|
Name |
Accession |
Description |
Interval |
E-value |
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-357 |
0e+00 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 546.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 1 MIKLAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGY 80
Cdd:PRK11144 1 MLELNFKQQLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 81 VFQEARLFPHYKVKGNLLYGAsRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASL 160
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGM-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 161 DLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAFQPWQKNSELSTLFKGML 240
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 241 TEHHPKYALSYVELARNiGVWMSGIQVKKGESLRVRIHASDVSITLSQAKDTSMRNIIPATIVELAKVTDptqPVSLRLS 320
Cdd:PRK11144 240 LEHHPHYAMTALALGDQ-HLWVNKLDAPLGTALRIRIQASDVSLVLQPPQQSSIRNILRAKVVEIYDDNG---QVEVKLE 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 515592652 321 LGsGLSLWANITAWAYDDLQLKTGQKVFAQIKGVRLT 357
Cdd:PRK11144 316 VG-GKTLWARITPWARDELALKPGQWLYAQIKSVSIT 351
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-354 |
4.58e-179 |
|
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: 500.78 E-value: 4.58e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 1 MIKLAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGY 80
Cdd:COG4148 2 MLEVDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 81 VFQEARLFPHYKVKGNLLYGASR---HYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPL 157
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRKRaprAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 158 ASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAFQPWQKNSELSTLFK 237
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 238 GMLTEHHPKYALSYVELArNIGVWMSGIQVKKGESLRVRIHASDVSITLSQAKDTSMRNIIPATIVELAKVTDPTqpVSL 317
Cdd:COG4148 242 ATVAAHDPDYGLTRLALG-GGRLWVPRLDLPPGTRVRVRIRARDVSLALEPPEGSSILNILPGRVVEIEPADGGQ--VLV 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 515592652 318 RLSLGsGLSLWANITAWAYDDLQLKTGQKVFAQIKGV 354
Cdd:COG4148 319 RLDLG-GQTLLARITRRSADELGLAPGQTVYAQIKSV 354
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-357 |
2.58e-150 |
|
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: 427.99 E-value: 2.58e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYV 81
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 82 FQEARLFPHYKVKGNLLYGASR---HYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 159 SLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAFqPWQKNSELSTLFKG 238
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL-PWLAREDQGSLIEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 239 MLTEHHPKYALSYVELArNIGVWMSGIQVKKGESLRVRIHASDVSITLSQAKDTSMRNIIPATIVELakVTDPTQPVSLR 318
Cdd:TIGR02142 240 VVAEHDQHYGLTALRLG-GGHLWVPENLGPTGARLRLRVPARDVSLALQKPEATSIRNILPARVVEI--EDSDIGRVGVV 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 515592652 319 LSLGsGLSLWANITAWAYDDLQLKTGQKVFAQIKGVRLT 357
Cdd:TIGR02142 317 LESG-GKTLWARITRWARDELGIAPGTPVFAQIKAVALR 354
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-212 |
5.49e-82 |
|
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: 248.75 E-value: 5.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 1 MIKLAFKQQLEQFMLDINVDIPQhGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGY 80
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 81 VFQEARLFPHYKVKGNLLYGASRHY---DRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPL 157
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKRKRnreDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 158 ASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-356 |
7.85e-61 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 199.22 E-value: 7.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 6 FKQQLEQFML--DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYdsnknINIAIDKRKIGYVFQ 83
Cdd:COG1118 8 ISKRFGSFTLldDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----TNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 EARLFPHYKVKGNLLYGAS-RHYDRNHFDQIV-QLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRvRPPSKAEIRARVeELLElvqLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 159 SLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRS--TAFQPW---QKNsels 233
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRpaTPFVARflgCVN---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 234 tLFKGmltehhpkyalsyveLARNIGVWMSGIQVKKGESL-----RVRIHASDVSItlsqAKDTSMRNIIPATIVELakv 308
Cdd:COG1118 239 -VLRG---------------RVIGGQLEADGLTLPVAEPLpdgpaVAGVRPHDIEV----SREPEGENTFPATVARV--- 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 309 tDPTQP---VSLRLSLGSGLSLWANITAWAYDDLQLKTGQKVFAQIKGVRL 356
Cdd:COG1118 296 -SELGPevrVELKLEDGEGQPLEAEVTKEAWAELGLAPGDPVYLRPRPARV 345
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-212 |
5.72e-57 |
|
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: 184.65 E-value: 5.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnkninIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPERRNIGMVFQDYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYD-----RNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:cd03259 92 NIAFGLKLRGVpkaeiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03259 172 ELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
11-352 |
6.52e-57 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 188.75 E-value: 6.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 11 EQFML-DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNI-NIAIDKRKIGYVFQEARLF 88
Cdd:NF040840 12 KEFKLrDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLD-------GKDItNLPPEKRGIAYVYQNYMLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 PHYKVKGNLLYGAS-RHYDRNHFD----QIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLP 163
Cdd:NF040840 85 PHKTVFENIAFGLKlRKVPKEEIErkvkEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 164 RKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRstafQPwqKNSELS------TLFK 237
Cdd:NF040840 165 TRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFR----RP--KNEFVArfvgfeNIIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 238 GMLTEHHPKYALSyvelARNIGVWMSGiqVKKGeslRVRIHASDVSITLSQAK-DTSMRNIIPATIVElakVTDPTQPVs 316
Cdd:NF040840 239 GVAEKGGEGTILD----TGNIKIELPE--EKKG---KVRIGIRPEDITISTEKvKTSARNEFKGKVEE---IEDLGPLV- 305
|
330 340 350
....*....|....*....|....*....|....*.
gi 515592652 317 lRLSLGSGLSLWANITAWAYDDLQLKTGQKVFAQIK 352
Cdd:NF040840 306 -KLTLDVGIILVAFITRSSFLDLEINEGKEVYASFK 340
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-352 |
1.29e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 182.99 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnknINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG3842 23 DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV------TGLPPEKRNVGMVFQDYALFPHLTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGAS-RHYDRNHFDQIVQ----LLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:COG3842 97 NVAFGLRmRGVPKAEIRARVAelleLVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMRE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRstafQPwqkNSE-------LSTLFKGMLTEH 243
Cdd:COG3842 177 ELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYE----RP---ATRfvadfigEANLLPGTVLGD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 244 HPkyalSYVELARNIGVWMSGIQVKKGESLRVRIHASDVSITlsqakDTSMRNIIPATIVELA---KVTDptqpvsLRLS 320
Cdd:COG3842 250 EG----GGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLS-----PEGPENGLPGTVEDVVflgSHVR------YRVR 314
|
330 340 350
....*....|....*....|....*....|..
gi 515592652 321 LGSGLSLWANITawAYDDLQLKTGQKVFAQIK 352
Cdd:COG3842 315 LGDGQELVVRVP--NRAALPLEPGDRVGLSWD 344
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
16-210 |
1.20e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.58 E-value: 1.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkniniaidkRKIGYVFQEARLFPHYKVKG 95
Cdd:COG1116 29 DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---------PDRGVVFQEPALLPWLTVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGAS-RHYDRNHFDQIVQ-LLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:COG1116 100 NVALGLElRGVPKAERRERAReLLElvgLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIED--GQIKA 210
Cdd:COG1116 180 ELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
16-221 |
4.80e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 170.24 E-value: 4.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNIniaidKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-----RRRIGYVPQEPALYPDLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:COG1131 93 NLrffarLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 171 FLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRST 221
Cdd:COG1131 173 LLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
16-208 |
2.37e-50 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 171.79 E-value: 2.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalyDSNkniNIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG3839 21 DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR---DVT---DLPPKDRNIAMVFQSYALYPHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGAS-RHYDRNHFDQIVQ----LLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:COG3839 95 NIAFPLKlRKVPKAEIDRRVReaaeLLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRA 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:COG3839 175 EIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-210 |
3.31e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.53 E-value: 3.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiniAIDK---RKIGYVFQEARLFPHYK 92
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSER---ELARlrrRHIGFVFQFFNLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGN----LLY-GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:COG1136 103 ALENvalpLLLaGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSlEEILHLADHMLLIEDGQIKA 210
Cdd:COG1136 183 VLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-216 |
3.47e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 167.62 E-value: 3.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 1 MIKL-AFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNIN-IAIDKRKI 78
Cdd:COG3840 1 MLRLdDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-------GQDLTaLPPAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 79 GYVFQEARLFPHYKVKGNLLYG--ASRHYDRNHFDQIVQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLM 153
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGlrPGLKLTAEQRAQVEQALErvgLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515592652 154 DEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIET 216
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-207 |
5.14e-50 |
|
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: 165.44 E-value: 5.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 12 QFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnKNINIAIDKRKIGYVFQEARLFPHY 91
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD--LEDELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYGasrhydrnhfdqivqlldlstlldrypvdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:cd03229 92 TVLENIALG-----------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRAL 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 172 LEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:cd03229 143 LKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-215 |
1.40e-49 |
|
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: 166.36 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 11 EQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGEralydsnKNI-NIAIDKRKIGYVFQEARLFP 89
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG-------KDItNLPPEKRDISYVPQNYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 HYKVKGNLLYGAS-RHYDRNHFD----QIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:cd03299 85 HMTVYKNIAYGLKkRKVDKKEIErkvlEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 165 KQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
12-222 |
9.40e-49 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 164.20 E-value: 9.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 12 QFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalyDSNkniNIAIDKRKIGYVFQEARLFPHY 91
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ---DAT---RVHARDRKIGFVFQHYALFKHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYGAS-RHYD----RNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:TIGR00968 88 TVRDNIAFGLEiRKHPkakiKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515592652 167 EVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTA 222
Cdd:TIGR00968 168 ELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPA 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
16-215 |
3.88e-48 |
|
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: 162.26 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkniniaidkRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---------PDRGYVFQQDALLPWLTVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG-----ASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:cd03293 93 NVALGlelqgVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIE--DGQIKASGDIE 215
Cdd:cd03293 173 ELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAEVEVD 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-208 |
5.91e-48 |
|
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: 161.50 E-value: 5.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 N-----LLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:cd03255 102 NvelplLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVME 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 171 FLEKLSQEINIPILYVTHSlEEILHLADHMLLIEDGQI 208
Cdd:cd03255 182 LLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-223 |
3.50e-47 |
|
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: 160.20 E-value: 3.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERAlydSNKNINiaidKRKIGYVFQEARLFPHYKVK 94
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFgGEDA---TDVPVQ----ERNVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYG-----ASRHYD----RNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:cd03296 93 DNVAFGlrvkpRSERPPeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 166 QEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWR--STAF 223
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDhpASPF 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
16-208 |
1.77e-46 |
|
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: 157.42 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiniaidKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------DRDIAMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG-ASRHYDRNHFDQIV----QLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:cd03301 92 NIAFGlKLRKVPKDEIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRA 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03301 172 ELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-217 |
6.89e-46 |
|
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: 157.27 E-value: 6.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnkniniAIDK---RKIGYVFQEAR--LFPH 90
Cdd:COG1124 23 DVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-------RRRKafrRRVQMVFQDPYasLHPR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 YKVKGNLLYGASRHYDRNHFDQIVQLLDL----STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:COG1124 96 HTVDRILAEPLRIHGLPDREERIAELLEQvglpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 167 EVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG1124 176 EILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-217 |
1.97e-45 |
|
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: 155.97 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYD-SNKNIniAidkRKIGYVFQEARLFPHYKVK 94
Cdd:COG1120 19 DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRREL--A---RRIAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGASRHY---------DRNHFDQIVQLLDLSTLLDRyPVD-LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:COG1120 94 ELVALGRYPHLglfgrpsaeDREAVEEALERTGLEHLADR-PVDeLSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAH 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 165 KQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG1120 173 QLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-215 |
3.72e-45 |
|
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: 154.66 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYD-SNKNINIAidKRKIGYVFQEARLFPHYKVK 94
Cdd:cd03258 23 DVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA--RRRIGMIFQHFNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03258 101 ENVALpleiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:cd03258 181 ALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-222 |
4.66e-45 |
|
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: 154.77 E-value: 4.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNINiAID----KRKIGYVFQEARLFPHY 91
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-------GEDIR-EQDpvelRRKIGYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNL-----LYGASRHYDRNHFDQIVQLLDL--STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD-LP 163
Cdd:cd03295 91 TVEENIalvpkLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpIT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 164 RKQEVMPFLeKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTA 222
Cdd:cd03295 171 RDQLQEEFK-RLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-215 |
4.04e-44 |
|
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: 152.10 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSN-KNIniaidKRKIGYVFQ--EARLF-Phy 91
Cdd:COG1122 19 DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlREL-----RRKVGLVFQnpDDQLFaP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYGASRH-YDRNHFDQIVQ----LLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:COG1122 92 TVEEDVAFGPENLgLPREEIRERVEealeLVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 167 EVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:COG1122 172 ELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
16-212 |
1.85e-43 |
|
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: 150.46 E-value: 1.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNI-NIAIDKRKIGYVFQEARLFPHYKVK 94
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-------GKDItNLPPHKRPVNTVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYG-----ASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03300 91 ENIAFGlrlkkLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03300 171 LELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-208 |
3.66e-43 |
|
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: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINiAIDKRKIGYVFQEAR--LFPHYKV 93
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KIRRKEIQMVFQDPMssLNPRMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYGASRHYD--------RNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:cd03257 102 GEQIAEPLRIHGKlskkearkEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 166 QEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03257 182 AQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-207 |
4.28e-43 |
|
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: 148.77 E-value: 4.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkninIAIDKRKIGYVFQEARL-FPHYKVK 94
Cdd:cd03225 19 DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELRRKVGLVFQNPDDqFFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGA-SRHYDRNHFDQIV----QLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03225 95 EEVAFGLeNLGLPEEEIEERVeealELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 170 PFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:cd03225 175 ELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-258 |
5.39e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 150.94 E-value: 5.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 14 MLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQ--EARLFPHY 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVK----GNLLYGASRHYDRNHFDQIVQLLDLS-TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPR-K 165
Cdd:PRK13634 103 VEKdicfGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD-PKgR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 166 QEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTA-FQPWQKNSELSTLFKGMLTE-- 242
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDeLEAIGLDLPETVKFKRALEEkf 261
|
250
....*....|....*...
