQKKEAQVKAK--ELLykfGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKAS 167
Cdd:PRK11144 95 GNL-----RYGMAKSMVAQFDKivALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 447179532 168 LQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQ 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-203 |
7.93e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.90 E-value: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYDEK-PI----IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL------TETKHHPVGYMPQK 79
Cdd:PRK13651 7 NIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWR----------------------------TIIENAALPLECQGVQKKEAQVKAKELLYKFGL-QGYETKHPKDL 130
Cdd:PRK13651 87 LVIQKTRfkkikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 131 SGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL-TKASLQewLFEQWQEWEKTILFITHDVEEALFLSNRVLVV 203
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILE--IFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-204 |
8.78e-18 |
|
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: 79.44 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKP---IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL-----TETKH---HP 72
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpiSQYEHkylHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VGYMPQKDMLLPWRTIIENAALPL-ECQGVQKKEAQVKAKELLYKFGL-QGYET---KHPKDLSGGMRQRVSFIRTLLTG 147
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLqSCSFECVKEAAQKAHAHSFISELaSGYDTevgEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 148 GEILLLDEPFSALDALTKASLQEWLFeQWQEwEKTILFITH---DVEEAlflsNRVLVVE 204
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALY-DWPE-RRTVLVIAHrlsTVERA----DQILVLD 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-198 |
1.55e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSI-----GKIE-----LTETK------H 70
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEffnqnIYERRvnlnrlR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 71 HPVGYMPQKDMLLPwRTIIENAALPLECQGVQKK-------EAQVKAKELLYKfgLQGYETKHPKDLSGGMRQRVSFIRT 143
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDE--IKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 144 LLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSN 198
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-188 |
1.86e-17 |
|
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: 76.81 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKH------HPvgYMPQ- 78
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDllflpqRP--YLPLg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 --KDMLL-PWRTIienaalplecqgvqkkeaqvkakellykfglqgyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:cd03223 79 tlREQLIyPWDDV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 447179532 156 PFSALDALTKASlqewLFEQWQEWEKTILFITH 188
Cdd:cd03223 118 ATSALDEESEDR----LYQLLKELGITVISVGH 146
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-170 |
2.09e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 9 FHNVSFHydekpiiheLNAsiheKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVGYMPQ------KDML 82
Cdd:PRK13539 18 FSGLSFT---------LAA----GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 83 LPWRTIIENAALPLECQGvqkkEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDA 162
Cdd:PRK13539 85 KPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
....*...
gi 447179532 163 LTKASLQE 170
Cdd:PRK13539 161 AAVALFAE 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-198 |
2.16e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 80.75 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKpiihelnasihekefVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETkhHPVGYMPQKDMLL 83
Cdd:TIGR03719 18 KEILKDISLSFFPGAK---------------IGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG--IKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRTIIENAALPL-ECQGVQKKEAQVKAK---------ELLYKFG-LQ-------GYETKH------------PKD---- 129
Cdd:TIGR03719 81 PTKTVRENVEEGVaEIKDALDRFNEISAKyaepdadfdKLAAEQAeLQeiidaadAWDLDSqleiamdalrcpPWDadvt 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 130 -LSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLfeqwQEWEKTILFITHDveeALFLSN 198
Cdd:TIGR03719 161 kLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD---RYFLDN 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-202 |
4.16e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.98 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 29 IHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTEtkhhpvgyMPQKDM-----------------LLPWR 86
Cdd:PRK15079 44 LYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkDLLG--------MKDDEWravrsdiqmifqdplasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 87 TIIENAALPLECQGVQKKEAQVK--AKELLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL 163
Cdd:PRK15079 116 TIGEIIAEPLRTYHPKLSRQEVKdrVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 447179532 164 TKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-202 |
4.22e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP----------VGYMPQKDMLLPWRTIIENAAL--- 94
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrsprdaialgIGMVHQHFMLVPNLTVAENIVLgle 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 95 PLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEP------------FSALDA 162
Cdd:COG3845 107 PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPtavltpqeadelFEILRR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447179532 163 LTKAslqewlfeqwqewEKTILFITHDVEEALFLSNRVLV 202
Cdd:COG3845 187 LAAE-------------GKSIIFITHKLREVMAIADRVTV 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-188 |
5.58e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTEtkhHPVGYMPQKDM--- 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG---QPIADYSEAALrqa 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 --LLPWR------TIIENAALPLEcqgvQKKEAQVkaKELLYKFGLQGY-ETKHPKD---------LSGGMRQRVSFIRT 143
Cdd:PRK11160 416 isVVSQRvhlfsaTLRDNLLLAAP----NASDEAL--IEVLQQVGLEKLlEDDKGLNawlgeggrqLSGGEQRRLGIARA 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447179532 144 LLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITH 188
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-205 |
6.05e-17 |
|
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: 76.94 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHP--------VGY 75
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgEDITGLPphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKA---------KELLYKFGlqgyetkhpKDLSGGMRQRVSFIRTLLT 146
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLErvyelfprlKERRRQRA---------GTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447179532 147 GGEILLLDEP------------FSALDALTKASLqewlfeqwqewekTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG0410 154 RPKLLLLDEPslglapliveeiFEIIRRLNREGV-------------TILLVEQNARFALEIADRAYVLER 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-200 |
6.66e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.46 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHY--DEKPIIHELNA---SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE-------LTETKHH 71
Cdd:TIGR03269 277 EPIIKVRNVSKRYisVDRGVVKAVDNvslEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 72 P---------VGYMPQKDMLLPWRTIIEN--AALPLEcqgVQKKEAQVKAKELLYKFGLQGYET-----KHPKDLSGGMR 135
Cdd:TIGR03269 357 PdgrgrakryIGILHQEYDLYPHRTVLDNltEAIGLE---LPDELARMKAVITLKMVGFDEEKAeeildKYPDELSEGER 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 136 QRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRV 200
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRA 498
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-229 |
8.72e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RSKNILQFHNVSFHYD--EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI----------ELTETK 69
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlldghdlrdyTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 HHpVGYMPQKDMLLPwRTIIENAALPleCQGVQKKEAQVKAKELLYKFGL-----QGYET---KHPKDLSGGMRQRVSFI 141
Cdd:PRK11176 417 NQ-VALVSQNVHLFN-DTIANNIAYA--RTEQYSREQIEEAARMAYAMDFinkmdNGLDTvigENGVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 142 RTLLTGGEILLLDEPFSALDALTKASLQEWLfEQWQEwEKTILFITH---DVEEAlflsNRVLVVEQQPITTLTERIVPL 218
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAAL-DELQK-NRTSLVIAHrlsTIEKA----DEILVVEDGEIVERGTHAELL 566
|
250
....*....|.
gi 447179532 219 DHNRTRKDLYK 229
Cdd:PRK11176 567 AQNGVYAQLHK 577
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-211 |
1.47e-16 |
|
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: 75.87 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 21 IIHELNASIHEKEFVSIIGPSGCGKST-----LFRLITGLEKVSiGKIELTETKHHP-------VGYMPQKDM--LLPWR 86
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaiLGLLPPGLTQTS-GEILLDGRPLLPlsirgrhIATIMQNPRtaFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 87 TIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYET---KHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL 163
Cdd:TIGR02770 80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447179532 164 TKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTL 211
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVmddgriVERGTVKEI 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-205 |
1.50e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYDEKPI--IHELNASIHEKEFVSIIGPSGCGKS----TLFRLITG-----------LEKVSIGKIELTETKHHPV 73
Cdd:PRK10261 19 NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQagglvqcdkmlLRRRSRQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQKDM----------LLPWRTIIENAALPLEC-QGVQKKEAQVKAKELLYKFGLQGYET---KHPKDLSGGMRQRVS 139
Cdd:PRK10261 99 RHVRGADMamifqepmtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 140 FIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-205 |
1.94e-16 |
|
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: 75.61 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKST----LFRLITGLE-KVSIGKIELTETKHHPV----GY 75
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVELSSgSILIDGVDISKIGLHDLrsriSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPwRTIIENAAlPL-ECQGVQKKEA--QVKAKELLYKF--GLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEI 150
Cdd:cd03244 83 IPQDPVLFS-GTIRSNLD-PFgEYSDEELWQAleRVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 151 LLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHDVeEALFLSNRVLVVEQ 205
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRL-DTIIDSDRILVLDK 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-164 |
2.56e-16 |
|
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: 75.39 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 18 EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG-LEKVSI--GKIELTETKHHP------VGYMPQKDMLLPWRTI 88
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTtsGQILFNGQPRKPdqfqkcVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 89 IE------NAALPLECQGVQKKeaQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDA 162
Cdd:cd03234 99 REtltytaILRLPRKSSDAIRK--KRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
..
gi 447179532 163 LT 164
Cdd:cd03234 177 FT 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-205 |
2.60e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.69 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RSKNILQFHNVSFHYDEK-PIIHELNASIHEKEFVSIIGPSGCGKSTLFRL-------------ITGLEkvsIGKIELTE 67
Cdd:PRK13657 330 RVKGAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLlqrvfdpqsgrilIDGTD---IRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 68 TKHHpVGYMPQKDMLLPwRTIIEN------AALPLECQGVQKKeAQvkAKELLYKfGLQGYET---KHPKDLSGGMRQRV 138
Cdd:PRK13657 407 LRRN-IAVVFQDAGLFN-RSIEDNirvgrpDATDEEMRAAAER-AQ--AHDFIER-KPDGYDTvvgERGRQLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 139 SFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITH---DVEEAlflsNRVLVVEQ 205
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHrlsTVRNA----DRILVFDN 544
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-216 |
3.22e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 10 HNVSFhydekpiihelnaSIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----------TETKHHPVGYMPQK 79
Cdd:COG1129 21 DGVSL-------------ELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrspRDAQAAGIAIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQG---VQKKEAQVKAKELLYKFGLQgyetKHP----KDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:COG1129 88 LNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLD----IDPdtpvGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 153 LDEPFSALDAltKASlqEWLFE---QWQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTLTE-RIV 216
Cdd:COG1129 164 LDEPTASLTE--REV--ERLFRiirRLKAQGVAIIYISHRLDEVFEIADRVTVlrdgrlVGTGPVAELTEdELV 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-215 |
4.14e-16 |
|
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: 77.03 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKvSIGKIELtetKHHPVGYMPQKDMLlPWR------------------TII 89
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRF---DGQDLDGLSRRALR-PLRrrmqvvfqdpfgslsprmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 90 ENAALPLECQGVQKKEAQVKAK--ELLYKFGLQGyETKH--PKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTK 165
Cdd:COG4172 383 QIIAEGLRVHGPGLSAAERRARvaEALEEVGLDP-AARHryPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQ 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 166 A-------SLQewlfeqwQEWEKTILFITHD--VEEAlfLSNRVLV------VEQQPittlTERI 215
Cdd:COG4172 462 AqildllrDLQ-------REHGLAYLFISHDlaVVRA--LAHRVMVmkdgkvVEQGP----TEQV 513
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-207 |
4.18e-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: 75.14 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKhhpVGYMPQK----------DMLlpwRTIIENAAlple 97
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---VSYKPQYikadyegtvrDLL---SSITKDFY---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 98 cqgvqkKEAQVKAkELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQ 177
Cdd:cd03237 91 ------THPYFKT-EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180 190
....*....|....*....|....*....|
gi 447179532 178 EWEKTILFITHDVEEALFLSNRVLVVEQQP 207
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIVFEGEP 193
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-203 |
7.69e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 7.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP---------VG 74
Cdd:PRK13647 3 NIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwvrskVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:PRK13647 83 LVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447179532 154 DEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVV 203
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVL 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-205 |
9.21e-16 |
|
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: 73.91 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 16 YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELT-------ETKH-HPVGY-MPQKDML---L 83
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvpwkrRKKFlRRIGVvFGQKTQLwwdL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PwrtIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL 163
Cdd:cd03267 111 P---VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447179532 164 TKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-193 |
9.24e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFR-------LITGLE---KVSIGKIELTETKHHPV-- 73
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRvegKVTFHGKNLYAPDVDPVev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 ----GYMPQKDMLLPwRTIIENAALplecqGVQKKEAQVKAKELLYKFGLQGYETKHPKD--------LSGGMRQRVSFI 141
Cdd:PRK14243 90 rrriGMVFQKPNPFP-KSIYDNIAY-----GARINGYKGDMDELVERSLRQAALWDEVKDklkqsglsLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447179532 142 RTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVEEA 193
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQA 213
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-208 |
1.32e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 75.52 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RSKNILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG----------LEKVSIGKIELTETK 69
Cdd:TIGR02203 326 RARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRfyepdsgqilLDGHDLADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 HHpVGYMPQKDMLLPwRTIIENAALPlecQGVQKKEAQVK-------AKELLYKF--GLQGYETKHPKDLSGGMRQRVSF 140
Cdd:TIGR02203 406 RQ-VALVSQDVVLFN-DTIANNIAYG---RTEQADRAEIEralaaayAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447179532 141 IRTLLTGGEILLLDEPFSALDALTKASLQEWLfEQWQEwEKTILFITH---DVEEAlflsNRVLVVEQQPI 208
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAAL-ERLMQ-GRTTLVIAHrlsTIEKA----DRIVVMDDGRI 545
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-191 |
1.39e-15 |
|
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: 73.13 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 20 PIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------ELTETKHHPVGYMPQKDMLLPwR 86
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeATRSRNRYSVAYAAQKPWLLN-A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 87 TIIENAAL--PLEcqgVQKKEAQVKAKEL-----LYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSA 159
Cdd:cd03290 94 TVEENITFgsPFN---KQRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190
....*....|....*....|....*....|...
gi 447179532 160 LDA-LTKASLQEWLFEQWQEWEKTILFITHDVE 191
Cdd:cd03290 171 LDIhLSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-216 |
1.68e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETK------------- 69
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqidai 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 --HHPVGYMPQKDMLLPWRTIIENAALPLECQGVQ-KKEAQVKAKELLYKFGLqgYETKHPK------DLSGGMRQRVSF 140
Cdd:PRK14246 87 klRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 141 IRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHDVEEA-------LFLSNRVLV-------VEQQ 206
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVarvadyvAFLYNGELVewgssneIFTS 242
|
250
....*....|
gi 447179532 207 PITTLTERIV 216
Cdd:PRK14246 243 PKNELTEKYV 252
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-175 |
2.34e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 17 DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI----------------ELTETKHHPvGYmpqKD 80
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhqDLLYLGHQP-GI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 MLLPWrtiiENAALPLECQGVQKKEAQVKAkelLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSAL 160
Cdd:PRK13538 88 ELTAL----ENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|....*
gi 447179532 161 DALTKASLQEwLFEQ 175
Cdd:PRK13538 161 DKQGVARLEA-LLAQ 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-205 |
2.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD-----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLE-----KVSIGKIELTETKHHP---- 72
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvptqgSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 ----VGYMPQ-KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLLT 146
Cdd:PRK13649 83 irkkVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 147 GGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEK 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-205 |
2.76e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.34 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RSKNILQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI---------------EL 65
Cdd:PRK13636 1 MEDYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 66 TETkhhpVGYMPQK-DMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTL 144
Cdd:PRK13636 81 RES----VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447179532 145 LTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-190 |
2.77e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 10 HNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTEtkhHPVGYMPQKDMLlpwRTIi 89
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG---LDVATTPSRELA---KRL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 90 enAALPLE--------------------CQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVsFI-RTLLTGG 148
Cdd:COG4604 78 --AILRQEnhinsrltvrelvafgrfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRA-FIaMVLAQDT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 149 EILLLDEPFSALD---------ALTKASlqewlfeqwQEWEKTILFITHDV 190
Cdd:COG4604 155 DYVLLDEPLNNLDmkhsvqmmkLLRRLA---------DELGKTVVIVLHDI 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-210 |
4.45e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.84 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKP-----IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEK-----VSIGKIELTETKHHP--- 72
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQptegkVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 -----VGYMPQ-KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLL 145
Cdd:PRK13643 81 pvrkkVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITT 210
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-202 |
4.57e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE--------LTETKHHP 72
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcarLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VG-YM-PQKDMLLPWRTIIENAALPLEcqgvQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEI 150
Cdd:PRK15439 86 LGiYLvPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 151 LLLDEPFSaldALTKASlQEWLFEQWQEWEKT---ILFITHDVEEALFLSNRVLV 202
Cdd:PRK15439 162 LILDEPTA---SLTPAE-TERLFSRIRELLAQgvgIVFISHKLPEIRQLADRISV 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-216 |
4.79e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRL------------ITG---LEKVSIGKIELTET 68
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGevyLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 69 KHHpVGYMPQKDMLLPWRTIIENAALPLECQGV--QKKEAQVKAKELLYKFGLQGyETKHPKD-----LSGGMRQRVSFI 141
Cdd:PRK14247 81 RRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWD-EVKDRLDapagkLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 142 RTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQewEKTILFITHDVEEALFLSNRVL------VVEQQPIT------ 209
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAflykgqIVEWGPTRevftnp 236
|
....*....
gi 447179532 210 --TLTERIV 216
Cdd:PRK14247 237 rhELTEKYV 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-211 |
5.86e-15 |
|
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: 73.57 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHN--VSFHYD--EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLekvsigkieLTETKHHPVGY- 75
Cdd:COG4172 1 MMSMPLLSVEDlsVAFGQGggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRL---------LPDPAAHPSGSi 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 ---------MPQKDM------------------LLPWRTIIENAALPLEC-QGVQKKEAQVKAKELLYKFGLQGYETK-- 125
Cdd:COG4172 72 lfdgqdllgLSERELrrirgnriamifqepmtsLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRld 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 126 -HPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHD---VEEalfLSNRVL 201
Cdd:COG4172 152 aYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVA 228
|
250
....*....|....*.