gi 515592652 243 --HHPKYALSYVELARNI 258
Cdd:PRK13634 262 giSFPKPCLTLEELAHEV 279
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-215 |
1.73e-42 |
|
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: 154.68 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiNIAIDKRKIGYVFQ--EARLFPHYKV 93
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR-SLRELRRRVQMVFQdpYSSLNPRMTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYGASRH--YDRNHFDQIV-QLLDL----STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:COG1123 362 GDIIAEPLRLHglLSRAERRERVaELLERvglpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQA 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 167 EVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:COG1123 442 QILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-208 |
2.29e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.19 E-value: 2.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQ 83
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL----SAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 EARLFPHyKVKGNLLYG---ASRHYDRNHFDQIVQLLDLST-LLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:COG4619 82 EPALWGG-TVRDNLPFPfqlRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 160 LDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:COG4619 161 LDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-212 |
2.48e-41 |
|
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: 142.96 E-value: 2.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAidkRKIGYVFQearlfphykvkg 95
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPKELA---RKIAYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 nllygasrhydrnhfdqIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:cd03214 81 -----------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 515592652 176 SQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03214 144 ARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
16-208 |
2.94e-41 |
|
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: 142.54 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGEralYDSNKNINIAidKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG---KDIKKEPEEV--KRRIGYLPEEPSLYENLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLlygasrhydrnhfdqivqlldlstlldrypvDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:cd03230 93 NL-------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL 141
|
170 180 190
....*....|....*....|....*....|...
gi 515592652 176 SQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03230 142 KKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-208 |
3.23e-41 |
|
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: 143.82 E-value: 3.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAidKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03262 18 GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL--RQKVGMVFQQFNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG--ASRHYDRNHFDQI-VQLLDLSTLLDR---YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03262 96 NITLApiKVKGMSKAEAEERaLELLEKVGLADKadaYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 515592652 170 PFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03262 176 DVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
15-212 |
1.10e-40 |
|
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: 142.63 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 15 LDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkniniaIDKRKIGYVFQEARLFPHYKVK 94
Cdd:cd03298 15 MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP------PADRPVSMLFQENNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGAS-----RHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03298 89 QNVGLGLSpglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-222 |
5.51e-40 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 144.46 E-value: 5.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 12 QFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIivgerALYDSNKNINIAIDkRKIGYVFQEARLFPHY 91
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-----RFHGTDVSRLHARD-RKVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYGAS---RHY--DRNHFDQIV-QLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PRK10851 90 TVFDNIAFGLTvlpRRErpNAAAIKAKVtQLLEmvqLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 163 PRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTA 222
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-216 |
9.35e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.99 E-value: 9.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalydsnkniNIAIDKRKIGYVFQEA---RLFP--- 89
Cdd:COG1121 24 DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---------PPRRARRRIGYVPQRAevdWDFPitv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 -------HYKvKGNLLYGASRHyDRNHFDQIVQLLDLSTLLDRyPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:COG1121 95 rdvvlmgRYG-RRGLFRRPSRA-DREAVDEALERVGLEDLADR-PIgELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 162 LPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIkASGDIET 216
Cdd:COG1121 172 AATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEE 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
16-216 |
1.04e-39 |
|
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: 140.39 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNN-----PDSGKIIVGERALYDSNKNINIAidKRKIGYVFQEARLFPh 90
Cdd:cd03260 18 DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLEL--RRRVGMVFQKPNPFP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 YKVKGNLLYGASRH--YDRNHFDQIV-QLLDLSTLLDR-----YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDl 162
Cdd:cd03260 95 GSIYDNVAYGLRLHgiKLKEELDERVeEALRKAALWDEvkdrlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515592652 163 PRKQEVMpflEKLSQEIN--IPILYVTHSLEEILHLADHMLLIEDGQIKASGDIET 216
Cdd:cd03260 174 PISTAKI---EELIAELKkeYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-212 |
3.23e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 140.66 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAIDKRKIGYVFQ--EARLF----- 88
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDI-TAKKKKKLKDLRKKVGLVFQfpEHQLFeetvy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 ------PHykvkgNLlyGASRHYDRNHFDQIVQLLDLS-TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:TIGR04521 102 kdiafgPK-----NL--GLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 162 lPR-KQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:TIGR04521 175 -PKgRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-217 |
6.63e-39 |
|
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: 137.95 E-value: 6.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNIN----IAIDKRKIGYVFQEARLFPHY 91
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-------GRDITglppHERARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYGASRHYDRNHFDQIVQLLD----LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPlaSLDLPRK-- 165
Cdd:cd03224 91 TVEENLLLGAYARRRAKRKARLERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP--SEGLAPKiv 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 166 QEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:cd03224 169 EEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
16-208 |
2.70e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.11 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG3638 21 DVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV-TALRGRALRRLRRRIGMIFQQFNLVPRLSVLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGA----------SRHYDRNHFDQIVQLLDLSTLLDR--YPVD-LSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:COG3638 100 NVLAGRlgrtstwrslLGLFPPEDRERALEALERVGLADKayQRADqLSGGQQQRVAIARALVQEPKLILADEPVASLDP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 163 PRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:COG3638 180 KTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
16-213 |
2.91e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 136.66 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINiAIdKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN-KL-RRKVGMVFQQFNLFPHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG--ASRHYDRNHFDQI-VQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:COG1126 97 NVTLApiKVKKMSKAEAEERaMELLErvgLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515592652 170 PFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGD 213
Cdd:COG1126 177 DVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-221 |
2.94e-38 |
|
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: 137.03 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIdKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL-RRRIGMLFQGGALFDSLTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRH--YDRNHFDQIV----QLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:COG1127 102 NVAFPLREHtdLSEAEIRELVleklELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVID 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRST 221
Cdd:COG1127 182 ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
16-208 |
3.08e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 138.69 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalydSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG1125 20 DLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGE----DIRDLDPVELRRRIGYVIQQIGLFPHMTVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 N-----LLYGASRHYDRNHFDQIVQL--LDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlP--RKQ 166
Cdd:COG1125 96 NiatvpRLLGWDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALD-PitREQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515592652 167 ---EVMpfleKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:COG1125 175 lqdELL----RLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRI 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-208 |
5.28e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.73 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIaidkrkigyVFQEARLFPHYKVKG 95
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRL---------MFQDARLLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDrnhfDQIVQLLDLSTLLDR---YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFL 172
Cdd:PRK11247 101 NVGLGLKGQWR----DAALQALAAVGLADRaneWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 173 EKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK11247 177 ESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-158 |
6.40e-38 |
|
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: 133.16 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnknINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD----DERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515592652 96 NLLYGA-----SRHYDRNHFDQIVQLLDLS----TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:pfam00005 79 NLRLGLllkglSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-208 |
8.65e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.18 E-value: 8.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiNIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG2884 20 DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRR-EIPYLRRRIGVVFQDFRLLPDRTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:COG2884 99 NVALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIME 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 171 FLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:COG2884 179 LLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-229 |
2.36e-37 |
|
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: 134.55 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRkIGYVFQEARLFPHYKVKG 95
Cdd:cd03261 18 GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNH--FDQIV----QLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03261 97 NVAFPLREHTRLSEeeIREIVleklEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTafQPWQKN 229
Cdd:cd03261 177 DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD--DPLVRQ 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-238 |
4.11e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 136.77 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKI-IVGEralyDSNKNiniAIDKRKIGYVFQEARLFPHYKVK 94
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfIDGE----DVTHR---SIQQRDICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYG-----ASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:PRK11432 97 ENVGYGlkmlgVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRstafqpwQKNSELSTLFKG 238
Cdd:PRK11432 177 EKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR-------QPASRFMASFMG 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-194 |
6.33e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.61 E-value: 6.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPD---SGKIIVGERALYDsnkninIAIDKRKIGYVFQEARLFPHYK 92
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA------LPAEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLLYGASRHYDR-NHFDQIVQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEV 168
Cdd:COG4136 93 VGENLAFALPPTIGRaQRRARVEQALEeagLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
170 180
....*....|....*....|....*.
gi 515592652 169 MPFLEKLSQEINIPILYVTHSLEEIL 194
Cdd:COG4136 173 REFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
12-209 |
7.75e-37 |
|
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: 132.45 E-value: 7.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 12 QFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIdKRKIGYVFQEARLFPHY 91
Cdd:TIGR02982 19 QVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL-RRRIGYIFQAHNLLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGN------LLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:TIGR02982 98 TARQNvqmaleLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515592652 166 QEVMPFLEKLSQEINIPILYVTHSlEEILHLADHMLLIEDGQIK 209
Cdd:TIGR02982 178 RDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-207 |
1.53e-36 |
|
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: 129.67 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQearlfphykvkg 95
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI----AKLPLEELRRRIGYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 nllygasrhydrnhfdqivqlldlstlldrypvdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:cd00267 81 ----------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 176 SQEiNIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:cd00267 127 AEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
29-218 |
1.67e-36 |
|
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: 134.54 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnknINIAIDKRKIGYVFQEARLFPHYKVKGNLLYGAS-RHYDR 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKmRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 108 NHFDQIV----QLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPI 183
Cdd:TIGR01187 75 AEIKPRVlealRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....*
gi 515592652 184 LYVTHSLEEILHLADHMLLIEDGQIKASGDIETMW 218
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIY 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-213 |
2.05e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 132.06 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 12 QFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlYDSNKNIN---IAIDKRKIGYVFQEARLF 88
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH-FDFSKTPSdkaIRELRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 PHYKVKGNLL------YGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PRK11124 95 PHLTVQQNLIeapcrvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 163 PRKQEVMPFLEKLsQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGD 213
Cdd:PRK11124 175 EITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-215 |
3.80e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.05 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYD-SNKNINIAidKRKIGYVFQEARLFPHYKVK 94
Cdd:COG1135 23 DVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA--RRKIGMIFQHFNLLSSRTVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPRK-QEV 168
Cdd:COG1135 101 ENVALpleiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD-PETtRSI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 169 MPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:COG1135 180 LDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-208 |
4.52e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 130.86 E-value: 4.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralyDSNKNINIAIDKRKIGYVFQEARLFPHYKVKGNLLYGAS----- 102
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTL------NGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNpglkl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 103 RHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIP 182
Cdd:PRK10771 103 NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLT 182
|
170 180
....*....|....*....|....*.
gi 515592652 183 ILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK10771 183 LLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-220 |
9.07e-36 |
|
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: 136.19 E-value: 9.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPD---SGKIIVGERALYDSNkninIAIDKRKIGYVFQE--ARLFP- 89
Cdd:COG1123 24 GVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS----EALRGRRIGMVFQDpmTQLNPv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 ---HYKVKGNLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:COG1123 100 tvgDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515592652 167 EVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRS 220
Cdd:COG1123 180 EILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
16-208 |
2.28e-35 |
|
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: 129.22 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNINIAidKRKIGYVFQEARLFPHYKVK 94
Cdd:cd03256 19 DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdGTDINKLKGKALRQL--RRQIGMIFQQFNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGA----------SRHYDRNHFDQIVQLLDLSTLLDRY--PVD-LSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:cd03256 97 ENVLSGRlgrrstwrslFGLFPKEEKQRALAALERVGLLDKAyqRADqLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 162 LPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03256 177 PASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-208 |
3.14e-35 |
|
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: 129.69 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD-LPRK--QE 167
Cdd:cd03294 122 NVAFglevqGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpLIRRemQD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515592652 168 VmpfLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03294 202 E---LLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-212 |
4.03e-35 |
|
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: 127.65 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsnKNINIAIDKRKIGYVFQEA---RLFPhYK 92
Cdd:cd03235 17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV---------FGKPLEKERKRIGYVPQRRsidRDFP-IS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLL------YGASRHYDRNHFDQIVQLLD---LSTLLDRyPVD-LSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:cd03235 87 VRDVVLmglyghKGLFRRLSKADKAKVDEALErvgLSELADR-QIGeLSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515592652 163 PRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIeDGQIKASG 212
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-217 |
8.55e-35 |
|
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: 127.79 E-value: 8.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnknINIAIDKR---KIGYVFQEARLFPHYK 92
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI------TGLPPHRIarlGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLLYGASRHYDRNHFDQivqllDLSTLLDRYPV----------DLSGGEKQRCAIARALLSEPEMLLMDEPlaSLDL 162
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRA-----DLERVYELFPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEP--SLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 163 -PR-KQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG0410 168 aPLiVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-207 |
1.05e-34 |
|
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: 125.19 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFpHYKVKG 95
Cdd:cd03228 20 DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL----RDLDLESLRKNIAYVPQDPFLF-SGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLygasrhydrnhfdqivqlldlstlldrypvdlSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:cd03228 95 NIL--------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 176 SQEINipILYVTHSLEEILHlADHMLLIEDGQ 207
Cdd:cd03228 143 AKGKT--VIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-215 |
1.94e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.05 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 12 QFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlYDSNKNINIAID---KRKIGYVFQEARLF 88
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ-FDFSQKPSEKAIrllRQKVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 PHYKVKGNLL------YGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:COG4161 95 PHLTVMENLIeapckvLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 163 PRKQEVMPFLEKLSQeINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:COG4161 175 EITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
16-222 |
2.08e-34 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 129.97 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:TIGR01186 11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQFALFPHMTILQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:TIGR01186 91 NTslgpeLLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTA 222
Cdd:TIGR01186 171 ELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPA 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-217 |
2.15e-34 |
|
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: 127.12 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIP--QHgiTAIFGRSGAGKTSIINAISGLNNPDSGKIIV--GERalydsNKNINIAIDKRKIGYVFQE--ARLFP 89
Cdd:COG1119 21 DISWTVKpgEH--WAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGER-----RGGEDVWELRKRIGLVSPAlqLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 HYKVKGNLLYGA------SRHY---DRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASL 160
Cdd:COG1119 94 DETVLDVVLSGFfdsiglYREPtdeQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 161 DLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG1119 174 DLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-216 |
2.69e-34 |
|
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: 132.57 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFpHYKVKG 95
Cdd:COG4988 355 GLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL----SDLDPASWRRQIAWVPQNPYLF-AGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGAsRHYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:COG4988 430 NLRLGR-PDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 165 KQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASGDIET 216
Cdd:COG4988 509 EAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-197 |
5.34e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 126.13 E-value: 5.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALY--DSNKniniaidkrkiGYVFQEARLFPHYKV 93
Cdd:COG4525 25 DVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpGADR-----------GVVFQKDALLPWLNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD-LPRKQe 167
Cdd:COG4525 94 LDNVafglrLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDaLTREQ- 172
|
170 180 190
....*....|....*....|....*....|
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSLEEILHLA 197
Cdd:COG4525 173 MQELLLDVWQRTGKGVFLITHSVEEALFLA 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
16-212 |
7.33e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 128.61 E-value: 7.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIpQHGITAIF-GRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnkninIAIDKRKIGYVFQEARLFPHYKVK 94
Cdd:PRK11000 21 DINLDI-HEGEFVVFvGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND------VPPAERGVGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:PRK11000 94 ENMsfglkLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-213 |
8.90e-34 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 124.20 E-value: 8.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralyDSNKNINIAIDKRKIGYVFQEARLFPHYKVKGNLLYGASRHY 105
Cdd:TIGR01277 26 IVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV------NDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 DRNHFDQ-----IVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEIN 180
Cdd:TIGR01277 100 KLNAEQQekvvdAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQ 179
|
170 180 190
....*....|....*....|....*....|...