gi 447179532 202 V------VEQQPITTL 211
Cdd:COG4172 229 VmrqgeiVEQGPTAEL 244
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-204 |
8.19e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.04 E-value: 8.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHY------DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEltetkhhpVGYM 76
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY--------VDGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPWR------------------TIIE-NAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQR 137
Cdd:PRK13633 73 DTSDEENLWDirnkagmvfqnpdnqivaTIVEeDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 138 VSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALfLSNRVLVVE 204
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMD 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-216 |
8.32e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTET-----------KHhpVG 74
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlaRR--LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKdMLLP----WRTIIENAALP-LECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:PRK11231 80 LLPQH-HLTPegitVRELVAYGRSPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 150 ILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEA-------LFLSNRVLVVEQQPITTLTERIV 216
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMR-LMRELNTQGKTVVTVLHDLNQAsrycdhlVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-189 |
8.57e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 37 IIGPSGCGKSTLFRLITGLEKVSIGkieltETKHHP---VGYMPQKDMLLPWRTIIENAAlplecQGVQ-KKEAQVKAKE 112
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG-----EARPAPgikVGYLPQEPQLDPEKTVRENVE-----EGVAeVKAALDRFNE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 113 LLYKFG---------------LQ-------GYETKH------------PKD-----LSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:PRK11819 108 IYAAYAepdadfdalaaeqgeLQeiidaadAWDLDSqleiamdalrcpPWDakvtkLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 447179532 154 DEPFSALDALTKAslqeWLfEQW-QEWEKTILFITHD 189
Cdd:PRK11819 188 DEPTNHLDAESVA----WL-EQFlHDYPGTVVAVTHD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-242 |
9.18e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 9.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHhpVGYMPQKDMLlp 84
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR--IGYVPQKLYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 85 wrtiieNAALPLECQ-------GVQKKE-----AQVKAKELLykfglqgyetKHP-KDLSGGMRQRVSFIRTLLTGGEIL 151
Cdd:PRK09544 79 ------DTTLPLTVNrflrlrpGTKKEDilpalKRVQAGHLI----------DAPmQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 152 LLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTLTerivpldhnrtrkdlykPE 231
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGT-----------------PE 205
|
250
....*....|.
gi 447179532 232 VLALKDELLSM 242
Cdd:PRK09544 206 VVSLHPEFISM 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-162 |
9.65e-15 |
|
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: 73.44 E-value: 9.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFR-LITGLEKVSiGKIELTETkhhpVGYMPQKdm 81
Cdd:TIGR00957 635 NSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHMKGS----VAYVPQQ-- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 llPWrtiIENAAL--------PLE---CQGVQKKEAQVKAKELL-----YKFGLQGYetkhpkDLSGGMRQRVSFIRTLL 145
Cdd:TIGR00957 708 --AW---IQNDSLrenilfgkALNekyYQQVLEACALLPDLEILpsgdrTEIGEKGV------NLSGGQKQRVSLARAVY 776
|
170
....*....|....*..
gi 447179532 146 TGGEILLLDEPFSALDA 162
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDA 793
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-205 |
9.77e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILqFHNVSFHYDEKP-----IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIG--------------KI 63
Cdd:PRK13645 4 SKDII-LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyaipanlkKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 64 ELTETKHHPVGYMPQ-KDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGL-QGYETKHPKDLSGGMRQRVSFI 141
Cdd:PRK13645 83 KEVKRLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 142 RTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-203 |
1.15e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTetkhhpvgympqkd 80
Cdd:COG2401 25 ERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 mlLPWRTIIENAALpLECqgVQKKEAQVKAKELLYKFGL---QGYETKhPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:COG2401 91 --VPDNQFGREASL-IDA--IGRKGDFKDAVELLNAVGLsdaVLWLRR-FKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447179532 158 SALDALTKASLQEWLFEQWQEWEKTILFITH--DVEEALFlSNRVLVV 203
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQ-PDLLIFV 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-224 |
1.52e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.92 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 37 IIGPSGCGKSTLFRLITGLEKVSIGkiELTETKHHPVGYMPQKDMLL----------------PWRTIIENAALPLECQ- 99
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPTGG--ELYYQGQDLLKADPEAQKLLrqkiqivfqnpygslnPRKKVGQILEEPLLINt 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 100 GVQKKEAQVKAKELLYKFGLQgyeTKH----PKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQ 175
Cdd:PRK11308 124 SLSAAERREKALAMMAKVGLR---PEHydryPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 176 WQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTLTERivPLdHNRTR 224
Cdd:PRK11308 201 QQELGLSYVFISHDLSVVEHIADEVMVmylgrcVEKGTKEQIFNN--PR-HPYTQ 252
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-192 |
1.72e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 16 YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEK----VSIGKIELTETKHHP-------VGYMPQkdmlLP 84
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgsLKINGIELRELDPESwrkhlswVGQNPQ----LP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 85 WRTIIENAAL---PLECQGVQKKEAQVKAKELLYKFGlQGYETKhPKD----LSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:PRK11174 436 HGTLRDNVLLgnpDASDEQLQQALENAWVSEFLPLLP-QGLDTP-IGDqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190
....*....|....*....|....*....|....*
gi 447179532 158 SALDALTKASLQEWLFEQWQewEKTILFITHDVEE 192
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASR--RQTTLMVTHQLED 546
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-203 |
1.90e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 9 FHNVSFhydekpiihelnaSIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP----------VGYMP- 77
Cdd:COG1129 268 VRDVSF-------------SVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagIAYVPe 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 --QKDMLLPWRTIIENAALP----LECQGV--QKKEAQVkAKELLYKFGLQgyeTKHPKD----LSGGMRQRVSFIRTLL 145
Cdd:COG1129 335 drKGEGLVLDLSIRENITLAsldrLSRGGLldRRRERAL-AEEYIKRLRIK---TPSPEQpvgnLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVV 203
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVM 467
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-193 |
2.06e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL--TETKHHPVGYMPQKDMLLP 84
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 85 wrtiiENAALPLECQgVQ-----------------KKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTG 147
Cdd:PRK10253 88 -----QNATTPGDIT-VQelvargryphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447179532 148 GEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEA 193
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQA 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-168 |
2.12e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.00 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 18 EKPIIHELNASIHEKEFVSIIGPSGCGKSTL-----FRLITGLEK---VSIGKIELTETKHHPV-GYMPQKDMLLPWRTI 88
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLmnalaFRSPKGVKGsgsVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 89 IEN----AALPLECQgVQKKEAQVKAKELLYKFGLQ-------GYETKHpKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:TIGR00955 117 REHlmfqAHLRMPRR-VTKKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170
....*....|.
gi 447179532 158 SALDALTKASL 168
Cdd:TIGR00955 195 SGLDSFMAYSV 205
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-161 |
2.34e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtETKHHP-------V 73
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATrgdrsrfM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQKDMLLPWRTIIENaaLPLECqGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:PRK13543 85 AYLGHLPGLKADLSTLEN--LHFLC-GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
....*...
gi 447179532 154 DEPFSALD 161
Cdd:PRK13543 162 DEPYANLD 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-201 |
2.65e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.85 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHhpVGYMPQ----- 78
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN--IGYYAQdhayd 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 --KDMLL-----PWRTIIENaalplecqgvqkkEAQVKAK--ELLykFGlQGYETKHPKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:PRK15064 395 feNDLTLfdwmsQWRQEGDD-------------EQAVRGTlgRLL--FS-QDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447179532 150 ILLLDEPFSALDALTKASLQEWLfeqwQEWEKTILFITHDVEEALFLSNRVL 201
Cdd:PRK15064 459 VLVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRII 506
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-204 |
5.47e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.14 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETK-----HHPV 73
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkDITDWQtakimREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQKDMLLPWRTIIENAALplecQGVQKKEAQVKAK-ELLYKFGLQGYETKHPK--DLSGGMRQRVSFIRTLLTGGEI 150
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAM----GGFFAERDQFQERiKWVYELFPRLHERRIQRagTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447179532 151 LLLDEPFSALDALTKASLQEWLfEQWQEWEKTILFITHDVEEALFLSNRVLVVE 204
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTI-EQLREQGMTIFLVEQNANQALKLADRGYVLE 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-200 |
6.67e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RS-KNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIElTETKHHpVGYMPQ-K 79
Cdd:PRK11147 314 RSgKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLE-VAYFDQhR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAAlplecQGvqKKEAQVKAKE---LLYkfgLQGYeTKHPKD-------LSGGMRQRVSFIRTLLTGGE 149
Cdd:PRK11147 392 AELDPEKTVMDNLA-----EG--KQEVMVNGRPrhvLGY---LQDF-LFHPKRamtpvkaLSGGERNRLLLARLFLKPSN 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 150 ILLLDEPFSALDALTKASLQEWLfeqwQEWEKTILFITHDVEealFLSNRV 200
Cdd:PRK11147 461 LLILDEPTNDLDVETLELLEELL----DSYQGTVLLVSHDRQ---FVDNTV 504
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-208 |
6.84e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.42 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYD-----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTE-TKHHPVgympqKD 80
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKT-----KD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 MLLpwRTIIENAALPL---ECQ-----------------GVQKKEAQVKAKELLYKFGL-QGYETKHPKDLSGGMRQRVS 139
Cdd:PRK13646 78 KYI--RPVRKRIGMVFqfpESQlfedtvereiifgpknfKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 140 FIRTLLTGGEILLLDEPFSALDALTKASLQEwLFEQWQEWE-KTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMR-LLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-216 |
1.60e-13 |
|
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: 67.93 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI--ELTETKHHPVGYMPQKD--- 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyIMRSGAELELYQLSEAErrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 -MLLPWRTIIENAALPLECQgvqkKEAQVKAKELLYKFGLQGY----ETKH----------------PKDLSGGMRQRVS 139
Cdd:TIGR02323 83 lMRTEWGFVHQNPRDGLRMR----VSAGANIGERLMAIGARHYgnirATAQdwleeveidptriddlPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 140 FIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI--TTLTERIV 216
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVveSGLTDQVL 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-246 |
1.90e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 33 EFVSIIGPSGCGKSTLFRLITGLEKVSIGKI--------ELTETKHHPVgympQKDM----------LLPWRTIIENAAL 94
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqridTLSPGKLQAL----RRDIqfifqdpyasLDPRQTVGDSIME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 95 PLECQGV-QKKEAQVKAKELLYKFGLQG-YETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWL 172
Cdd:PRK10261 427 PLRVHGLlPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 173 FEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTLTERIVPLD---HNRTRKDL----------YKPEVLALKDEL 239
Cdd:PRK10261 507 LDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEnpqHPYTRKLMaavpvadpsrQRPQRVLLSDDL 586
|
....*..
gi 447179532 240 LSMLQRQ 246
Cdd:PRK10261 587 PSNIHLR 593
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-207 |
2.15e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 29 IHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETkhhpVGYMPQKdmllpwrtiIENAalplECQGVQKKEAQV 108
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----ISYKPQY---------IKPD----YDGTVEDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 109 KAK--------ELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD-----ALTKA--SLQEwlf 173
Cdd:PRK13409 425 TDDlgssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlAVAKAirRIAE--- 501
|
170 180 190
....*....|....*....|....*....|....
gi 447179532 174 eqwqEWEKTILFITHDVEEALFLSNRVLVVEQQP 207
Cdd:PRK13409 502 ----EREATALVVDHDIYMIDYISDRLMVFEGEP 531
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-202 |
2.82e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 22 IHELNASIHEKEFVSIIGPSGCGKS-TLFRLI---------------TGLEKVSIGKIELTETKHHPVGYMPQKDM--LL 83
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqTAFALMgllaangriggsatfNGREILNLPEKELNKLRAEQISMIFQDPMtsLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PWRTIIENAA--LPLEcQGVQKKEA---------QVKAKELLYKFGLqgyetkHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:PRK09473 112 PYMRVGEQLMevLMLH-KGMSKAEAfeesvrmldAVKMPEARKRMKM------YPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-210 |
3.44e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKP-----IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPvGYMPQKD 80
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD-KKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 MLLPWRTIIENAA-----------LPlECQ-----------------GVQKKEAQVKAKELLYKFGLQ-GYETKHPKDLS 131
Cdd:PRK13631 100 ITNPYSKKIKNFKelrrrvsmvfqFP-EYQlfkdtiekdimfgpvalGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 132 GGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVVEQQPITT 210
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-170 |
3.59e-13 |
|
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: 66.36 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 17 DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVGYMPQKDML-LPWRTIIENAALP 95
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLyLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 96 LE-CQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQE 170
Cdd:cd03231 91 LEnLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-193 |
6.41e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGlekvsigkieltetkHHPVGYmpQKDMLLP 84
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG---------------DHPQGY--SNDLTLF 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 85 WR------TIIE--------NAALPLE---------------------CQGVQKKEaQVKAKELLYKFGLQGYETKHP-K 128
Cdd:PRK10938 322 GRrrgsgeTIWDikkhigyvSSSLHLDyrvstsvrnvilsgffdsigiYQAVSDRQ-QKLAQQWLDILGIDKRTADAPfH 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 129 DLSGGmRQRVSFI-RTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEA 193
Cdd:PRK10938 401 SLSWG-QQRLALIvRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-205 |
6.68e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 17 DEKPIIHELNASIHEKEFVSIIGPSGCGKST----LFRLITglekvSIGKIELtetKHHPVGYMPQKDMLlPWRTIIE-- 90
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWF---DGQPLHNLNRRQLL-PVRHRIQvv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 91 ----NAAL-------PLECQGVQ---------KKEAQVKakELLYKFGLQGyETKH--PKDLSGGMRQRVSFIRTLLTGG 148
Cdd:PRK15134 368 fqdpNSSLnprlnvlQIIEEGLRvhqptlsaaQREQQVI--AVMEEVGLDP-ETRHryPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 149 EILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-207 |
8.58e-13 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 64.52 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 29 IHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKhhpVGYMPQKdmllpwrtiienaalplecqgvqkkeaqv 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT---PVYKPQY----------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 109 kakellykfglqgyetkhpKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITH 188
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEH 130
|
170
....*....|....*....
gi 447179532 189 DVEEALFLSNRVLVVEQQP 207
Cdd:cd03222 131 DLAVLDYLSDRIHVFEGEP 149
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-190 |
9.25e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 36 SIIGPSGCGKSTLFRLITGLEKVSIGKIELTET------KHHPVGYMPQK---DMLLPwrTIIENAAL-----PLECQGV 101
Cdd:PRK15056 37 ALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalQKNLVAYVPQSeevDWSFP--VLVEDVVMmgrygHMGWLRR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 102 QKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEwEK 181
Cdd:PRK15056 115 AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GK 193
|
....*....
gi 447179532 182 TILFITHDV 190
Cdd:PRK15056 194 TMLVSTHNL 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-205 |
1.06e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.04 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 13 SFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTEtkhhpvgyMPQKDMLL-PWR--- 86
Cdd:PRK10789 320 QFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD--------IPLTKLQLdSWRsrl 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 87 ------------TIIENAALplECQGVQKKEAQVKAK-----ELLYKFGlQGYETKHPKD---LSGGMRQRVSFIRTLLT 146
Cdd:PRK10789 392 avvsqtpflfsdTVANNIAL--GRPDATQQEIEHVARlasvhDDILRLP-QGYDTEVGERgvmLSGGQKQRISIARALLL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 147 GGEILLLDEPFSALDALTKASLQEWLfEQWQEwEKTILFITHDVeEALFLSNRVLVVEQ 205
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNL-RQWGE-GRTVIISAHRL-SALTEASEILVMQH 524
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-205 |
1.16e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 15 HYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP----VGYMPqkDMllpwrTIIE 90
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALlelgAGFHP--EL-----TGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 91 NAALPLECQGVQKKEAQVKAKELLyKF-GLQGYEtKHP-KDLSGGMRQRVSF-IRTLLTgGEILLLDEPFSALDALTKAS 167
Cdd:COG1134 108 NIYLNGRLLGLSRKEIDEKFDEIV-EFaELGDFI-DQPvKTYSSGMRARLAFaVATAVD-PDILLVDEVLAVGDAAFQKK 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 447179532 168 LQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:COG1134 185 CLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-203 |
2.13e-12 |
|
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: 66.58 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHYD--EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVS------IGKIELTETK--HHPVG 74
Cdd:TIGR01257 1936 DILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTsgdatvAGKSILTNISdvHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447179532 155 EPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVV 203
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-207 |
2.91e-12 |
|
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: 65.58 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETkhhpVGYMPQK---DMLLPWRTIIENAALPlecqGVQKK 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK----ISYKPQYispDYDGTVEEFLRSANTD----DFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 105 EAQVkakELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD-----ALTKA--SLQEwlfeqwq 177
Cdd:COG1245 434 YYKT---EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlAVAKAirRFAE------- 503
|
170 180 190
....*....|....*....|....*....|
gi 447179532 178 EWEKTILFITHDVEEALFLSNRVLVVEQQP 207
Cdd:COG1245 504 NRGKTAMVVDHDIYLIDYISDRLMVFEGEP 533
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-209 |
3.29e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.44 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHYD-EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-----ELTETKHHPVGYM-- 76
Cdd:PRK13652 2 HLIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgePITKENIREVRKFvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 -----PQKDMLLPwrTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEIL 151
Cdd:PRK13652 82 lvfqnPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 152 LLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPIT 209
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-211 |
3.70e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL-EKVS---------IGKIELTETK-----HHPVGY 75
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrysgdvlLGGRSIFNYRdvlefRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQKDMLLPwRTIIENAALPLECQG-VQKKEAQVKAKELLYKFGL----QGYETKHPKDLSGGMRQRVSFIRTLLTGGEI 150
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 151 LLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVEEALFLSNRVL------VVEQQPITTL 211
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAAlffdgrLVEEGPTEQL 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-161 |
6.43e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL---------TETKHHPVGYMPQKDM 81
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 L---LPWRTIIENAALPLECQGVQKKEAQVKA-KELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:PRK09536 88 LsfeFDVRQVVEMGRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
....