gi 515592652 181 IPILYVTHSLEEILHLADHMLLIEDGQIKASGD 213
Cdd:TIGR01277 180 RTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-212 |
1.45e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.76 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 7 KQQLEQFMLDINvdipqHG--ITaIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydSNKNIN-IAIDKRKIGYVFQ 83
Cdd:PRK09452 27 KEVISNLDLTIN-----NGefLT-LLGPSGCGKTTVLRLIAGFETPDSGRIML-------DGQDIThVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 EARLFPHYKVKGNLLYG------ASRHYDRNHFD--QIVQLLDLStllDRYPVDLSGGEKQRCAIARALLSEPEMLLMDE 155
Cdd:PRK09452 94 SYALFPHMTVFENVAFGlrmqktPAAEITPRVMEalRMVQLEEFA---QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 156 PLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-208 |
3.64e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.07 E-value: 3.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYD-SNKNINIAidKRKIGYVFQEARLFPHYKVK 94
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKA--RRQIGMIFQHFNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:PRK11153 101 DNValpleLAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK11153 181 ELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-209 |
5.24e-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: 121.98 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLEQFMLD-INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNINIAIDKRKIGY 80
Cdd:cd03226 3 ENISFSYKKGTEILDdLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN-------GKPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 81 VFQEAR--LFPHyKVKGNLLYGASRHYDRNH-FDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPL 157
Cdd:cd03226 76 VMQDVDyqLFTD-SVREELLLGLKELDAGNEqAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 158 ASLDLPRKQEVMPFLEKLSQEINIpILYVTHSLEEILHLADHMLLIEDGQIK 209
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKA-VIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
16-215 |
7.58e-33 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 122.55 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINiAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI--TGLPPH-EIARLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNHF---------------DQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASL 160
Cdd:cd03219 95 NVMVAAQARTGSGLLlararreereareraEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 161 DLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:cd03219 175 NPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-212 |
1.11e-32 |
|
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: 121.46 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGEralYDSNKNINIAidKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAA--RQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:cd03263 95 HLrfyarLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 171 FLEKLSQeiNIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03263 175 LILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-217 |
4.83e-32 |
|
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: 127.26 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFPhykvkG 95
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL----RQIDPASLRRQIGVVLQDVFLFS-----G 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 ----NLLYGASrHYDrnhFDQIVQLLDLSTLLD---RYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPL 157
Cdd:COG2274 564 tireNITLGDP-DAT---DEEIIEAARLAGLHDfieALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 158 ASLDLPRKQEVMPFLEKLSQeiNIPILYVTHSLeEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG2274 640 SALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-215 |
7.26e-32 |
|
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: 120.53 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalydsnkNIN------IAidKRKIGYVFQEARLFP 89
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-------DITglpphrIA--RLGIARTFQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 HYKVKGNLLYGASRHYDRNHFDQIVQL--------------------LDLSTLLDRYPVDLSGGEKQRCAIARALLSEPE 149
Cdd:COG0411 93 ELTVLENVLVAAHARLGRGLLAALLRLprarreereareraeellerVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515592652 150 MLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
16-217 |
1.33e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 119.17 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVG----------ERAlydsnkniniaidKRKIGYVFQEA 85
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDgeditklpphERA-------------RAGIAYVPQGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 86 RLFPHYKVKGNLLYGASRHYDRNHF--DQIVQLLD-LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:TIGR03410 85 EIFPRLTVEENLLTGLAALPRRSRKipDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 163 PRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-215 |
1.75e-31 |
|
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: 118.63 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNiniaidKRKIGYVFQEARLFPHYKVK 94
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVREPREV------RRRIGIVFQDLSVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03265 92 ENLyiharLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:cd03265 172 EYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-217 |
4.72e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.89 E-value: 4.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSnkniniAIDKRKI----GYVFQEARLFPHY 91
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDP------KVDERLIrqeaGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYG------ASRHYDRnhfDQIVQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PRK09493 93 TALENVMFGplrvrgASKEEAE---KQARELLAkvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 163 PRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:PRK09493 170 ELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-217 |
1.48e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.06 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLN--NPD---SGKIIVGERALYDsnKNINIAIDKRKIGYVFQEARLFPH 90
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIYD--PDVDVVELRRRVGMVFQKPNPFPK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 --YKvkgNLLYGASRH--YDRNHFDQIVQlldlSTL------------LDRYPVDLSGGEKQRCAIARALLSEPEMLLMD 154
Cdd:COG1117 107 siYD---NVAYGLRLHgiKSKSELDEIVE----ESLrkaalwdevkdrLKKSALGLSGGQQQRLCIARALAVEPEVLLMD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515592652 155 EPLASLDlprkqevmP--------FLEKLSQEINIPIlyVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG1117 180 EPTSALD--------PistakieeLILELKKDYTIVI--VTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-208 |
1.79e-30 |
|
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: 115.58 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiNIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR-AIPYLRRKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:cd03292 98 NVAFalevtGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 171 FLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03292 178 LLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-212 |
6.52e-30 |
|
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: 114.00 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgerALYDSNKNINIAidKRKIGYVFQEARLFPHYKVKGNL-----LYG 100
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV---DGFDVVKEPAEA--RRRLGFVSDSTGLYDRLTARENLeyfagLYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 101 ASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLsQEIN 180
Cdd:cd03266 108 LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALG 186
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 181 IPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03266 187 KCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-213 |
7.58e-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: 120.26 E-value: 7.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnknINIAIDKRKIGYVFQEARLFpHYKVKG 95
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD----LDEDDLRRRIAVVPQRPHLF-DTTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDrnhfDQIVQLLD---LSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:COG4987 428 NLRLARPDATD----EELWAALErvgLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 162 LPRKQEVMPFLEKLSQeiNIPILYVTHSLEEiLHLADHMLLIEDGQIKASGD 213
Cdd:COG4987 504 AATEQALLADLLEALA--GRTVLLITHRLAG-LERMDRILVLEDGRIVEQGT 552
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-223 |
1.49e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.84 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 14 MLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQ--EARLFPHY 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVK----GNLLYGASRHYDRNHFDQIVQLLDLS-TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:PRK13649 103 VLKdvafGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 167 EVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAF 223
Cdd:PRK13649 183 ELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDF 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
16-220 |
1.64e-29 |
|
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: 113.41 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkniniaIDKRK---IGYVFQEARLFPHYK 92
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP------MHKRArlgIGYLPQEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLL-----YGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:cd03218 92 VEENILavleiRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 168 VMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRS 220
Cdd:cd03218 172 IQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-212 |
2.34e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnKNINIAIDKRKIGYVFQ--EARLFPHYKV 93
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD--KKVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KG------NLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:PRK13637 103 KDiafgpiNLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK13637 183 ILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
16-214 |
5.27e-29 |
|
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: 112.17 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydSNKNINIAIDKRKIgyVFQEARLFPHYKVKG 95
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-------EGKQITEPGPDRMV--VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NL-------LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEV 168
Cdd:TIGR01184 74 NIalavdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 169 MPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDI 214
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-212 |
1.05e-28 |
|
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: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSN-KNIniaidKRKIGYVFQ---------- 83
Cdd:TIGR04520 20 NVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDEENlWEI-----RKKVGMVFQnpdnqfvgat 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 ---------EARLFPHYKVkgnllygasrhydRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMD 154
Cdd:TIGR04520 95 veddvafglENLGVPREEM-------------RKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 155 EPLASLDlPR-KQEVMPFLEKLSQEINIPILYVTHSLEEILhLADHMLLIEDGQIKASG 212
Cdd:TIGR04520 162 EATSMLD-PKgRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
16-212 |
1.53e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.45 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydSNKNINIAiDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-------DGKPLDIA-ARNRIGYLPEERGLYPKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPRKQEVMp 170
Cdd:cd03269 90 QLVYlaqlkGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD-PVNVELL- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515592652 171 fLEKLSQ--EINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03269 168 -KDVIRElaRAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
17-210 |
1.70e-28 |
|
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: 110.52 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKGN 96
Cdd:TIGR02211 24 VSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHHLLPDFTALEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 97 -----LLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:TIGR02211 104 vamplLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDL 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 515592652 172 LEKLSQEINIPILYVTHSLEEILHLaDHMLLIEDGQIKA 210
Cdd:TIGR02211 184 MLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-223 |
1.97e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.13 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 14 MLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQ--EARLFPHY 91
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVK----GNLLYGASRHYDRNHFDQIVQLLDLST-LLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:PRK13643 102 VLKdvafGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 167 EVMPFLEKLSQEINIPILyVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAF 223
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDF 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
16-212 |
2.60e-28 |
|
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: 109.59 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQhGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNIniaidKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03264 18 GVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-----RRRIGYLPQEFGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGA------SRHYDRnHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03264 92 FLDYIAwlkgipSKEVKA-RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 170 PFLEKLSQEiNIPILyVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03264 171 NLLSELGED-RIVIL-STHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-218 |
2.96e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 110.61 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNIN-----IAIDKRKIGYVFQEARLFPHY 91
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI-DTARSLSqqkglIRQLRQHVGFVFQNFNLFPHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYG------ASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:PRK11264 101 TVLENIIEGpvivkgEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 166 QEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMW 218
Cdd:PRK11264 181 GEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-212 |
5.00e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.88 E-value: 5.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFpHYKVKG 95
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI----RDLTLESLRRQIGVVPQDTFLF-SGTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG---ASRhydrnhfDQIVQ---LLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:COG1132 433 NIRYGrpdATD-------EEVEEaakAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515592652 159 SLDLPRKQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:COG1132 506 ALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-208 |
6.65e-28 |
|
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: 109.06 E-value: 6.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARHVGFVFQSFQLLPTLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNHFDQIVQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFL 172
Cdd:COG4181 110 NVMLPLELAGRRDARARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 173 EKLSQEINIPILYVTHSlEEILHLADHMLLIEDGQI 208
Cdd:COG4181 190 FELNRERGTTLVLVTHD-PALAARCDRVLRLRAGRL 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
16-217 |
7.10e-28 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 109.29 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkniniaIDKRK---IGYVFQEARLFPHYK 92
Cdd:TIGR04406 19 DVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLP------MHERArlgIGYLPQEASIFRKLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLLYGASRHYDRNHfDQIVQLLD-------LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:TIGR04406 93 VEENIMAVLEIRKDLDR-AEREERLEalleefqISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 166 QEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:TIGR04406 172 GDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-208 |
3.77e-27 |
|
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: 105.20 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAIDkRKIGYVFQearlfphykvkg 95
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV--SFASPRDARR-AGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 nllygasrhydrnhfdqivqlldlstlldrypvdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:cd03216 83 ----------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|...
gi 515592652 176 SQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03216 129 RAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-206 |
3.77e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.86 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKniniaidKRkiGYVFQEARLFPHYKVKG 95
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-------ER--GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:PRK11248 90 NVafglqLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDG 206
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-203 |
4.06e-27 |
|
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: 111.99 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnknINIAIDKRKIGYVFQEARLFPHyKVKG 95
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD----ADADSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG---ASRHY-----DRNHFDQIVQLL--DLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:TIGR02857 415 NIRLArpdASDAEirealERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 166 QEVMPFLEKLSQeiNIPILYVTHSLeEILHLADHMLLI 203
Cdd:TIGR02857 495 AEVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-201 |
1.47e-26 |
|
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: 107.45 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNP---DSGKIIVGERALYD-SNKNINiAIDKRKIGYVFQE--ARLFP 89
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlSEKELR-KIRGREIQMIFQDpmTSLNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 HYKVKGNLLYGASRHYDRNH---FDQIVQLLDL------STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASL 160
Cdd:COG0444 102 VMTVGDQIAEPLRIHGGLSKaeaRERAIELLERvglpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515592652 161 DLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHML 201
Cdd:COG0444 182 DVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-212 |
2.25e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.55 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSnKNINIAidkRKIGYVFQE----ARL---- 87
Cdd:COG4604 19 DVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT-PSRELA---KRLAILRQEnhinSRLtvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 88 ------FPHYKvkGNLlygaSRHyDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:COG4604 95 lvafgrFPYSK--GRL----TAE-DREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 162 LPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:COG4604 168 MKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-212 |
2.38e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 105.11 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNIniaidKRKIGYVF-QEARLFPHYKVK 94
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF-----LRRIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRyPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEV 168
Cdd:cd03267 114 DSFyllaaIYDLPPARFKKRLDELSELLDLEELLDT-PVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515592652 169 MPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-212 |
6.99e-26 |
|
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: 108.65 E-value: 6.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnknINIAIDKRKIGYVFQEARLFPHyKVKG 95
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD----YTLASLRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:TIGR02203 425 NIAYGRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515592652 165 KQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:TIGR02203 505 ERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-212 |
1.01e-25 |
|
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: 102.68 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralyDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF------DGKSYQKNIEALRRIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGAsRHYDRNH--FDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLE 173
Cdd:cd03268 92 NLRLLA-RLLGIRKkrIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 515592652 174 KLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03268 171 SLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-242 |
1.02e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.39 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGlNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFpHYKVKGN 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIEL----RELDPESWRKHLSWVGQNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 97 LLYGASRHYDrnhfDQIVQLLDLSTLLD---------RYPVD-----LSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PRK11174 443 VLLGNPDASD----EQLQQALENAWVSEflpllpqglDTPIGdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 163 PRKQEVMPFLEKLSQeiNIPILYVTHSLEEiLHLADHMLLIEDGQIKASGDIETMwrstafqpwqknSELSTLFKGMLTE 242
Cdd:PRK11174 519 HSEQLVMQALNAASR--RQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAEL------------SQAGGLFATLLAH 583
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-212 |
1.22e-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: 103.07 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFPHyKVKG 95
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI----RDISRKSLRSMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYD--------RNHFDQIVQLL--DLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:cd03254 96 NIRLGRPNATDeevieaakEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 166 QEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:cd03254 176 KLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-213 |
1.32e-25 |
|
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: 103.08 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnknINIAIDKRKIGYVFQEARLFpHYKVKG 95
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD----YTLASLRRQIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHyDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:cd03251 95 NIAYGRPGA-TREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 165 KQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASGD 213
Cdd:cd03251 174 ERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-212 |
1.33e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.32 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 18 NVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAID-KRKIGYVFQearlFPHYK---- 92
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlRKEIGLVFQ----FPEYQlfqe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 -VKGNLLYGASrHYDRNH---FDQIVQLLDLSTLLDRY----PVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:PRK13645 107 tIEKDIAFGPV-NLGENKqeaYKKVPELLKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515592652 165 KQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-208 |
1.84e-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: 103.35 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIdKRKIGYVFQ 83
Cdd:TIGR02769 17 LFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAF-RRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 EA-RLFPHYKVKGNLLYGASRHYDR----NHFDQIVQLLDLSTL----LDRYPVDLSGGEKQRCAIARALLSEPEMLLMD 154
Cdd:TIGR02769 96 DSpSAVNPRMTVRQIIGEPLRHLTSldesEQKARIAELLDMVGLrsedADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515592652 155 EPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-240 |
2.34e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.12 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydSNKNINIAIDK----------------RKIGYVFQEARLFP 89
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVV-------NGQTINLVRDKdgqlkvadknqlrllrTRLTMVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 HYKVKGNLL------YGASRHYDRnhfDQIVQLLDLSTLLDR----YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:PRK10619 106 HMTVLENVMeapiqvLGLSKQEAR---ERAVKYLAKVGIDERaqgkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 160 LDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTafqpwqKNSELSTLFKGM 239
Cdd:PRK10619 183 LDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP------QSPRLQQFLKGS 255
|
.