gi 447179532 158 SALD 161
Cdd:PRK09536 168 ASLD 171
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-162 |
1.19e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 18 EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG-------LEKVSIGKIELTETKHHPVGYMPQKDMLLPWRTIIE 90
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriqgnnfTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 91 N---AALPLECQGVQKKEAQVKAKELLYKFGLQGYET-----KHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDA 162
Cdd:PLN03211 160 TlvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-205 |
1.75e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.58 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY-DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----TETKHHPV----GYMP 77
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrpLSSLSHSVlrqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPWRTIIENAALPLEC--QGVQKKEAQVKAKELLYKF--GLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDIseEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 154 DEPFSALDALTKASLQEWLFEQWQewEKTILFITH------DVEEALFLsNRVLVVEQ 205
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHrlstivEADTILVL-HRGQAVEQ 555
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
2.02e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE--LTETKHHPVGYMPQ 78
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 KDMLLPWRT----IIENAAlplecQGVQkkeAQVKA----KELLYKFGLQGYET--------------------KHPKDL 130
Cdd:PRK11701 81 AERRRLLRTewgfVHQHPR-----DGLR---MQVSAggniGERLMAVGARHYGDiratagdwlerveidaaridDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 131 SGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI-- 208
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVve 232
|
250
....*....|.
gi 447179532 209 TTLTERIvpLD 219
Cdd:PRK11701 233 SGLTDQV--LD 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-224 |
2.04e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDeKPIIHELNASIHEKEFVSIIGPSGCGKS-----TLFRLITGLEKVSiGKIELTETKHHP-------VG 74
Cdd:PRK10418 5 IELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQTA-GRVLLDGKPVAPcalrgrkIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQ--KDMLLPWRTIIENAALPLECQGVQKKEAQVKAkeLLYKFGLQGYET---KHPKDLSGGMRQRVSFIRTLLTGGE 149
Cdd:PRK10418 83 TIMQnpRSAFNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 150 ILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTLTERivPlDHNRT 223
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVmshgriVEQGDVETLFNA--P-KHAVT 237
|
.
gi 447179532 224 R 224
Cdd:PRK10418 238 R 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-205 |
2.13e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 16 YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEltetkhhpV-GYMPQKDmllpwRtiIENAA- 93
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR--------VlGYVPFKR-----R--KEFARr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 94 --------------LPL--------ECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEIL 151
Cdd:COG4586 97 igvvfgqrsqlwwdLPAidsfrllkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 152 LLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITH---DVEEalfLSNRVLVVEQ 205
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHdmdDIEA---LCDRVIVIDH 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-193 |
3.89e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.07 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHY-DEKP---IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL----EKVSIGKIE--------LTETK 69
Cdd:PRK11022 3 LLNVDKLSVHFgDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEfngqdlqrISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 HHP-----VGYMPQKDM--LLPWRT----IIEnaALPLEcQGVQKKEAQVKAKELLYKFGLQGYETK---HPKDLSGGMR 135
Cdd:PRK11022 83 RRNlvgaeVAMIFQDPMtsLNPCYTvgfqIME--AIKVH-QGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447179532 136 QRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHD---VEEA 193
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-212 |
4.99e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDE-----KPIihelNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTE---TKHHPVGYMPQ 78
Cdd:PRK10522 323 LELRNVTFAYQDngfsvGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpvTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 -----KDMLLPWRTiienaalpLECQGVQKKEAQVKA----KELLYKFGLQGYETKHPKdLSGGMRQRVSFIRTLLTGGE 149
Cdd:PRK10522 399 fsavfTDFHLFDQL--------LGPEGKPANPALVEKwlerLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 150 ILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDveEALFLS-NRVLVVEQQPITTLT 212
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD--DHYFIHaDRLLEMRNGQLSELT 531
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-205 |
7.05e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 14 FHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL------------EKVSIGKIELTETKHHPVGYMPQKDM 81
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlrpqkgavlwqgKPLDYSKRGLLALRQQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 82 LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447179532 162 ALTKASLQEWLFEQWQEWEKTILfITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQ 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
5-205 |
7.21e-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: 60.64 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 5 NILQFHNVSFHYDekPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIeltetKHH-PVGYMPQKDMLL 83
Cdd:cd03291 38 NNLFFSNLCLVGA--PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHSgRISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PwRTIIENAALPLECQGVQKKEAqVKAKEL---LYKFGLQGYET--KHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:cd03291 111 P-GTIKENIIFGVSYDEYRYKSV-VKACQLeedITKFPEKDNTVlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447179532 159 ALDALTKASLQEWLFEQWQEwEKTILFITHDVEEaLFLSNRVLVVEQ 205
Cdd:cd03291 189 YLDVFTEKEIFESCVCKLMA-NKTRILVTSKMEH-LKKADKILILHE 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-161 |
8.27e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 38 IGPSGCGKSTLFRLITGLEKVSIGKIEL---------TETKHHpVGYMPQKDMLLPWRTIIENaaLPLECQ--GVQKKEA 106
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdagdIATRRR-VGYMSQAFSLYGELTVRQN--LELHARlfHLPAAEI 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 107 QVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:NF033858 375 AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
127-211 |
1.38e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 127 PKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV---- 202
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVmqng 233
|
90
....*....|.
gi 447179532 203 --VEQQPITTL 211
Cdd:PRK15134 234 rcVEQNRAATL 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-188 |
1.82e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.58 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKSTL----FRLI---TG---LEKVSIGKIELTETKHHpVG 74
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLeaeEGkieIDGIDISTIPLEDLRSS-LT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPwRTIIENAALPLECQGVQKKEAqVKAKEllykFGLqgyetkhpkDLSGGMRQRVSFIRTLLTGGEILLLD 154
Cdd:cd03369 86 IIPQDPTLFS-GTIRSNLDPFDEYSDEEIYGA-LRVSE----GGL---------NLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|....
gi 447179532 155 EPFSALDALTKASLQEWLFEQWQewEKTILFITH 188
Cdd:cd03369 151 EATASIDYATDALIQKTIREEFT--NSTILTIAH 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-188 |
1.90e-10 |
|
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: 58.69 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSI--GKIELtetKHHPVGYMP-----QK 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILF---KGEDITDLPpeeraRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTiienaalPLECQGvqkkeaqVKAKELL----YKFglqgyetkhpkdlSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:cd03217 78 GIFLAFQY-------PPEIPG-------VKNADFLryvnEGF-------------SGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|...
gi 447179532 156 PFSALDaLTKASLQEWLFEQWQEWEKTILFITH 188
Cdd:cd03217 131 PDSGLD-IDALRLVAEVINKLREEGKSVLIITH 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-170 |
4.22e-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: 59.54 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYdeKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIeltetKHHP-VGYMPQKDMLLPw 85
Cdd:TIGR01271 429 LFFSNFSLYV--TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHSGrISFSPQTSWIMP- 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 RTIIENAALplecqGVQKKEAQ----VKAKELLYKFGLQGYETKHPK-----DLSGGMRQRVSFIRTLLTGGEILLLDEP 156
Cdd:TIGR01271 501 GTIKDNIIF-----GLSYDEYRytsvIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
170
....*....|....
gi 447179532 157 FSALDALTKASLQE 170
Cdd:TIGR01271 576 FTHLDVVTEKEIFE 589
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-242 |
4.62e-10 |
|
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: 59.05 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKV---------------SIGKIELTETKHH 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYeptsgriiyhvalceKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 72 P-----------------------------VGYMPQKDM-LLPWRTIIENAALPLECQGVQKKEAQVKAKELLYKFGLQG 121
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlsdklrrrirkrIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 122 YETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITH-------DVEEAL 194
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpeviedLSDKAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447179532 195 FLSNRVLVVEQQPITTLTERIvpldhnRTRKDLYKPEVLALKDELLSM 242
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFM------EGVSEVEKECEVEVGEPIIKV 282
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-164 |
5.48e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTE--------TKHHPVGYMP 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlcTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLPWRTIIENAALPLecqgvQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDI-----HFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
....*..