gi 515592652 240 L 240
Cdd:PRK10619 256 L 256
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-212 |
9.76e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.63 E-value: 9.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNI-NIaidKRKIGY 80
Cdd:PRK13635 11 ISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--SEETVwDV---RRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 81 VFQEA-RLFPHYKVKGNLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMD 154
Cdd:PRK13635 86 VFQNPdNQFVGATVQDDVAFgleniGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 155 EPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-208 |
1.52e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQ--EARLFPHYKV 93
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 K----GNLLYGASRHYDRNHFDQIVQLLDLST-LLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPRKQEV 168
Cdd:PRK13641 105 KdvefGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD-PEGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515592652 169 MPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-212 |
2.16e-24 |
|
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: 99.61 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFpHYKVKG 95
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDSLRRAIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG--------------ASRHYDRnhfdqIVQLLD-LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASL 160
Cdd:cd03253 94 NIRYGrpdatdeevieaakAAQIHDK-----IMRFPDgYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 161 DLPRKQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:cd03253 169 DTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-205 |
2.34e-24 |
|
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: 98.71 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNIniaidKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-----RRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNHFDQIVQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFL 172
Cdd:COG4133 95 NLRFWAALYGLRADREAIDEALEavgLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
170 180 190
....*....|....*....|....*....|...
gi 515592652 173 EKLSQEINIpILYVTHSLEEIlhLADHMLLIED 205
Cdd:COG4133 175 AAHLARGGA-VLLTTHQPLEL--AAARVLDLGD 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-215 |
2.71e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNIniaidKRKIGYVFQ--EARLFPHyKV 93
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREV-----RKFVGLVFQnpDDQIFSP-TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYGA-----SRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEV 168
Cdd:PRK13652 97 EQDIAFGPinlglDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 169 MPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-212 |
2.78e-24 |
|
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: 99.20 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIivgeraLYDsnkNINIA-ID----KRKIGYVFQEARLFpHYKVKGNLLYGAS 102
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSV------LLD---GTDIRqLDpadlRRNIGYVPQDVTLF-YGTLRDNITLGAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 103 RHYDRNHFdQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlprKQEVMPF 171
Cdd:cd03245 104 LADDERIL-RAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD---MNSEERL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 172 LEKLSQEI-NIPILYVTHSLeEILHLADHMLLIEDGQIKASG 212
Cdd:cd03245 180 KERLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
16-247 |
3.05e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralyDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML------DGVDLSHVPPYQRPINMMFQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG-----ASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLP---RKQ- 166
Cdd:PRK11607 111 NIAFGlkqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdRMQl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 167 EVMPFLEKlsqeINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRstafqpwQKNSELS-------TLFKGM 239
Cdd:PRK11607 191 EVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE-------HPTTRYSaefigsvNVFEGV 259
|
....*...
gi 515592652 240 LTEHHPKY 247
Cdd:PRK11607 260 LKERQEDG 267
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-213 |
3.32e-24 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 99.15 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGEralyDSNKNINIAIDKRKIGYVFQEARLFPHyKVKG 95
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRDLNLRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG-----------ASRHYdrNHFDQIVQLLD-LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLP 163
Cdd:cd03249 96 NIRYGkpdatdeeveeAAKKA--NIHDFIMSLPDgYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515592652 164 RKQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASGD 213
Cdd:cd03249 174 SEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-220 |
5.69e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.44 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 8 QQLEQFML-DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiniaiDKRK-IGYVFQEA 85
Cdd:PRK13648 18 QSDASFTLkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE-----KLRKhIGIVFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 86 -RLFPHYKVKGNLLYGASRH---YDRNH--FDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:PRK13648 93 dNQFVGSIVKYDVAFGLENHavpYDEMHrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515592652 160 LDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHlADHMLLIEDGQIKASGDIETMWRS 220
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-214 |
9.76e-24 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 97.85 E-value: 9.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLeqFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalyDSNKNiniaiDKRKIGYV 81
Cdd:TIGR03740 6 LSKRFGKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH---PWTRK-----DLHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 82 FQEARLFPHYKVKGNLLYGAS-RHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASL 160
Cdd:TIGR03740 76 IESPPLYENLTARENLKVHTTlLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515592652 161 DLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDI 214
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
16-213 |
1.00e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.18 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNI-NIAIDKRK---IGYVFQEARLFPHY 91
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD-------GEDItHLPMHKRArlgIGYLPQEASIFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLL-----YGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlP--- 163
Cdd:COG1137 94 TVEDNILavlelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD-Piav 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 164 -RKQEVMPFLeklsQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGD 213
Cdd:COG1137 173 aDIQKIIRHL----KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-198 |
1.08e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.70 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNN-----PDSGKIIVGERALYDSNknINIAIDKRKIGYVFQEARLFPH 90
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPD--VDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 yKVKGNLLYGASRHYDRNHFDQIVQL-LDLSTLLDRYP-------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PRK14243 106 -SIYDNIAYGARINGYKGDMDELVERsLRQAALWDEVKdklkqsgLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 163 PRKQEVMPFLEKLSQEINIPIlyVTHSLEEILHLAD 198
Cdd:PRK14243 185 ISTLRIEELMHELKEQYTIII--VTHNMQQAARVSD 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-213 |
2.23e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.77 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGE-----------RALYDSNKNI-NIAIDKRKIGYVFQ 83
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnheLITNPYSKKIkNFKELRRRVSMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 earlFPHYK-----VKGNLLYG-------ASRHYDRNHFDQIVQLLDlSTLLDRYPVDLSGGEKQRCAIARALLSEPEML 151
Cdd:PRK13631 124 ----FPEYQlfkdtIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLD-DSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515592652 152 LMDEPLASLDlPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGD 213
Cdd:PRK13631 199 IFDEPTAGLD-PKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-217 |
2.47e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAIDKRkIGYVFQEARLFPHYKVKG 95
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV--RFRSPRDAQAAG-IAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGasRHYDRNHF----------DQIVQLLDLSTLLDRyPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:COG1129 99 NIFLG--REPRRGGLidwramrrraRELLARLGLDIDPDT-PVgDLSVAQQQLVEIARALSRDARVLILDEPTASLTERE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 165 KQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG1129 176 VERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
16-208 |
2.82e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.15 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYD-SNKNINIAIdkrkigyVFQEARLFPHYKVK 94
Cdd:PRK11650 22 GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEPADRDIAM-------VFQNYALYPHMSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYG-ASRHYDRNHFDQIVQ----LLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlpRKQEVM 169
Cdd:PRK11650 95 ENMAYGlKIRGMPKAEIEERVAeaarILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD--AKLRVQ 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515592652 170 PFLE--KLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK11650 173 MRLEiqRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-208 |
3.74e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.83 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLN--NPDS---GKIIVGERALYdsNKNINIAIDKRKIGYVFQEARLFPH 90
Cdd:PRK14267 22 GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelNEEArveGEVRLFGRNIY--SPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 YKVKGNLLYGASRH---YDRNHFDQIVQ-LLDLSTLLDR-------YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvKSKKELDERVEwALKKAALWDEvkdrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 160 LDLPRKQEVMPFLEKLSQEINIPIlyVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEYTIVL--VTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-198 |
3.82e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.03 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDS-----GKIIVGERALYDSNKNINIAidKRKI 78
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRL--RRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 79 GYVFQEARLFPhYKVKGNLLYGAS--RHYDRNHFDQIVQ-------LLD-LSTLLDRYPVDLSGGEKQRCAIARALLSEP 148
Cdd:PRK14258 91 SMVHPKPNLFP-MSVYDNVAYGVKivGWRPKLEIDDIVEsalkdadLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515592652 149 EMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLAD 198
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-208 |
4.51e-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: 94.93 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNP--DSGKIIVGERALYDSNKniniaidKRKIGYVFQEARLFPHYKVKGNLLYGAsr 103
Cdd:cd03213 37 LTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSF-------RKIIGYVPQDDILHPTLTVRETLMFAA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 104 hydrnhfdqivqlldlstLLDRypvdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNIPI 183
Cdd:cd03213 108 ------------------KLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTI 164
|
170 180
....*....|....*....|....*.
gi 515592652 184 LYVTHSL-EEILHLADHMLLIEDGQI 208
Cdd:cd03213 165 ICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-220 |
7.93e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.88 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINI-AIDKRK-IGYVFQEARLFPHYKV 93
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIdAIKLRKeVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYGASRH--YDRNHFDQIVQ--------LLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLP 163
Cdd:PRK14246 108 YDNIAYPLKSHgiKEKREIKKIVEeclrkvglWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 164 RKQEVMPFLEKLSQEINIPIlyVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRS 220
Cdd:PRK14246 188 NSQAIEKLITELKNEIAIVI--VSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
7.99e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.21 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 1 MIK---LAFKQQLEQFML--DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKI-IVGERALYDSNKNIniaid 74
Cdd:PRK13632 7 MIKvenVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITISKENLKEI----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 75 KRKIGYVFQEA-RLFPHYKVKGNLLYG-ASRHYDRNHFDQIV----QLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEP 148
Cdd:PRK13632 82 RKKIGIIFQNPdNQFIGATVEDDIAFGlENKKVPPKKMKDIIddlaKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 149 EMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILhLADHMLLIEDGQIKASGD 213
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-235 |
9.63e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLEQFML-DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNIniaidKRKIG 79
Cdd:PRK13650 10 LTFKYKEDQEKYTLnDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDI-----RHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 80 YVFQEA-RLFPHYKVKGNLLYG-----ASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLM 153
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGlenkgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 154 DEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILhLADHMLLIEDGQIKASgdietmwrSTAFQPWQKNSELS 233
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVEST--------STPRELFSRGNDLL 235
|
..
gi 515592652 234 TL 235
Cdd:PRK13650 236 QL 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-215 |
9.85e-23 |
|
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: 99.11 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGK--IIVGERALyDSNKN--INIAIDKRKIGYVFQEARLFPHYK 92
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWV-DMTKPgpDGRGRAKRYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLLYGASRHYDrnhfDQIVQLLDLSTL-------------LDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:TIGR03269 382 VLDNLTEAIGLELP----DELARMKAVITLkmvgfdeekaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515592652 160 LDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-223 |
9.91e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.69 E-value: 9.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIivgERALYDSNKN----------INIAIDK---------- 75
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI---EWIFKDEKNKkktkekekvlEKLVIQKtrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 76 ---RKIGYVFQ--EARLFPHYKVK----GNLLYGASRHYDRNHFDQIVQLLDLS-TLLDRYPVDLSGGEKQRCAIARALL 145
Cdd:PRK13651 102 eirRRVGVVFQfaEYQLFEQTIEKdiifGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 146 SEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAF 223
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKF 258
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-212 |
1.07e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYD-SNKNIniaidKRKIGYVFQEaRLFPH-YKV 93
Cdd:PRK11231 20 DLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQL-----ARRLALLPQH-HLTPEgITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYGASRHY---------DRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:PRK11231 94 RELVAYGRSPWLslwgrlsaeDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515592652 165 KQEVMPFLEKLSQEINIPILyVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK11231 174 QVELMRLMRELNTQGKTVVT-VLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-208 |
1.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQ--EARLFPHyKV 93
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFED-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYGAsRHYDRN-------HFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:PRK13646 104 EREIIFGP-KNFKMNldevknyAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 167 EVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-217 |
1.97e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.22 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GE-------RALYDSNKniniaidkrKIGYVFQEARL 87
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGEnipamsrSRLYTVRK---------RMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 88 FPHYKVKGNLLYGASRHydrnhfDQIVQLLDLSTLL------------DRYPVDLSGGEKQRCAIARALLSEPEMLLMDE 155
Cdd:PRK11831 96 FTDMNVFDNVAYPLREH------TQLPAPLLHSTVMmkleavglrgaaKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515592652 156 PLASLDlprkQEVMPFLEKLSQEIN----IPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:PRK11831 170 PFVGQD----PITMGVLVKLISELNsalgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-215 |
2.52e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.56 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSnkniniaiDKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE--------DRRRIGYLPEERGLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLY-----GASRHYDRNHFDQIVQLLDLSTLLDRyPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPRKQEVM 169
Cdd:COG4152 91 QLVYlarlkGLSKAEAKRRADEWLERLGLGDRANK-KVeELSKGNQQKVQLIAALLHDPELLILDEPFSGLD-PVNVELL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 170 pfleklSQEI------NIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:COG4152 169 ------KDVIrelaakGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-212 |
2.74e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAidkRKIGYVFQEARL-FPhYKVK 94
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-ADWSPAELA---RRRAVLPQHSSLsFP-FTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 -----GNLLYGASRHYDRNHFDQIVQLLDLSTLLDR-YPVdLSGGEKQRCAIARAL--LSEPEM----LLMDEPLASLDL 162
Cdd:PRK13548 95 evvamGRAPHGLSRAEDDALVAAALAQVDLAHLAGRdYPQ-LSGGEQQRVQLARVLaqLWEPDGpprwLLLDEPTSALDL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515592652 163 PRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK13548 174 AHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-210 |
3.29e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.73 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 N-----LLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:PRK11629 107 NvamplLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 171 FLEKLSQEINIPILYVTHSleeiLHLADHM---LLIEDGQIKA 210
Cdd:PRK11629 187 LLGELNRLQGTAFLVVTHD----LQLAKRMsrqLEMRDGRLTA 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-209 |
3.57e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.69 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKGN-----LLYGAS 102
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENvelpaLLRGES 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 103 RHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIP 182
Cdd:PRK10584 120 SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTT 199
|
170 180
....*....|....*....|....*..
gi 515592652 183 ILYVTHSlEEILHLADHMLLIEDGQIK 209
Cdd:PRK10584 200 LILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-208 |
4.24e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.37 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIdKRKIGYVFQ 83
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF-RRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 EA--RLFPHYKVkGNLLYGASRHY------DRNH-FDQIVQLLDLS-TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLM 153
Cdd:PRK10419 97 DSisAVNPRKTV-REIIREPLRHLlsldkaERLArASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 154 DEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
28-213 |
4.54e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 94.13 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkninIAIDKRKIGYVFQEAR--LFPHYKVkGNLLYGASRH- 104
Cdd:COG4167 43 AIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD----YKYRCKHIRMIFQDPNtsLNPRLNI-GQILEEPLRLn 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 105 -----YDRNhfDQIVQLLDLSTLL----DRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:COG4167 118 tdltaEERE--ERIFATLRLVGLLpehaNFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLEL 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 176 SQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGD 213
Cdd:COG4167 196 QEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
6.02e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.14 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNIniaIDKRK-IGYVFQEArlfphykvk 94
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGL---MKLREsVGMVFQDP--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGASRHYD---------------RNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:PRK13636 92 DNQLFSASVYQDvsfgavnlklpedevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 160 LDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMW 218
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-207 |
8.41e-22 |
|
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: 91.76 E-value: 8.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalydsnkniniaidkrkIGYVFQEARLFPHyKVKG 95
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASrhYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPR 164
Cdd:cd03250 85 NILFGKP--FDEERYEKVIKACALEPDLEILPdgdlteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD-AH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 165 ------KQEVMPFLEKlsqeiNIPILYVTHSLeEILHLADHMLLIEDGQ 207
Cdd:cd03250 162 vgrhifENCILGLLLN-----NKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-212 |
8.67e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.71 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDS---GKIIV-----GERALYDSnkniniaidKRKIGYVFQEA-R 86
Cdd:PRK13640 25 DISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVdgitlTAKTVWDI---------REKVGIVFQNPdN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 87 LFPHYKVKGNLLYG-ASRHYDRNHFDQIVQ--LLDLSTL--LDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PRK13640 96 QFVGATVGDDVAFGlENRAVPRPEMIKIVRdvLADVGMLdyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 162 LPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQG 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-220 |
1.14e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNP-----DSGKIIVGERALYDSNKNINIaidKRKIGYVFQEARLFPhY 91
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEF---RRRVGMLFQRPNPFP-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYGASRH--YDRNHFDQIVQ-------LLD-LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PRK14271 116 SIMDNVLAGVRAHklVPRKEFRGVAQarltevgLWDaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 162 LPRKQEVMPFLEKLSQEINIPIlyVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRS 220
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVII--VTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
1.26e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.84 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNIniaidKRKIGYV 81
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-----SSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 82 FQEARLFPhykvkgnllygasrhydrnhfdqivqlldlSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:cd03247 81 NQRPYLFD------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 162 LPRKQEVMPFLekLSQEINIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:cd03247 131 PITERQLLSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-212 |
1.39e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAL--YDSNKninIAidkRKiGYV--FQEARLF---- 88
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQ---IA---RM-GVVrtFQHVRLFremt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 --------PHYKVKGNLLYG-----ASRHYDRNHFDQIVQLLDLSTLLD---RYPVDLSGGEKQRCAIARALLSEPEMLL 152
Cdd:PRK11300 97 vienllvaQHQQLKTGLFSGllktpAFRRAESEALDRAATWLERVGLLEhanRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 153 MDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-208 |
2.01e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NL----LY-GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:PRK10535 106 NVevpaVYaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 171 FLEKLSQEINIPILyVTHSlEEILHLADHMLLIEDGQI 208
Cdd:PRK10535 186 ILHQLRDRGHTVII-VTHD-PQVAAQAERVIEIRDGEI 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-217 |
2.58e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.23 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNiniaidKRKIGYVF-QEARLFPHYKV 93
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlGYVPFKRRKEF------ARRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNL-----LYGASRHYDRNHFDQIVQLLDLSTLLDRyPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:COG4586 114 IDSFrllkaIYRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG4586 193 IREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-208 |
3.76e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 31 GRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAIDKRKIGYVFQEARLFPHYKVKGN-----LLYGASRHY 105
Cdd:PRK10908 35 GHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-TRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNvaiplIIAGASGDD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 DRNhfdQIVQLLDLSTLLDR---YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQeINIP 182
Cdd:PRK10908 114 IRR---RVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVT 189
|
170 180
....*....|....*....|....*.
gi 515592652 183 ILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK10908 190 VLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-199 |
6.85e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.55 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAIdKRKIGYVFQEARLFPHYKVKG 95
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV--RIRSPRDAI-ALGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGA-SRHYDRNHFDQIVQllDLSTLLDRYPV---------DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:COG3845 100 NIVLGLePTKGGRLDRKAARA--RIRELSERYGLdvdpdakveDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190
....*....|....*....|....*....|....
gi 515592652 166 QEVMPFLEKLSQEiNIPILYVTHSLEEILHLADH 199
Cdd:COG3845 178 DELFEILRRLAAE-GKSIIFITHKLREVMAIADR 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-212 |
1.72e-20 |
|
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: 88.87 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNnpDSGKIIVGeRALYDsNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSG-QILFN-GQPRKPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGA-------SRHYDRNHFDQIVQLLDL--STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:cd03234 101 TLTYTAilrlprkSSDAIRKKRVEDVLLRDLalTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 167 EVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-239 |
1.90e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.63 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFPHYKVKG 95
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYG------ASRHYDRNHFDQIVQLlDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:PRK10070 126 NTAFGmelagiNAEERREKALDALRQV-GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAfqpwqkNSELSTLFKGM 239
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA------NDYVRTFFRGV 268
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-217 |
2.33e-20 |
|
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: 92.17 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNN--PDSGKII-----------------VGERA-------------LY 63
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskVGEPCpvcggtlepeevdFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 64 DSNKNINIAIdKRKIGYVFQeaRLFPHY---KVKGNLL-------YGASRHYDRnhfdqIVQLLDLSTLLDRY---PVDL 130
Cdd:TIGR03269 98 NLSDKLRRRI-RKRIAIMLQ--RTFALYgddTVLDNVLealeeigYEGKEAVGR-----AVDLIEMVQLSHRIthiARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 131 SGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKA 210
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE 249
|
....*..
gi 515592652 211 SGDIETM 217
Cdd:TIGR03269 250 EGTPDEV 256
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-224 |
5.92e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIaidKRKIGYVFQEARL-FPHYKVK 94
Cdd:PRK13644 20 NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGI---RKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGASR-----HYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:PRK13644 97 EDLAFGPENlclppIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 170 PFLEKLsQEINIPILYVTHSLEEiLHLADHMLLIEDGQIKASGDIETMWRSTAFQ 224
Cdd:PRK13644 177 ERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
16-212 |
6.09e-20 |
|
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: 87.96 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKI-----GYVFQEAR--LF 88
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLmrtewGFVHQNPRdgLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 PHYKVKGN----LLYGASRHYDRNHFDQIVQLLDLS---TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:TIGR02323 101 MRVSAGANigerLMAIGARHYGNIRATAQDWLEEVEidpTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 162 LPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:TIGR02323 181 VSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-208 |
8.34e-20 |
|
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: 85.56 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAIdKRKIGYVfQEAR----LFPHY 91
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV--TRRSPRDAI-RAGIAYV-PEDRkregLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLygasrhydrnhfdqivqlldLSTLLdrypvdlSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:cd03215 94 SVAENIA--------------------LSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 515592652 172 LEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:cd03215 147 IRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-212 |
8.97e-20 |
|
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: 90.95 E-value: 8.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFPHyKVKG 95
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL----KDIDRHTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPV-----------DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:TIGR01193 567 NLLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515592652 165 KQEVMPFLEKLSQEInipILYVTHSLeEILHLADHMLLIEDGQIKASG 212
Cdd:TIGR01193 647 EKKIVNNLLNLQDKT---IIFVAHRL-SVAKQSDKIIVLDHGKIIEQG 690
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-226 |
1.15e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAIdKRKIGYVFQ 83
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLAL-RQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 --EARLFpHYKVKGNLLY-----GASRHYDRNHFDQIVQLLDlSTLLDRYPVD-LSGGEKQRCAIARALLSEPEMLLMDE 155
Cdd:PRK13638 85 dpEQQIF-YTDIDSDIAFslrnlGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 156 PLASLDLPRKQEVMPFLEKLSQEINiPILYVTHSLEEILHLADHMLLIEDGQIKASGD-------IETMWRSTAFQPW 226
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGApgevfacTEAMEQAGLTQPW 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-212 |
1.92e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYD---SNKNINIAIdkrkigyVFQEARLFpHYK 92
Cdd:PRK11176 361 NINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytlASLRNQVAL-------VSQNVHLF-NDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLLYGASRHYDRNHFDQIVQL---------LD--LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PRK11176 433 IANNIAYARTEQYSREQIEEAARMayamdfinkMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 162 LPRKQEVMPFLEKLSQeiNIPILYVTHSLEEIlHLADHMLLIEDGQIKASG 212
Cdd:PRK11176 513 TESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-212 |
1.95e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNIniaidKRKIGYVFQEARL------- 87
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQHYASKEV-----ARRIGLLAQNATTpgditvq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 88 -------FPHYKvkgnlLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASL 160
Cdd:PRK10253 100 elvargrYPHQP-----LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 161 DLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-231 |
2.34e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.37 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLN--NPD---SGKIIVGERALYDSNKNiniAIDKRK-IGYVFQEARLFP 89
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYSPRTD---TVDLRKeIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 hYKVKGNLLYGASRH--YDRNHFDQIVQ--LLDLST---LLDRY---PVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:PRK14239 100 -MSIYENVVYGLRLKgiKDKQVLDEAVEksLKGASIwdeVKDRLhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515592652 160 LDLPRKQEVMPFLEKLSQEINipILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWrstaFQPWQKNSE 231
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF----MNPKHKETE 244
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-215 |
3.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.33 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSN-KNIniaidKRKIGYVFQEarlfPHYKVK- 94
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENeKWV-----RSKVGLVFQD----PDDQVFs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 ---------GNLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:PRK13647 95 stvwddvafGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515592652 166 QEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:PRK13647 175 ETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-208 |
3.35e-19 |
|
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: 83.80 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiniaiDKRK-IGYVFQEARLFPhykvk 94
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN-----ELGDhVGYLPQDDELFS----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLygasrhydrnhfDQIvqlldlstlldrypvdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEK 174
Cdd:cd03246 90 GSIA------------ENI----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA 141
|
170 180 190
....*....|....*....|....*....|....
gi 515592652 175 LSQEINIPILyVTHSLeEILHLADHMLLIEDGQI 208
Cdd:cd03246 142 LKAAGATRIV-IAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-233 |
3.51e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAiDKRKIGYVFQEARLFPHYKVKGNLLYGASRHY 105
Cdd:PRK15439 39 VHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC--ARLTPAKA-HQLGIYLVPQEPLLFPNLSVKENILFGLPKRQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 DR-NHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLsQEINIPIL 184
Cdd:PRK15439 116 ASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 185 YVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRS---TAFQPWQKNSELS 233
Cdd:PRK15439 195 FISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDdiiQAITPAAREKSLS 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-208 |
4.49e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsNKNI-NIAIDKR--KIGYVFQEARL--FPH 90
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-------GKDVtKLPEYKRakYIGRVFQDPMMgtAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 YKVKGNLLYGASRH-----------YDRNHFDQIVQLLDLStLLDR--YPVD-LSGGEKQRCAIARALLSEPEMLLMDEP 156
Cdd:COG1101 97 MTIEENLALAYRRGkrrglrrgltkKRRELFRELLATLGLG-LENRldTKVGlLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 157 LASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-220 |
5.19e-19 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 84.85 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVG--ERALYDSNKNiniaidKRKIGYVFQEARLFpHYKV 93
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghDLALADPAWL------RRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYG-----------ASRHYDRNHFdqIVQL-LDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:cd03252 93 RDNIALAdpgmsmervieAAKLAGAHDF--ISELpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 162 LPRKQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASGDIETMWRS 220
Cdd:cd03252 171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-212 |
5.60e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIaidKRKIGYVFQE------ARLFP 89
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI---RNKAGMVFQNpdnqivATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 HYKVKG--NLlyGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:PRK13633 105 EDVAFGpeNL--GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
26-212 |
7.15e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFPHYKVKGNLLYGASRHY 105
Cdd:PRK09536 31 LVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV----EALSARAASRRVASVPQDTSLSFEFDVRQVVEMGRTPHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 ---------DRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLS 176
Cdd:PRK09536 107 srfdtwtetDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 177 QEINIPILYVtHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK09536 187 DDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAG 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-190 |
1.82e-18 |
|
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: 86.65 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINiaidKRKIGYVFQEARLFpHYKVKG 95
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----RRRVSVCAQDAHLF-DTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNHFDQI--VQLLD--------LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:TIGR02868 428 NLRLARPDATDEELWAALerVGLADwlralpdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|....*
gi 515592652 166 QEVMPFLEKLSQEINipILYVTHSL 190
Cdd:TIGR02868 508 DELLEDLLAALSGRT--VVLITHHL 530
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-212 |
4.27e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.70 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKI-IVGE----RALYDsnkniniaidKRKIGYVFQEARLFPHYKVKGNLL----- 98
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEpvpsRARHA----------RQRVGVVPQFDNLDPDFTVRENLLvfgry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 99 YGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPRKQEVMpfLEKLSQE 178
Cdd:PRK13537 108 FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD-PQARHLM--WERLRSL 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 179 I--NIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK13537 185 LarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-212 |
4.54e-18 |
|
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: 81.81 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGER--ALYDsnknINIAIDKRKIGYvfQEARLfphykv 93
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLG----LGGGFNPELTGR--ENIYL------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 kGNLLYGASRHYDRNHFDQIVQLLDLSTLLDRyPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFL 172
Cdd:cd03220 108 -NGRLLGLSRKEIDEKIDEIIEFSELGDFIDL-PVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515592652 173 EKLSQEINIpILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:cd03220 186 RELLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-212 |
4.93e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKniniaIDKRKIGYVFQEARLFPHYKVKGNLL-YGasrHYDR 107
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-----LARARIGVVPQFDNLDLEFTVRENLLvFG---RYFG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 108 NHFDQ----IVQLLDLSTLLDRYPV---DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiN 180
Cdd:PRK13536 144 MSTREieavIPSLLEFARLESKADArvsDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-G 222
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 181 IPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK13536 223 KTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-212 |
6.83e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.28 E-value: 6.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERA-----LYDSNKNiniaiDKRKI-----GYVFQEAR--LFPHYKVKG 95
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEA-----ERRRLlrtewGFVHQHPRdgLRMQVSAGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 N----LLYGASRHYDR-----NHFDQIVQLlDLSTLLDRyPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQ 166
Cdd:PRK11701 111 NigerLMAVGARHYGDirataGDWLERVEI-DAARIDDL-PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 167 EVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK11701 189 RLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-212 |
8.63e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.18 E-value: 8.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISG-LNNPDS--GKIIVGERALydsNKNINIAIDKRKI-------------G 79
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprGARVTGDVTL---NGEPLAAIDAPRLarlravlpqaaqpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 80 YVFQEARL-----FPHYKVKgnllyGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARAL---------L 145
Cdd:PRK13547 96 FAFSAREIvllgrYPHARRA-----GALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 146 SEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-212 |
1.02e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.48 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGEralydsnKNINI----AIDKRKIGYVFQEARLFPHY 91
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDISLlplhARARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLL--------YGASRHYDRNhfDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLP 163
Cdd:PRK10895 94 SVYDNLMavlqirddLSAEQREDRA--NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 164 RKQEVMPFLEKLsQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK10895 172 SVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-208 |
1.28e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 80.98 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAL--YDsNKNINiaidkRKIGYVFQEARLFPHyKVKGNLLYG-AS 102
Cdd:cd03248 42 VTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqYE-HKYLH-----SKVSLVGQEPVLFAR-SLQDNIAYGlQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 103 RHYDR-------NHFDQIVQLLDL--STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLE 173
Cdd:cd03248 115 CSFECvkeaaqkAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY 194
|
170 180 190
....*....|....*....|....*....|....*
gi 515592652 174 KLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQI 208
Cdd:cd03248 195 DWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
27-207 |
1.36e-17 |
|
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: 80.56 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 27 TAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralYDSNKNINIA---------IDKRKIGYVFQEARLFPHYK----V 93
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGNYLPDSGSILV-----RHDGGWVDLAqaspreilaLRRRTIGYVSQFLRVIPRVSaldvV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLL-YGASRHYDRNHFDQIVQLLDL-STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:COG4778 115 AEPLLeRGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVEL 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 172 LEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:COG4778 195 IEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-214 |
1.50e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlYDSNKNINIAidKRKIGYVFQEARLFPHYKVKG 95
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDHKLAA--QLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGasRHYDRNHF--------------DQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PRK09700 100 NLYIG--RHLTKKVCgvniidwremrvraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 162 LPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDI 214
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
114-219 |
1.75e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.90 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 114 VQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEI 193
Cdd:PRK10418 125 VGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVV 204
|
90 100
....*....|....*....|....*.