gi 447179532 158 SALDALT 164
Cdd:PRK13540 156 VALDELS 162
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-204 |
6.34e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHY--DEKPIIHELNASIHEKEFVSIIGPSGCGKS----TLFRLITgLEK-------VSIGKIELTETK 69
Cdd:PLN03130 1234 SSGSIKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIVE-LERgrilidgCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 HHpVGYMPQKDMLLPwRTIIENAALPLECQGVQKKEAQVKA--KELLYK--FGLQGYETKHPKDLSGGMRQRVSFIRTLL 145
Cdd:PLN03130 1313 KV-LGIIPQAPVLFS-GTVRFNLDPFNEHNDADLWESLERAhlKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVeEALFLSNRVLVVE 204
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSC--TMLIIAHRL-NTIIDCDRILVLD 1446
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-164 |
6.71e-10 |
|
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: 56.89 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 17 DEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL--EKVSI-GKI--------ELTETKHHPVGYMPQKDMLLPW 85
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSVeGDIhyngipykEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 86 RTIIENAALPLECQGVQKkeaqvkakellykfgLQGyetkhpkdLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALT 164
Cdd:cd03233 98 LTVRETLDFALRCKGNEF---------------VRG--------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-192 |
8.71e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 22 IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEltetKHHPVGYMPQKDMLLPWRTIIENAALPLECQGV 101
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD----RNGEVSVIAISAGLSGQLTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 102 QKKEAQVKAKELLyKFGLQGYETKHP-KDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD-ALTKASLQEwlFEQWQEW 179
Cdd:PRK13546 116 KRKEIKAMTPKII-EFSELGEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQKCLDK--IYEFKEQ 192
|
170
....*....|...
gi 447179532 180 EKTILFITHDVEE 192
Cdd:PRK13546 193 NKTIFFVSHNLGQ 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-204 |
9.27e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 3 SKNILQFHNVSFHYDEK--PIIHELNASIHEKEFVSIIGPSGCGKST----LFRLITgLEK-------VSIGKIELTETK 69
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVE-LEKgrimiddCDVAKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 70 HhPVGYMPQKDMLLPwRTIIENAALPLECQGVQKKEAQVKA--KELLYK--FGLQGYETKHPKDLSGGMRQRVSFIRTLL 145
Cdd:PLN03232 1310 R-VLSIIPQSPVLFS-GTVRFNIDPFSEHNDADLWEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 146 TGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVeEALFLSNRVLVVE 204
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSC--TMLVIAHRL-NTIIDCDKILVLS 1443
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-161 |
3.40e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNI--LQFHNVSFHYDEKP---IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKH-------- 70
Cdd:PTZ00265 378 KDIkkIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlkdinlkw 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 71 --HPVGYMPQkDMLLPWRTIIENAALPL--------------------------------ECQGV--------------- 101
Cdd:PTZ00265 458 wrSKIGVVSQ-DPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDlndmsnttdsnelie 536
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 102 QKKEAQ---------VKAKELLYKF--GL-QGYET---KHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:PTZ00265 537 MRKNYQtikdsevvdVSKKVLIHDFvsALpDKYETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-161 |
1.08e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHE-LNASIHEKEFVSIIGPSGCGKSTLFRLITG-LEKVS-----IGKIELTE-TKHHPVGYMP 77
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKnLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSgtvfrSAKVRMAVfSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 78 QKDMLLpwrtiienaaLPLEC-QGVQKKeaqvKAKELLYKFGLQGYETKHPK-DLSGGMRQRVSFIRTLLTGGEILLLDE 155
Cdd:PLN03073 588 SSNPLL----------YMMRCfPGVPEQ----KLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
....*.
gi 447179532 156 PFSALD 161
Cdd:PLN03073 654 PSNHLD 659
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-172 |
1.59e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.69 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 25 LNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSiGKIELTET--KHHPV-------GYMPQKDMLLPWRTIIENAALP 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRplSDWSAaelarhrAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 96 LECQGVQKKEAQVKAkELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLT-------GGEILLLDEPFSALDALTKASL 168
Cdd:COG4138 94 QPAGASSEAVEQLLA-QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAAL 172
|
....
gi 447179532 169 QEWL 172
Cdd:COG4138 173 DRLL 176
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-212 |
1.99e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 26 NASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTET-------KHHPVGYMPQKDML---------LPWRTII 89
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnQETPALPQPALEYVidgdreyrqLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 90 EN--------AALPLECQGVQKKEAQVKAKELLYKFGLQGYETKHP-KDLSGGMRQRVSFIRTLLTGGEILLLDEPFSAL 160
Cdd:PRK10636 101 ANerndghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447179532 161 DALTKASLQEWLfeqwQEWEKTILFITHDVEEALFLSNRVLVVEQQPITTLT 212
Cdd:PRK10636 181 DLDAVIWLEKWL----KSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYT 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-202 |
2.28e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----------TETKHHPVGYM 76
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrfastTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPWRTIIEN---AALPLECQGVQKKEAQVKAKELLYKFGLQ-GYETKhPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:PRK11288 85 YQELHLVPEMTVAENlylGQLPHKGGIVNRRLLNYEAREQLEHLGVDiDPDTP-LKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447179532 153 LDEPFSALDALTkaslQEWLF---EQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:PRK11288 164 FDEPTSSLSARE----IEQLFrviRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-193 |
3.00e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.87 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETK---------HHP 72
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VGYMPQKdmlLP---WRTIIENAAL-------PLECQGVQKKEaqvKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIR 142
Cdd:PRK10575 87 VAYLPQQ---LPaaeGMTVRELVAIgrypwhgALGRFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447179532 143 TLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEA 193
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMA 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
101-205 |
4.45e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.82 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 101 VQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKAslqewlfEQWQEWE 180
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN-------EVWDEVR 188
|
90 100 110
....*....|....*....|....*....|.
gi 447179532 181 K------TILFITHDVEEALFLSNRVLVVEQ 205
Cdd:NF000106 189 SmvrdgaTVLLTTQYMEEAEQLAHELTVIDR 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-205 |
6.06e-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: 53.03 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDE--KPIIHELNASIHEKEFVSIIGPSGCGKST----LFRLITGLE------KVSIGKIELTETKHHpVG 74
Cdd:TIGR00957 1285 VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAEgeiiidGLNIAKIGLHDLRFK-IT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 75 YMPQKDMLLPwrtiiENAALPLECQGVQKKEAQVKAKELLYkfgLQGYETKHP-----------KDLSGGMRQRVSFIRT 143
Cdd:TIGR00957 1364 IIPQDPVLFS-----GSLRMNLDPFSQYSDEEVWWALELAH---LKTFVSALPdkldhecaeggENLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 144 LLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVEEALFLSnRVLVVEQ 205
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDK 1494
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
14-192 |
6.54e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 14 FHYdekpIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETkhhpVGYMPQKDMLLPWRTIIENAA 93
Cdd:PRK13545 36 YHY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----AALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 94 LPLECQGVQKKEAQVKAKELLyKFGLQGYETKHP-KDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD-ALTKASLQEw 171
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEII-EFADIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDK- 185
|
170 180
....*....|....*....|.
gi 447179532 172 lFEQWQEWEKTILFITHDVEE 192
Cdd:PRK13545 186 -MNEFKEQGKTIFFISHSLSQ 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-240 |
6.78e-08 |
|
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: 52.52 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL------------EKVSIGKIELTETKHHPV 73
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgeiywSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 74 GYMPQKDMLLPWRTIIENAALPLECQ---GVQKKEAQV-KAKELLYKFGLQGYETKHP-KDLSGGMRQRVSFIRTLLTGG 148
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITlpgGRMAYNAMYlRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 149 EILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTLTE-RIVPLDHN 221
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLD-IIRDLKAHGVACVYISHKLNEVKAVCDTICVirdgqhVATKDMSTMSEdDIITMMVG 239
|
250
....*....|....*....
gi 447179532 222 RTRKDLYKPEVLALKDELL 240
Cdd:TIGR02633 240 REITSLYPHEPHEIGDVIL 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-202 |
7.87e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 4 KNILQFHNVSFH-YDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTE---TKHHP------- 72
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGediTGLSPrerrrlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VGYMP---QKDMLLPWRTIIENAAL------PLECQG-VQKKEAQVKAKELLYKFGL--QGYETKhPKDLSGGMRQRVSF 140
Cdd:COG3845 335 VAYIPedrLGRGLVPDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIEEFDVrtPGPDTP-ARSLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 141 IRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLV 202
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAV 474
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-216 |
8.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYD---EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG-LEKVSIGKIELTETkhhpVGYMPQkdmlLPW- 85
Cdd:PLN03232 619 NGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS----VAYVPQ----VSWi 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 --RTIIENAALPLECQGVQKKEAqVKAKELLYKFGL-QGYET----KHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:PLN03232 691 fnATVRENILFGSDFESERYWRA-IDVTALQHDLDLlPGRDLteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 159 ALDaltkASLQEWLFEQWqewektilfithdVEEALFLSNRVLVVEQQPITTLTERIV 216
Cdd:PLN03232 770 ALD----AHVAHQVFDSC-------------MKDELKGKTRVLVTNQLHFLPLMDRII 810
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-171 |
1.11e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIE-----LTETKH-----HPVGY 75
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARHrravcPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 76 MPQ---KDmLLPWRTIIEN----AALplecQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGG 148
Cdd:NF033858 81 MPQglgKN-LYPTLSVFENldffGRL----FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180
....*....|....*....|...