gi 515592652 194 LHLADHMLLIEDGQIKASGDIETMWR 219
Cdd:PRK10418 205 ARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-258 |
1.94e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNINIaidKRKIGYVFQ--EARLF-PHYK 92
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKYDKKSLLEV---RKTVGIVFQnpDDQLFaPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VK---GNLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:PRK13639 98 EDvafGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 170 PFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASG-------DIETMWRSTAFQPWqknseLSTLFKGMLTE 242
Cdd:PRK13639 178 KLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGtpkevfsDIETIRKANLRLPR-----VAHLIEILNKE 251
|
250
....*....|....*...
gi 515592652 243 HHPKYALSYV--ELARNI 258
Cdd:PRK13639 252 DNLPIKMGYTigEARRNI 269
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
28-200 |
1.98e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.09 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiniAIDK--RKIGYVFQE--ARLFPHYKVKG-------- 95
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGR---ELRPlrRRMQMVFQDpyASLNPRMTVGDiiaeplri 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 -NLLYGASRHydrnhfDQIVQLLDLSTL----LDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLP-RKQeVM 169
Cdd:COG4608 125 hGLASKAERR------ERVAELLELVGLrpehADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSiQAQ-VL 197
|
170 180 190
....*....|....*....|....*....|.
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHM 200
Cdd:COG4608 198 NLLEDLQDELGLTYLFISHDLSVVRHISDRV 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-207 |
2.10e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQ--LEQFMLDINVDIPQHGITAIFGRSGAGKTsiINAISGLN---NPD----SGKIIV-GERALYDSNKNINiAI 73
Cdd:PRK15134 13 VAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSILRllpSPPvvypSGDIRFhGESLLHASEQTLR-GV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 74 DKRKIGYVFQE--ARLFPHYKVKGNL-----LY-GASRHYDRnhfDQIVQLLD------LSTLLDRYPVDLSGGEKQRCA 139
Cdd:PRK15134 90 RGNKIAMIFQEpmVSLNPLHTLEKQLyevlsLHrGMRREAAR---GEILNCLDrvgirqAAKRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 140 IARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
29-198 |
2.24e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.14 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFPHyKVKGNLLYG---ASRHY 105
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI----STLKPEIYRQQVSYCAQTPTLFGD-TVYDNLIFPwqiRNQQP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 DRNHFDQIVQLLDL-STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPIL 184
Cdd:PRK10247 113 DPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVL 192
|
170
....*....|....
gi 515592652 185 YVTHSLEEILHlAD 198
Cdd:PRK10247 193 WVTHDKDEINH-AD 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-212 |
2.39e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSgkiivgeraLYDSNKNIN-IAIDKRKI----GYVFQEARLFPHYKVKGNLLYGA- 101
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKGV---------KGSGSVLLNgMPIDAKEMraisAYVQQDDLFIPTLTVREHLMFQAh 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 102 ---SRHYD----RNHFDQIVQLLDLS----TLL---DRYPVdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:TIGR00955 126 lrmPRRVTkkekRERVDEVLQALGLRkcanTRIgvpGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-215 |
2.53e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.69 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSgkiIVGERALYDSNKNINIA------IDKRKIGYVFQE--ARL 87
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSATFNGREILNLPekelnkLRAEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 88 FPHYKVKGNLLYGASRHYDRNH---FDQIVQLLDLSTL------LDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKaeaFEESVRMLDAVKMpearkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 159 SLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-208 |
2.63e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 6 FKQQLEQFMLDINVdipQHG-ITAIFGRSGAGKTSIINAISGL----NNPDSGKIIVGERALYDSNKNINIAIDKRKIGY 80
Cdd:PRK09984 14 FNQHQALHAVDLNI---HHGeMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGRLARDIRKSRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 81 VFQEARLFPHYKVKGNLLYGA----------SRHYDRNHFDQIVQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSE 147
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIGAlgstpfwrtcFSWFTREQKQRALQALTrvgMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515592652 148 PEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-217 |
2.91e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.63 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsnkniniaiDKRKIGYVFQEARLFpHYKVKG 95
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----------------IRGTVAYVPQVSWIF-NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASrhYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:PLN03130 698 NILFGSP--FDPERYERAIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515592652 165 KQEVmpFLEKLSQEI-NIPILYVTHSLEEILHLaDHMLLIEDGQIKASGDIETM 217
Cdd:PLN03130 776 GRQV--FDKCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEEL 826
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-213 |
3.09e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKniniAIDKRKIGYVFQEARLFPHyKVKG 95
Cdd:PRK11160 358 GLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE----AALRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDrNHFDQIVQLLDLSTLLDRY-PVD---------LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:PRK11160 433 NLLLAAPNASD-EALIEVLQQVGLEKLLEDDkGLNawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515592652 166 QEVMPFLEKLSQeiNIPILYVTHSLEEILHLaDHMLLIEDGQIKASGD 213
Cdd:PRK11160 512 RQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-212 |
3.09e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.34 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQleQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGErALYDSNK--NINIAIDKRKIG 79
Cdd:PRK14247 9 LKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGE-VYLDGQDifKMDVIELRRRVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 80 YVFQEARLFPHYKVKGNLLYGASRHY----DRNHFDQIVQLLDLSTL-------LDRYPVDLSGGEKQRCAIARALLSEP 148
Cdd:PRK14247 86 MVFQIPNPIPNLSIFENVALGLKLNRlvksKKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515592652 149 EMLLMDEPLASLDLPRKQEVMPFLEKLSQEINipILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMT--IVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-201 |
3.16e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.68 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKII-VGERALYDSNKNINiaiDKRK-IGYVFQE--ARLFPHYKVkGNLLYGASRH 104
Cdd:PRK15079 52 VVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWR---AVRSdIQMIFQDplASLNPRMTI-GEIIAEPLRT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 105 Y----DRNHFDQIVQLLD-----LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:PRK15079 128 YhpklSRQEVKDRVKAMMlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
170 180
....*....|....*....|....*.
gi 515592652 176 SQEINIPILYVTHSLEEILHLADHML 201
Cdd:PRK15079 208 QREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-208 |
3.88e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.54 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 8 QQLEQFMLDINvdipQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkniNIAIDKRKIGYVFQEARL 87
Cdd:PRK11614 19 QALHEVSLHIN----QGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQ---TAKIMREAVAIVPEGRRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 88 FPHYKVKGNLLYGASrHYDRNHFDQ-IVQLLDLSTLLDRYPVD----LSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PRK11614 92 FSRMTVEENLAMGGF-FAERDQFQErIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 163 PRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK11614 171 IIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-224 |
4.97e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 22 PQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAidkRKIGYVFQ-----------EARLFPH 90
Cdd:PRK10575 35 PAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-ESWSSKAFA---RKVAYLPQqlpaaegmtvrELVAIGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 YKVKGNL-LYGASrhyDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVM 169
Cdd:PRK10575 111 YPWHGALgRFGAA---DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 170 PFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRSTAFQ 224
Cdd:PRK10575 188 ALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-210 |
5.05e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.99 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAIdKRKIGYVfQEAR----LFPHYKVKGNLLYGA 101
Cdd:COG1129 280 ILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV--RIRSPRDAI-RAGIAYV-PEDRkgegLVLDLSIRENITLAS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 102 SRHYDRNHF----------DQIVQLLDLSTLLDRYPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:COG1129 356 LDRLSRGGLldrrreralaEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYR 435
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515592652 171 FLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKA 210
Cdd:COG1129 436 LIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-216 |
5.94e-17 |
|
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: 82.04 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNnPDSGKIIVGERALYDSNKNINIAIdKRKIGYVFQE--ARLFPHY-- 91
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPL-RRRMQVVFQDpfGSLSPRMtv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 --------KVKGNLLYGASRHydrnhfDQIVQLLD---LS-TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:COG4172 382 gqiiaeglRVHGPGLSAAERR------ARVAEALEevgLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 160 LDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIET 216
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-209 |
7.72e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 7.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlydsnkniniaidkrKIGYVFQE-ARLFPHYKVK 94
Cdd:COG0488 333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---------------KIGYFDQHqEELDPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGASRHYDRnhfdQIVQLL--------DLSTlldryPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:COG0488 398 DELRDGAPGGTEQ----EVRGYLgrflfsgdDAFK-----PVgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 166 QEvmpfLEKLSQEINIPILYVTHS---LEEIlhlADHMLLIEDGQIK 209
Cdd:COG0488 469 EA----LEEALDDFPGTVLLVSHDryfLDRV---ATRILEFEDGGVR 508
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-206 |
8.78e-17 |
|
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: 78.14 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAIDKRKIGYVFQEARLFpHYKVKG 95
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASrhYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:cd03290 98 NITFGSP--FNKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 165 KQEVM-PFLEKLSQEINIPILYVTHSLEEILHlADHMLLIEDG 206
Cdd:cd03290 176 SDHLMqEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-216 |
9.56e-17 |
|
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: 81.27 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNnPDSGKIIVGeRALYDSnKNINIAIDK-------RKIGYVFQE--AR 86
Cdd:COG4172 28 GVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDPAAHPSG-SILFDG-QDLLGLSERelrrirgNRIAMIFQEpmTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 87 LFPHYKVkGNLLY-------GASRHYDRnhfDQIVQLLDL------STLLDRYPVDLSGGEKQRCAIARALLSEPEMLLM 153
Cdd:COG4172 105 LNPLHTI-GKQIAevlrlhrGLSGAAAR---ARALELLERvgipdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515592652 154 DEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIET 216
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-216 |
9.92e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGER--ALYDsnkniniaidkrkIGYVFQearlfPHYKV 93
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLE-------------LGAGFH-----PELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGN-----LLYGASRHYDRNHFDQIVQLLDLSTLLDRyPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:COG1134 106 RENiylngRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515592652 168 VMPFLEKLSQEINIpILYVTHSLEEILHLADHMLLIEDGQIKASGDIET 216
Cdd:COG1134 185 CLARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-203 |
1.07e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.27 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsnkniniaiDKRKIGYVFQEARL-------- 87
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---------------GGARVAYVPQRSEVpdslpltv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 88 --------FPHYkvkgnllyGASRHY---DRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEP 156
Cdd:NF040873 75 rdlvamgrWARR--------GLWRRLtrdDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 157 LASLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILhLADHMLLI 203
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-209 |
3.22e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsNKNIniaidkrKIGYVFQEARLFPHYKVKG 95
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGL-------RIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYD-RNHFDQIVQLLD--------LSTLLDRY----------------------------PV-DLSGGEKQR 137
Cdd:COG0488 81 TVLDGDAELRAlEAELEELEAKLAepdedlerLAELQEEFealggweaearaeeilsglgfpeedldrPVsELSGGWRRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 138 CAIARALLSEPEMLLMDEPLASLDLprkqEVMPFLEKLSQEINIPILYVTHS---LEEIlhlADHMLLIEDGQIK 209
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHDryfLDRV---ATRILELDRGKLT 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-207 |
5.17e-16 |
|
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: 74.02 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlydsnkniniaidkrKIGYvfqearlfphykvkg 95
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------------KIGY--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 nllygasrhydrnhFDQivqlldlstlldrypvdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQevmpFLEKL 175
Cdd:cd03221 68 --------------FEQ-----------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE----ALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 176 SQEINIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-230 |
5.43e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.63 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNP--DSGKIIVGeralydsnkniniaidkrKIGYVFQEARLFpHYKV 93
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRG------------------SVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLYGASrhYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PLN03232 696 RENILFGSD--FESERYWRAIDVTALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 163 PRKQEVMPFLEKLSQEINIPILyVTHSLeEILHLADHMLLIEDGQIKASGDIETMWRS-TAFQPWQKNS 230
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVL-VTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSgSLFKKLMENA 840
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-199 |
7.45e-16 |
|
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: 78.67 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 21 IPQHG-ITAIFGRSGAGKTSIINAISG-----LNNPDSG----KIIvgER----ALYD-----SNKNINIAIdkrKIGYV 81
Cdd:COG1245 95 VPKKGkVTGILGPNGIGKSTALKILSGelkpnLGDYDEEpswdEVL--KRfrgtELQDyfkklANGEIKVAH---KPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 82 FQEARLFphykvKGN---LLYGASrhyDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:COG1245 170 DLIPKVF-----KGTvreLLEKVD---ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 159 SLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLeEIL-HLADH 199
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEE-GKYVLVVEHDL-AILdYLADY 281
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-161 |
1.07e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.99 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 1 MIKLAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIvgeraLYDSNKNINIAIDKRKIGY 80
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL-----FERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 81 VFQEARLFPHYKVKGNLLYGASRHYDRNHFDQIVQLLDLSTLLDrYPVD-LSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
..