gi 447179532 149 EILLLDEPFSALDALTKAslQEW 171
Cdd:NF033858 156 DLLILDEPTTGVDPLSRR--QFW 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-222 |
1.55e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 14 FHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIeLTEtkhHPVGYMPQKdmllPW------RT 87
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAE---RSIAYVPQQ----AWimnatvRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 88 II-----ENAALPLECQGVQKKEAQVK--AKELLYKFGLQGYetkhpkDLSGGMRQRVSFIRTLLTGGEILLLDEPFSAL 160
Cdd:PTZ00243 740 NIlffdeEDAARLADAVRVSQLEADLAqlGGGLETEIGEKGV------NLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447179532 161 DAltkaslqewlfeqwqewektilFITHDVEEALFL-----SNRVLVVEQQPITTLTERIVPLDHNR 222
Cdd:PTZ00243 814 DA----------------------HVGERVVEECFLgalagKTRVLATHQVHVVPRADYVVALGDGR 858
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-204 |
1.83e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 25 LNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHP----------VGYMPQKDMLLPWRTIIEN--- 91
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhklaaqlgIGIIYQELSVIDELTVLENlyi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 92 AALPLE----CQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSaldALTKAS 167
Cdd:PRK09700 104 GRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS---SLTNKE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447179532 168 LqEWLF---EQWQEWEKTILFITHDVEEALFLSNRVLVVE 204
Cdd:PRK09700 181 V-DYLFlimNQLRKEGTAIVYISHKLAEIRRICDRYTVMK 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-214 |
5.26e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.14 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDE--KPIIHELNASIHEKEFVSIIGPSGCGKSTL----FRLITGLE-KVSIGKIELTETKHHPVG---YM 76
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFDgKIVIDGIDISKLPLHTLRsrlSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 77 PQKDMLLPWRTIIENAALPLECQGVQKKE----AQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPECKCTDDRLWEaleiAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQewEKTILFITH------DVEEALFLSNRVLVVEQQPITTLTER 214
Cdd:cd03288 180 MDEATASIDMATENILQKVVMTAFA--DRTVVTIAHrvstilDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-192 |
6.01e-07 |
|
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: 47.75 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 32 KEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPvgympqkdmllpwrtiienaalplecqgvqkkeaqvkak 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 112 ELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQE-----WLFEQWQEWEKTILFI 186
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKSEKNLTVILT 122
|
....*.
gi 447179532 187 THDVEE 192
Cdd:smart00382 123 TNDEKD 128
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-162 |
6.81e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.39 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYD----EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRL---------ITGleKVSIGKIELTETKHHP 72
Cdd:cd03232 3 VLTWKNLNYTVPvkggKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVlagrktagvITG--EILINGRPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 73 VGYMPQKDMLLPWRTIIENaalplecqgvqkkeaqvkakeLLYKFGLQGyetkhpkdLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREA---------------------LRFSALLRG--------LSVEQRKRLTIGVELAAKPSILF 131
|
170
....*....|
gi 447179532 153 LDEPFSALDA 162
Cdd:cd03232 132 LDEPTSGLDS 141
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-209 |
7.14e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 28 SIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELtetKHHPV-----------GYM--PQ---KDMLLPWRTIIEN 91
Cdd:PRK11288 275 SVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL---DGKPIdirsprdairaGIMlcPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 92 AA-------LPLECQGVQKKEAQvKAKELLYKFGLQgyeTKHPK----DLSGGMRQRVSFIRTLLTGGEILLLDEPFSAL 160
Cdd:PRK11288 352 INisarrhhLRAGCLINNRWEAE-NADRFIRSLNIK---TPSREqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447179532 161 DALTKASLQEWLFEqWQEWEKTILFITHDVEEALFLSNRVLVVEQQPIT 209
Cdd:PRK11288 428 DVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-189 |
7.57e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGlekvsigkiELTETKHhPVGYMPQKDMLLPW 85
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---------DLTGGGA-PRGARVTGDVTLNG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 RTIIENAALPLEC-QGVQKKEAQ----VKAKELL----YKFGLQGYETKH-------------------PKD---LSGGM 134
Cdd:PRK13547 71 EPLAAIDAPRLARlRAVLPQAAQpafaFSAREIVllgrYPHARRAGALTHrdgeiawqalalagatalvGRDvttLSGGE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447179532 135 RQRVSFIRTL---------LTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHD 189
Cdd:PRK13547 151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHD 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
128-190 |
8.65e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 8.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447179532 128 KDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDV 190
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-63 |
8.79e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 8.79e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447179532 1 MRSKNILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSI--GKI 63
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIleGDI 66
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-164 |
9.62e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 15 HYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG-LEKVSIGK--------IELTETKHH---PVGYMPQKDML 82
Cdd:TIGR00956 70 DTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIGVegvitydgITPEEIKKHyrgDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 83 LPWRTIIENAALPLECQGVQKKEAQVKAKELLYK--------FGL-QGYETKHPKDL----SGGMRQRVSFIRTLLTGGE 149
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKTPQNRPDGVSREEYAKHiadvymatYGLsHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAK 229
|
170
....*....|....*
gi 447179532 150 ILLLDEPFSALDALT 164
Cdd:TIGR00956 230 IQCWDNATRGLDSAT 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-205 |
1.02e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 14 FHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTEtkhHPV-----GYMPQK--------- 79
Cdd:PRK15112 21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLhfgdySYRSQRirmifqdps 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 DMLLPWRTIIENAALPLECQGVQKKEAQVKA-KELLYKFGL-QGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPF 157
Cdd:PRK15112 98 TSLNPRQRISQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447179532 158 SALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-189 |
1.47e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 10 HNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKI-------------------------- 63
Cdd:PRK11147 7 HGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlqqdpprnvegtvydf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 64 ---------ELTETKH---HPVGYMPQKDMLLPWRTIIENaalpLECQGVQKKEAQVKakELLYKFGLQGyETKHpKDLS 131
Cdd:PRK11147 87 vaegieeqaEYLKRYHdisHLVETDPSEKNLNELAKLQEQ----LDHHNLWQLENRIN--EVLAQLGLDP-DAAL-SSLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447179532 132 GGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKaslqEWLFEQWQEWEKTILFITHD 189
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI----EWLEGFLKTFQGSIIFISHD 212
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-238 |
1.54e-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: 47.93 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 21 IIHELNASIHEKEFVSIIGPSGCGKSTLF----RLIT-----GLEKVSIGKIELTETKhHPVGYMPQKDMLL--PWRTII 89
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNtegdiQIDGVSWNSVPLQKWR-KAFGVIPQKVFIFsgTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 90 EnaalPLEC---QGVQKKEAQVKAKELLYKFGLQ--------GYEtkhpkdLSGGMRQRVSFIRTLLTGGEILLLDEPFS 158
Cdd:cd03289 98 D----PYGKwsdEEIWKVAEEVGLKSVIEQFPGQldfvlvdgGCV------LSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 159 ALDALTKASLQEWLFEQWQEWekTILFITHDVeEALFLSNRVLVVEQQPITT-------LTE--------------RIVP 217
Cdd:cd03289 168 HLDPITYQVIRKTLKQAFADC--TVILSEHRI-EAMLECQRFLVIEENKVRQydsiqklLNEkshfkqaispsdrlKLFP 244
|
250 260
....*....|....*....|.
gi 447179532 218 LDHNRTRKDLYKPEVLALKDE 238
Cdd:cd03289 245 RRNSSKSKRKPRPQIQALQEE 265
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-188 |
1.79e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.59 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 2 RSKNILQFHNVSFHYDEKPI-IHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKieLTETKHHPVGYMPQKd 80
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPNGDVlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR--LTKPAKGKLFYVPQR- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 mllPWRT--------IIENAALPLECQGVQKKEAQ-----VKAKELLYKFGlqGYET-KHPKD-LSGGMRQRVSFIRTLL 145
Cdd:TIGR00954 524 ---PYMTlgtlrdqiIYPDSSEDMKRRGLSDKDLEqildnVQLTHILEREG--GWSAvQDWMDvLSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447179532 146 TGGEILLLDEPFSALdaltKASLQEWLFEQWQEWEKTILFITH 188
Cdd:TIGR00954 599 HKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
130-202 |
2.00e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 2.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447179532 130 LSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLV 202
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILV 463
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-55 |
2.14e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.26 E-value: 2.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 447179532 7 LQFHNVSFHY----DEKP-IIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGL 55
Cdd:COG4615 328 LELRGVTYRYpgedGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGL 381
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-214 |
3.62e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.85 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 25 LNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSiGKI----------ELTETKHHPvGYMPQKDMLLPWRTIIENAAL 94
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIqfagqpleawSAAELARHR-AYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 95 PLEcQGVQKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLT-------GGEILLLDEPFSALDALTKAS 167
Cdd:PRK03695 93 HQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447179532 168 LQEwLFEQWQEWEKTILFITHDV-------EEALFLSNRVLVVEQQPITTLTER 214
Cdd:PRK03695 172 LDR-LLSELCQQGIAVVMSSHDLnhtlrhaDRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-162 |
4.25e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 11 NVSFHYD---EKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITG-LEKVSIGKIELTETkhhpVGYMPQkdmlLPW- 85
Cdd:PLN03130 619 NGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT----VAYVPQ----VSWi 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 --RTIIENAALPLECQGVQKKEAqVKAKEL-----------LYKFGLQGYetkhpkDLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:PLN03130 691 fnATVRDNILFGSPFDPERYERA-IDVTALqhdldllpggdLTEIGERGV------NISGGQKQRVSMARAVYSNSDVYI 763
|
170
....*....|
gi 447179532 153 LDEPFSALDA 162
Cdd:PLN03130 764 FDDPLSALDA 773
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
130-205 |
5.48e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.74 E-value: 5.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 130 LSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGE 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-209 |
5.77e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 10 HNVSFhydekpiihelnaSIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELTETKHHPVGymPQ----------- 78
Cdd:PRK10762 269 NDVSF-------------TLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS--PQdglangivyis 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 79 ----KDMLLPWRTIIENAALP----LECQGVQ-KKEAQVKAKEllyKFgLQGYETKHP------KDLSGGMRQRVSFIRT 143
Cdd:PRK10762 334 edrkRDGLVLGMSVKENMSLTalryFSRAGGSlKHADEQQAVS---DF-IRLFNIKTPsmeqaiGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 144 LLTGGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPIT 209
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-189 |
1.06e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIELteTKHHPVGYMPQKDMllpw 85
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--AKGIKLGYFAQHQL---- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 86 rTIIENAALPLE-CQGVQKKEAQVKAKELLYKFGLQGYE-TKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDAL 163
Cdd:PRK10636 386 -EFLRADESPLQhLARLAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180
....*....|....*....|....*.
gi 447179532 164 TKASLQEWLFeqwqEWEKTILFITHD 189
Cdd:PRK10636 465 MRQALTEALI----DFEGALVVVSHD 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-244 |
1.06e-05 |
|
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: 46.44 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 12 VSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLF----RLITGLEKVSIGKIELT----ETKHHPVGYMPQKDMLL 83
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIQIDGVSWNsvtlQTWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 84 PwRTIIENAAlPLEC---QGVQKKEAQVKAKELLYKFGLQ--------GYEtkhpkdLSGGMRQRVSFIRTLLTGGEILL 152
Cdd:TIGR01271 1305 S-GTFRKNLD-PYEQwsdEEIWKVAEEVGLKSVIEQFPDKldfvlvdgGYV------LSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 153 LDEPFSALDALTKASLQEWLFEQWQEWekTILFITHDVeEALFLSNRVLVVEQQPITT-------LTER----------- 214
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEHRV-EALLECQQFLVIEGSSVKQydsiqklLNETslfkqamsaad 1453
|
250 260 270
....*....|....*....|....*....|...
gi 447179532 215 ---IVPLDHNRTRKDLYKPEVLALKDELLSMLQ 244
Cdd:TIGR01271 1454 rlkLFPLHRRNSSKRKPQPKITALREEAEEEVQ 1486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
123-202 |
3.33e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 123 ETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDalTKASLqeWLFEQWQEWEKTILFITHD-------VEEALF 195
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVL--WLETYLLKWPKTFIVVSHAreflntvVTDILH 413
|
....*..
gi 447179532 196 LSNRVLV 202
Cdd:PLN03073 414 LHGQKLV 420
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-207 |
4.12e-05 |
|
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: 43.51 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 35 VSIIGPSGCGKSTLFRLITGLEKVSIGKIE-----------------------LTETKHHPVgYMPQKDMLLPwRTIIEN 91
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnyftkLLEGDVKVI-VKPQYVDLIP-KAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 92 AALPLEcqgvqKKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDA---LTKASL 168
Cdd:cd03236 107 VGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARL 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 447179532 169 QEWLFEQwqewEKTILFITHDVEEALFLSNRVLVVEQQP 207
Cdd:cd03236 182 IRELAED----DNYVLVVEHDLAVLDYLSDYIHCLYGEP 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-202 |
1.65e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.20 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 26 NASIHEKEFVSIIGPSGCGKSTLFRLITGLEK---------VSIGKIELT----ETKHHPVGympqKDM----------L 82
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrFRWNGIDLLklspRERRKIIG----REIamifqepsscL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 83 LPWRTIIE--NAALP---LECQGVQKKEAQVK-AKELLYKFGLQGYE---TKHPKDLSGGMRQRVSFIRTLLTGGEILLL 153
Cdd:COG4170 103 DPSAKIGDqlIEAIPswtFKGKWWQRFKWRKKrAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447179532 154 DEPFSALDALTKASLQEWLFEQWQEWEKTILFITHDVEEALFLSNRVLV 202
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-213 |
2.21e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 37 IIGPSGCGKSTLFRLITGLEKVSIGKIEL----------TETKHHPVGYMPQKDMLLPWRTIIENAALPLECQ----GVQ 102
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVnrfgRID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 103 KKEAQVKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPfsaLDALTKASlQEWLFEQWQEWEKT 182
Cdd:PRK10762 115 WKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDALTDTE-TESLFRVIRELKSQ 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447179532 183 ---ILFITHDVEEALFLSNRVLV------VEQQPITTLTE 213
Cdd:PRK10762 191 grgIVYISHRLKEIFEICDDVTVfrdgqfIAEREVADLTE 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
130-205 |
2.32e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 2.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 130 LSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEwEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHE 480
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
6-161 |
4.05e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 6 ILQFHNVSFHYDEKpIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGLEKVSIGKIEL----TETKHHP-VGYMPQKD 80
Cdd:PRK13541 1 MLSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYkncnINNIAKPyCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 81 MLLPWRTIIENAALPLEcqgVQKKEAQVKAKelLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSAL 160
Cdd:PRK13541 80 GLKLEMTVFENLKFWSE---IYNSAETLYAA--IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
.
gi 447179532 161 D 161
Cdd:PRK13541 155 S 155
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
130-205 |
4.76e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 4.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447179532 130 LSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQ 205
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
109-203 |
8.95e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 109 KAKELLYKFGLQGYE---TKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEWLFEQWQEWEKTILF 185
Cdd:PRK15093 135 RAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILL 214
|
90
....*....|....*...
gi 447179532 186 ITHDVEEALFLSNRVLVV 203
Cdd:PRK15093 215 ISHDLQMLSQWADKINVL 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-172 |
1.05e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 7 LQFHNVSFHYDEKPIIHELNASIHEKEFVSIIGPSGCGKSTLFRLITGleKVSIGKIELTETKHHPVGY---MPQK---- 79
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG--ELPLLSGERQSQFSHITRLsfeQLQKlvsd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 80 -------DMLLPW-----RT---IIENAAlplecqgvqKKEAqvKAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTL 144
Cdd:PRK10938 82 ewqrnntDMLSPGeddtgRTtaeIIQDEV---------KDPA--RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180
....*....|....*....|....*...
gi 447179532 145 LTGGEILLLDEPFSALDALTKASLQEWL 172
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELL 178
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-161 |
2.16e-03 |
|
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: 39.00 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 35 VSIIGPSGCGKSTLFRLITGLEKVSIGKIEltetkhHPVGympqkdmllpWRTIIE---NAALPLECQGVQKKEAQV--- 108
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYD------EEPS----------WDEVLKrfrGTELQDYFKKLANGEIKVahk 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447179532 109 -------------KAKELLYK-------------FGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:COG1245 166 pqyvdlipkvfkgTVRELLEKvdergkldelaekLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
109-161 |
4.01e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 38.25 E-value: 4.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 447179532 109 KAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALD 161
Cdd:PRK13409 192 KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
129-211 |
4.19e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 38.23 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 129 DLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEwLFEQWQEWEKTILFITHDVEEALFLSNRVLVVEQQPI 208
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
...
gi 447179532 209 TTL 211
Cdd:PRK09700 488 TQI 490
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-240 |
5.35e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.60 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 33 EFVSIIGPSGCGKSTLFRLITGL--------------EKVSIGKIELTETKHHPVGYmpQKDMLLPWRTIIENAALPLEC 98
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGVyphgtyegeiifegEELQASNIRDTERAGIAIIH--QELALVKELSVLENIFLGNEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447179532 99 Q--GVQKKEAQV-KAKELLYKFGLQGYETKHPKDLSGGMRQRVSFIRTLLTGGEILLLDEPFSALDALTKASLQEwLFEQ 175
Cdd:PRK13549 110 TpgGIMDYDAMYlRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLD-IIRD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447179532 176 WQEWEKTILFITHDVEEALFLSNRVLV------VEQQPITTLTE-RIVPLDHNRTRKDLYKPEVLALKDELL 240
Cdd:PRK13549 189 LKAHGIACIYISHKLNEVKAISDTICVirdgrhIGTRPAAGMTEdDIITMMVGRELTALYPREPHTIGEVIL 260
|
|
| |