gi 515592652 160 LD 161
Cdd:PRK13540 158 LD 159
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-208 |
1.56e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQLEQFMLDIN---VDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKI-IVGERALYDSNKNIniaidKRKIG 79
Cdd:PRK13642 10 LVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkIDGELLTAENVWNL-----RRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 80 YVFQEA-RLFPHYKVKGNLLYGAS-----RHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLM 153
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515592652 154 DEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHlADHMLLIEDGQI 208
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-212 |
1.97e-15 |
|
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: 78.13 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnkNINIAIDKRKIGYVFQEARLFPHYKVKGN 96
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 97 LLYGAS---RHYDRNHFDQIVQLLD--LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:TIGR01257 1024 ILFYAQlkgRSWEEAQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515592652 172 LEKLSQeiNIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:TIGR01257 1104 LLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-161 |
2.59e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 21 IPQHG-ITAIFGRSGAGKTSIINAISG-----LNNPDSG----KIIvgER----ALYD-----SNKNINIAidkRKIGYV 81
Cdd:PRK13409 95 IPKEGkVTGILGPNGIGKTTAVKILSGelipnLGDYEEEpswdEVL--KRfrgtELQNyfkklYNGEIKVV---HKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 82 FQEARLFphykvKGN---LLYGASrhyDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:PRK13409 170 DLIPKVF-----KGKvreLLKKVD---ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
...
gi 515592652 159 SLD 161
Cdd:PRK13409 242 YLD 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-222 |
2.61e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLEQFMLDINVDIP-QHGIT-AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNInIAIDKRK-- 77
Cdd:PRK10261 18 LNIAFMQEQQKIAAVRNLSFSlQRGETlAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQV-IELSEQSaa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 78 ---------IGYVFQE--ARLFPHYKVKGNLLYGASRHYDRNHFDQIVQ---LLDL------STLLDRYPVDLSGGEKQR 137
Cdd:PRK10261 97 qmrhvrgadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEakrMLDQvripeaQTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 138 CAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
....*
gi 515592652 218 WRSTA 222
Cdd:PRK10261 257 FHAPQ 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
125-220 |
2.99e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.67 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 125 RYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIE 204
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLR 500
|
90
....*....|....*.
gi 515592652 205 DGQIKASGDIETMWRS 220
Cdd:PRK15134 501 QGEVVEQGDCERVFAA 516
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
28-198 |
3.33e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.39 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKI-IVGERALydSNKNINIAIDKRKIGYVFQE--ARLFPHYKVKGNL------- 97
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELyYQGQDLL--KADPEAQKLLRQKIQIVFQNpyGSLNPRKKVGQILeepllin 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 98 --LYGASRHydrnhfDQIVQLLDLSTL----LDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:PRK11308 123 tsLSAAERR------EKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL 196
|
170 180
....*....|....*....|....*..
gi 515592652 172 LEKLSQEINIPILYVTHSLEEILHLAD 198
Cdd:PRK11308 197 MMDLQQELGLSYVFISHDLSVVEHIAD 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-208 |
4.26e-15 |
|
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: 76.40 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDsnknINIAIDKRKIGYVFQEARLFP---HYk 92
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD----VTQASLRAAIGIVPQDTVLFNdtiAY- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 vkgNLLYG---ASRhydrnhfDQIVQLLDLSTLLD---RYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDE 155
Cdd:COG5265 451 ---NIAYGrpdASE-------EEVEAAARAAQIHDfieSLPdgydtrvgergLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 156 PLASLDLPRKQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQI 208
Cdd:COG5265 521 ATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-220 |
4.38e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.16 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGL-NNPdsGKIIvGERALYDSNKNINIAIDKRK------IGYVFQEA--RL 87
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVM-AEKLEFNGQDLQRISEKERRnlvgaeVAMIFQDPmtSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 88 FPHYKVKGNLLYGASRHYDRNHFDQIVQLLDLSTL---------LDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgipdpasrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515592652 159 SLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETMWRS 220
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
28-212 |
4.76e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNkninIAIDKRKIGYVFQEA--RLFPHYKVKGNL-------- 97
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD----YSYRSQRIRMIFQDPstSLNPRQRISQILdfplrlnt 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 98 -LYGASRHydrnhfDQIVQLLDLSTLL----DRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFL 172
Cdd:PRK15112 119 dLEPEQRE------KQIIETLRQVGLLpdhaSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515592652 173 EKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK15112 193 LELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
29-207 |
5.32e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.00 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIV--GERALYdsnkniniaidkrkigyVFQEARLfPHYKVKGNLLY-GASRHY 105
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLF-----------------LPQRPYL-PLGTLREALLYpATAEAF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 DRnhfDQIVQLLD---LSTLLDRYPVD------LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMpflEKLS 176
Cdd:COG4178 456 SD---AELREALEavgLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY---QLLR 529
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 177 QEI-NIPILYVTHSlEEILHLADHMLLIEDGQ 207
Cdd:COG4178 530 EELpGTTVISVGHR-STLAAFHDRVLELTGDG 560
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-215 |
1.46e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.41 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGlnNPD----SGKIivgeraLYDsNKNI-NIAIDKRK---IGYVFQ---E 84
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSI------LLD-GEDIlELSPDERAragIFLAFQypvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 85 arlFPHYKVKgNLL---YGASRH--YDRNHFDQIVQ----LLDLST-LLDRY-PVDLSGGEKQRCAIARALLSEPEMLLM 153
Cdd:COG0396 89 ---IPGVSVS-NFLrtaLNARRGeeLSAREFLKLLKekmkELGLDEdFLDRYvNEGFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 154 DEPLASLDLprkqevmPFLEKLSQEIN------IPILYVTHSlEEILHL--ADHMLLIEDGQIKASGDIE 215
Cdd:COG0396 165 DETDSGLDI-------DALRIVAEGVNklrspdRGILIITHY-QRILDYikPDFVHVLVDGRIVKSGGKE 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-212 |
1.87e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.61 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralyDSN--KNINIAIDKRKIGYVFQEARLFpHYKVKGNLLYGASRHY 105
Cdd:PRK13657 365 AIVGPTGAGKSTLINLLQRVFDPQSGRILI------DGTdiRTVTRASLRRNIAVVFQDAGLF-NRSIEDNIRVGRPDAT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 DRNHFD--QIVQLLD-LSTLLDRYPVD-------LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:PRK13657 438 DEEMRAaaERAQAHDfIERKPDGYDTVvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
170 180 190
....*....|....*....|....*....|....*..
gi 515592652 176 SQeiNIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:PRK13657 518 MK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-212 |
2.20e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFPHyKVKGNLLYGASRHY 105
Cdd:TIGR00958 509 VVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL----VQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTP 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 106 DR---------NHFDQIVQLL-DLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:TIGR00958 584 DEeimaaakaaNAHDFIMEFPnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA 663
|
170 180 190
....*....|....*....|....*....|....*..
gi 515592652 176 SQeiniPILYVTHSLeEILHLADHMLLIEDGQIKASG 212
Cdd:TIGR00958 664 SR----TVLLIAHRL-STVERADQILVLKKGSVVEMG 695
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-207 |
3.65e-14 |
|
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: 71.29 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 7 KQQLEQFMLDINV-DIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIvgeralydsnkniniaIDKRKIGYVFQEa 85
Cdd:cd03237 7 KKTLGEFTLEVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE----------------IELDTVSYKPQY- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 86 rLFPHYKVK-GNLLYGASR-HYDRNHFD-QIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:cd03237 70 -IKADYEGTvRDLLSSITKdFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515592652 163 PRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHmLLIEDGQ 207
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADR-LIVFEGE 192
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
9-223 |
4.76e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.66 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 9 QLEQFML--DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsnkniniaidKRKIGYVFQEAR 86
Cdd:PTZ00243 669 ELEPKVLlrDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------------ERSIAYVPQQAW 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 87 LFpHYKVKGNLLY----GASRHYDRNHFDQI---VQLLD--LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPL 157
Cdd:PTZ00243 732 IM-NATVRGNILFfdeeDAARLADAVRVSQLeadLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 158 ASLDLPRKQEVMP--FLEKLSQEINIpilYVTHSLeEILHLADHMLLIEDGQIKASGDIETMWRSTAF 223
Cdd:PTZ00243 811 SALDAHVGERVVEecFLGALAGKTRV---LATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSLY 874
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-215 |
5.21e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQleQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIivgERAlydsnkniniaiDKRKIGYV 81
Cdd:PRK09544 10 VSVSFGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KRN------------GKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 82 FQE--------------ARLFPHYKvKGNLLYGASRHydrnhfdQIVQLLDlstlldrYPVD-LSGGEKQRCAIARALLS 146
Cdd:PRK09544 73 PQKlyldttlpltvnrfLRLRPGTK-KEDILPALKRV-------QAGHLID-------APMQkLSGGETQRVLLARALLN 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 147 EPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIeDGQIKASGDIE 215
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPE 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-216 |
5.41e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlydsnknINIAIDKRKIGYVFQEARL---FPhYK 92
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-------TRQALQKNLVAYVPQSEEVdwsFP-VL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLLYGASRH---------YDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLP 163
Cdd:PRK15056 97 VEDVVMMGRYGHmgwlrrakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 164 RKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEdGQIKASGDIET 216
Cdd:PRK15056 177 TEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTET 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-207 |
5.95e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNK----NINIAIdkrkigyVFQEARLFPHY 91
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtaalAAGVAI-------IYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLYGasrhydrnHFDQIVQLLDLSTL-------LDRYPVD---------LSGGEKQRCAIARALLSEPEMLLMDE 155
Cdd:PRK11288 95 TVAENLYLG--------QLPHKGGIVNRRLLnyeareqLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 156 PLASLDLPRKQEVMPFLEKLSQEINIpILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-209 |
9.84e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 69.36 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 2 IKLAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsnKNINIA-ID----KR 76
Cdd:cd03369 12 LSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI---------DGIDIStIPledlRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 77 KIGYVFQEARLFPHyKVKGNLlygasRHYDRNHFDQIVQLLDLSTLLDrypvDLSGGEKQRCAIARALLSEPEMLLMDEP 156
Cdd:cd03369 83 SLTIIPQDPTLFSG-TIRSNL-----DPFDEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 157 LASLDLPRKQEVMPFLEKLSQeiNIPILYVTHSLEEILHLaDHMLLIEDGQIK 209
Cdd:cd03369 153 TASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-212 |
1.72e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 69.06 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsnkNINIA-ID----KRKIGYVFQEARLFPH 90
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID---------GVDISkIGlhdlRSRISIIPQDPVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 yKVKGNL----------LYGAsrhYDRNHFDQIVQLLD--LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:cd03244 93 -TIRSNLdpfgeysdeeLWQA---LERVGLKEFVESLPggLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 159 SLDlprkqevmPFLEKLSQEI------NIPILYVTHSLEEILHlADHMLLIEDGQIKASG 212
Cdd:cd03244 169 SVD--------PETDALIQKTireafkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-161 |
3.43e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 5 AFKQQLEQFMLDINV-DIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIivgeralydsNKNIniaidkrKIGYVFQ 83
Cdd:PRK13409 345 DLTKKLGDFSLEVEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV----------DPEL-------KISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 eaRLFPHYKVK-GNLLYGASRHYDRNHFD-QIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PRK13409 408 --YIKPDYDGTvEDLLRSITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-198 |
4.10e-13 |
|
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: 68.55 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 21 IPQHG-ITAIFGRSGAGKTSIINAISGLNNPDSGKiivgeralYDSNKNINIAIDKRKiGYVFQE--ARLF--------- 88
Cdd:cd03236 22 VPREGqVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDWDEILDEFR-GSELQNyfTKLLegdvkvivk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 PHY------KVKGNLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:cd03236 93 PQYvdlipkAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 163 PRKQEVMPFLEKLSQEINiPILYVTHSLEEILHLAD 198
Cdd:cd03236 173 KQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSD 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-213 |
4.59e-13 |
|
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: 70.16 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKniniaiDK--RKIGYVFQEARLFPHyKV 93
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR------EElgRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLlygaSRHYDRNhFDQIV---QLLDL----STLLDRY--PVD-----LSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:COG4618 423 AENI----ARFGDAD-PEKVVaaaKLAGVhemiLRLPDGYdtRIGeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515592652 160 LDLPRKQEVMPFLEKLSQEiNIPILYVTHSLeEILHLADHMLLIEDGQIKASGD 213
Cdd:COG4618 498 LDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-207 |
5.41e-13 |
|
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: 68.34 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalydsnkniniaidkrkIGYVFQEARLFPHyKVKG 95
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASrhYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:cd03291 117 NIIFGVS--YDEYRYKSVVKACQLEEDITKFPekdntvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515592652 165 KQEVM-PFLEKLSQeiNIPILYVTHSLEEiLHLADHMLLIEDGQ 207
Cdd:cd03291 195 EKEIFeSCVCKLMA--NKTRILVTSKMEH-LKKADKILILHEGS 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-217 |
8.97e-13 |
|
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: 69.08 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGL--NNPDSGKIIVGERALYDSNkninIAIDKRK-IGYVFQEARLFPHYKVKGNL----- 97
Cdd:TIGR02633 29 CVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASN----IRDTERAgIVIIHQELTLVPELSVAENIflgne 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 98 --LYGASRHYD----RNHfdQIVQLLDLSTLLDRYPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:TIGR02633 105 itLPGGRMAYNamylRAK--NLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 171 FLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:TIGR02633 183 IIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-205 |
1.05e-12 |
|
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: 65.25 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlydsnkniniaidkrKIGYVFQEArlfphYKVKG 95
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------DLLFLPQRP-----YLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLygasrhydrnhfDQIVqlldlstlldrYPVD--LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLE 173
Cdd:cd03223 79 TLR------------EQLI-----------YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 174 KLSqeinIPILYVTHSlEEILHLADHMLLIED 205
Cdd:cd03223 136 ELG----ITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-193 |
4.63e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGeralyDSN--KNINIAIDKRKIGYVFQEARLFPHyKV 93
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-----DSHnlKDINLKWWRSKIGVVSQDPLLFSN-SI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 94 KGNLLY------------------GASRHYDRNH-----------FDQIVQLLD-------------------------- 118
Cdd:PTZ00265 477 KNNIKYslyslkdlealsnyynedGNDSQENKNKrnscrakcagdLNDMSNTTDsneliemrknyqtikdsevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 119 -----LSTLLDRYPV-------DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYV 186
Cdd:PTZ00265 557 lihdfVSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
....*..
gi 515592652 187 THSLEEI 193
Cdd:PTZ00265 637 AHRLSTI 643
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-161 |
7.12e-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: 66.73 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 5 AFKQQLEQFMLDINVDIPQHG-ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKnINIAIDKRkigyVfq 83
Cdd:COG1245 346 DLTKSYGGFSLEVEGGEIREGeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQY-ISPDYDGT----V-- 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 84 EARLFPHYKVKgnllYGASRHYDrnhfdQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:COG1245 419 EEFLRSANTDD----FGSSYYKT-----EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-177 |
1.08e-11 |
|
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: 63.28 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNIniaidKRKIGYVFQEARLFPHYKVKGNLLYGASRHYDrn 108
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGLLYLGHAPGIKTTLSVLENLRFWHADHSD-- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515592652 109 hfDQIVQLLD---LSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlprKQEVMPFLEKLSQ 177
Cdd:cd03231 104 --EQVEEALArvgLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD---KAGVARFAEAMAG 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-215 |
1.15e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIV-GERALYDSNKNiniAIDKrKIGYVFQEARLFPHYKVK 94
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFKSSKE---ALEN-GISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GNLLYGasRHYDRNHF-DQIVQLLDLSTLLDRYPVD---------LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:PRK10982 92 DNMWLG--RYPTKGMFvDQDKMYRDTKAIFDELDIDidprakvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515592652 165 KQEVMPFLEKLsQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIE 215
Cdd:PRK10982 170 VNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLA 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-215 |
1.31e-11 |
|
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: 62.93 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGlnNPDSgkIIVGERALYDSNKNINIAIDKRK---IGYVFQEARLFPHYK 92
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKY--EVTEGEILFKGEDITDLPPEERArlgIFLAFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKgNLLygasrhydrnhfdqivqlldlstlldRY-PVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:cd03217 94 NA-DFL--------------------------RYvNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 172 LEKLSQEiNIPILYVTHsLEEILHL--ADHMLLIEDGQIKASGDIE 215
Cdd:cd03217 147 INKLREE-GKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-208 |
1.46e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.51 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnKNINIAIDKRKIGYVFQEARLFPHyKVKG 95
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL----SSLSHSVLRQGVAMVQQDPVVLAD-TFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGasRHYDRNHFDQI---VQLLDLS--------TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:PRK10790 434 NVTLG--RDISEEQVWQAletVQLAELArslpdglyTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515592652 165 KQEVMPFLEKLSQeiNIPILYVTHSLEEILHlADHMLLIEDGQI 208
Cdd:PRK10790 512 EQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-210 |
2.31e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIaidKRKIGYVFQEAR---LFPHYK 92
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV---KKGMAYITESRRdngFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNL----------LYGA----SRHYDRNHFDQIVQLLDLS-TLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPL 157
Cdd:PRK09700 358 IAQNMaisrslkdggYKGAmglfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 158 ASLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKA 210
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-205 |
2.61e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 15 LDINVDIPQHGITAIFGRSGAGKTSIINAISG--LNNPDSGKIIVGERALYdSNKNINIAIDKRKigyvfqearlfphyk 92
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG-REASLIDAIGRKG--------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 vkgnllygasrhydrnHFDQIVQLLDLSTLLD-----RYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:COG2401 111 ----------------DFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIED 205
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-207 |
5.07e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGL--NNPDSGKIIVGERALydsNKNIniaidKRKIGYVFQEARLFPHYKVKGNLLYGA-- 101
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKP---TKQI-----LKRTGFVTQDDILYPHLTVRETLVFCSll 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 102 ------SRHYDRNHFDQIVQLLDLS----TLL-DRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMP 170
Cdd:PLN03211 168 rlpkslTKQEKILVAESVISELGLTkcenTIIgNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 515592652 171 FLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-188 |
5.09e-11 |
|
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: 63.80 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlydsnkniniaidkrKIGYVFQEARLFPHYKVKGNLLYGASRHYDR- 107
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---------------KVGYLPQEPQLDPTKTVRENVEEGVAEIKDAl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 108 NHFDQIVQLL---------------------------DLSTLLD------RYP------VDLSGGEKQRCAIARALLSEP 148
Cdd:TIGR03719 101 DRFNEISAKYaepdadfdklaaeqaelqeiidaadawDLDSQLEiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515592652 149 EMLLMDEPLASLDlprkQEVMPFLEKLSQEINIPILYVTH 188
Cdd:TIGR03719 181 DMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTH 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-206 |
5.63e-11 |
|
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: 64.16 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERalydsnkniniaidkrkIGYVFQEARLFPHyKVKG 95
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASrhYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPR 164
Cdd:TIGR01271 506 NIIFGLS--YDEYRYTSVIKACQLEEDIALFPekdktvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515592652 165 KQEVMP-FLEKLSqeINIPILYVTHSLEEiLHLADHMLLIEDG 206
Cdd:TIGR01271 584 EKEIFEsCLCKLM--SNKTRILVTSKLEH-LKKADKILLLHEG 623
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-207 |
7.24e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.51 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNpDSGKIiVGERALYDSNKNINIAIDKRK------IGYVFQEAR--LF 88
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRV-TADRMRFDDIDLLRLSPRERRklvghnVSMIFQEPQscLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 89 PHYKVKGNLLYG------ASRHYDRNHFDQ--IVQLL------DLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMD 154
Cdd:PRK15093 104 PSERVGRQLMQNipgwtyKGRWWQRFGWRKrrAIELLhrvgikDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515592652 155 EPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
130-211 |
7.97e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 130 LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIK 209
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
..
gi 515592652 210 AS 211
Cdd:TIGR02633 483 GD 484
|
|
| TOBE |
pfam03459 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
294-356 |
7.99e-11 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulfate. Found in ABC transporters immediately after the ATPase domain.
Pssm-ID: 427310 [Multi-domain] Cd Length: 60 Bit Score: 56.90 E-value: 7.99e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515592652 294 MRNIIPATIVElakVTDPTQPVSLRLSLGSGLSLWANITAWAYDDLQLKTGQKVFAQIKGVRL 356
Cdd:pfam03459 1 ARNQLPGTVTV---IEPLGSEVEVRVDLGGGLTLTARITRDSAEELGLAPGDEVWALIKATKV 60
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-223 |
1.22e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 17 INVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsnkniniaidKRKIGYVFQEARLfPHYKVKGN 96
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------------KGSVAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 97 LLYGasRHYDRNHFDQIVQLLDLSTLLDRYP-----------VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRK 165
Cdd:TIGR00957 719 ILFG--KALNEKYYQQVLEACALLPDLEILPsgdrteigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515592652 166 QEVmpFLEKLSQE---INIPILYVTHSLeEILHLADHMLLIEDGQIKASGDI-ETMWRSTAF 223
Cdd:TIGR00957 797 KHI--FEHVIGPEgvlKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYqELLQRDGAF 855
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-161 |
1.30e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGE----------RALYDSNKNINIAI----DKRKIGyv 81
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtvklayvdqsRDALDPNKTVWEEIsgglDIIKLG-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 82 fqearlfpHYKVKgnllygaSRHY-DRNHF---DQivqlldlstllDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPL 157
Cdd:TIGR03719 418 --------KREIP-------SRAYvGRFNFkgsDQ-----------QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
....
gi 515592652 158 ASLD 161
Cdd:TIGR03719 472 NDLD 475
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-208 |
1.59e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALyDSNKNINIAIDKRKIGYVFQE--ARLFPHYKVKGNLLYGASRH- 104
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-DTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHg 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 105 --YDRNHFDQIVQLLDLSTLLD----RYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQE 178
Cdd:PRK10261 433 llPGKAAAARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRD 512
|
170 180 190
....*....|....*....|....*....|...
gi 515592652 179 INIPILYVTHSL---EEILHLADHMLLiedGQI 208
Cdd:PRK10261 513 FGIAYLFISHDMavvERISHRVAVMYL---GQI 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-208 |
2.44e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 11 EQFMlDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAIDKrkiGYVF-----QEA 85
Cdd:PRK15439 277 EGFR-NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI--NALSTAQRLAR---GLVYlpedrQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 86 RLFPHYKVKGN---LLYG-----ASRHYDRNHFDQIVQLLDLSTLLDRYPV-DLSGGEKQRCAIARALLSEPEMLLMDEP 156
Cdd:PRK15439 351 GLYLDAPLAWNvcaLTHNrrgfwIKPARENAVLERYRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515592652 157 LASLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-212 |
3.23e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNnPDSGKIIVGERAL--YDSNKninIAidkRKIGYVFQEAR---LFP--HYKVkgnlL 98
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeaWSAAE---LA---RHRAYLSQQQTppfAMPvfQYLT----L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 99 Y---GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALL-------SEPEMLLMDEPLASLDLPRKQEV 168
Cdd:PRK03695 93 HqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515592652 169 MPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK03695 173 DRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-206 |
4.04e-10 |
|
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: 58.41 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 27 TAIFGRSGAGKTSIINAISGlnNPDSGkIIVGERALYDSNKNINIAidkRKIGYVFQEARLFPHYKVKGNLLYGAsrhYD 106
Cdd:cd03232 36 TALMGESGAGKTTLLDVLAG--RKTAG-VITGEILINGRPLDKNFQ---RSTGYVEQQDVHSPNLTVREALRFSA---LL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 107 RnhfdqivqlldlstlldrypvDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNIPILYV 186
Cdd:cd03232 107 R---------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCT 164
|
170 180
....*....|....*....|.
gi 515592652 187 THS-LEEILHLADHMLLIEDG 206
Cdd:cd03232 165 IHQpSASIFEKFDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
130-210 |
4.76e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 130 LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIK 209
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
.
gi 515592652 210 A 210
Cdd:PRK13549 485 G 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-207 |
1.14e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKII-VGERALYDSNKNINIAidkrKIGYVFQEARLFPHYKVKGNLLYGasRHYd 106
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEA----GIGIIHQELNLIPQLTIAENIFLG--REF- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 107 RNHF------------DQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEK 174
Cdd:PRK10762 107 VNRFgridwkkmyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRE 186
|
170 180 190
....*....|....*....|....*....|...
gi 515592652 175 LSQEiNIPILYVTHSLEEILHLADHMLLIEDGQ 207
Cdd:PRK10762 187 LKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-208 |
1.78e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGlNNPD--SGKIIV-GERAlyDSNKNI-NIaidKRKIGYVfqEARLFPHYKVKGNL------- 97
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITG-DHPQgySNDLTLfGRRR--GSGETIwDI---KKHIGYV--SSSLHLDYRVSTSVrnvilsg 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 98 ------LYGASRhyDRNHF--DQIVQLLDLSTLLDRYPV-DLSGGEkQRCA-IARALLSEPEMLLMDEPLASLDLPRKQE 167
Cdd:PRK10938 363 ffdsigIYQAVS--DRQQKlaQQWLDILGIDKRTADAPFhSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQL 439
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 168 VMPFLEKLSQEINIPILYVTHSLEEILHLADHML-LIEDGQI 208
Cdd:PRK10938 440 VRRFVDVLISEGETQLLFVSHHAEDAPACITHRLeFVPDGDI 481
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
24-204 |
2.49e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.46 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 24 HGITAIFGRSGAGKTSIINAIS----GLNNPDSgkiivgeralYDSNKNINIAIDKRKIGYVfqeaRLfpHYKVKGNLLY 99
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALKyaltGELPPNS----------KGGAHDPKLIREGEVRAQV----KL--AFENANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 100 GASRHYdrNHFDQIVQLL--DLSTLLDRYPVDLSGGEKQ------RCAIARALLSEPEMLLMDEPLASLDLPRKQEVM-P 170
Cdd:cd03240 86 TITRSL--AILENVIFCHqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaE 163
|
170 180 190
....*....|....*....|....*....|....
gi 515592652 171 FLEKLSQEINIPILYVTHSlEEILHLADHMLLIE 204
Cdd:cd03240 164 IIEERKSQKNFQLIVITHD-EELVDAADHIYRVE 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-176 |
3.53e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNP---DSGKIIVGERALYDSNkniniaidKRKIGYVFQEARLFPHYKVKGNLLYGA- 101
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSF--------QRSIGYVQQQDLHLPTSTVRESLRFSAy 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 102 ---SRH---YDRNHF-DQIVQLLDLSTLLDRYpVDLSGG-----EKQRCAIARALLSEPEMLL-MDEPLASLDLPRKQEV 168
Cdd:TIGR00956 863 lrqPKSvskSEKMEYvEEVIKLLEMESYADAV-VGVPGEglnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
|
....*...
gi 515592652 169 MPFLEKLS 176
Cdd:TIGR00956 942 CKLMRKLA 949
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
130-215 |
3.56e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 130 LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIK 209
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
....*.
gi 515592652 210 ASGDIE 215
Cdd:PRK10762 475 GEFTRE 480
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
25-188 |
5.36e-09 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 55.74 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 25 GITAIFGRSGAGKTSIINAIS-GLnnpdSGKIIvGERALYDSNKNINIAIDKRKIGYVFQearlfphykvKGNLLYGA-- 101
Cdd:cd03279 29 GLFLICGPTGAGKSTILDAITyAL----YGKTP-RYGRQENLRSVFAPGEDTAEVSFTFQ----------LGGKKYRVer 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 102 SRHYDRNHFDQIVQLL--DLSTLLDRYPVDLSGGEKQRCAIARAL-LSEP---------EMLLMDEPLASLDLPRKQEVM 169
Cdd:cd03279 94 SRGLDYDQFTRIVLLPqgEFDRFLARPVSTLSGGETFLASLSLALaLSEVlqnrggarlEALFIDEGFGTLDPEALEAVA 173
|
170
....*....|....*....
gi 515592652 170 PFLEKLSQEiNIPILYVTH 188
Cdd:cd03279 174 TALELIRTE-NRMVGVISH 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-216 |
6.93e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINIAIdKRKIGYVFQEAR---LFPHYK 92
Cdd:PRK10982 266 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI--NNHNANEAI-NHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 93 VKGNLLYGASRHYdRNHF---DQIVQLLDLSTLLDRYPV----------DLSGGEKQRCAIARALLSEPEMLLMDEPLAS 159
Cdd:PRK10982 343 IGFNSLISNIRNY-KNKVgllDNSRMKSDTQWVIDSMRVktpghrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 160 LDLPRKQEVMPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGqiKASGDIET 216
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG--LVAGIVDT 475
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-161 |
1.35e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGE----------RALYDSNKNI---------NIAIDKR 76
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvklayvdqsRDALDPNKTVweeisggldIIKVGNR 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 77 KIgyvfqearlfphykvkgnllygASRHY-DRNHF---DQivqlldlstlldRYPV-DLSGGEKQRCAIARALLSEPEML 151
Cdd:PRK11819 422 EI----------------------PSRAYvGRFNFkggDQ------------QKKVgVLSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|
gi 515592652 152 LMDEPLASLD 161
Cdd:PRK11819 468 LLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
128-204 |
1.36e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.73 E-value: 1.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 128 VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEILHLADHMLLIE 204
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
126-193 |
2.68e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 2.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 126 YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILYVTHSLEEI 193
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-217 |
3.02e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNnPD---SGKIIVGERALydsnKNINIAIDKRK-IGYVFQEARLFPHYKVKGNLLYGA 101
Cdd:PRK13549 33 IVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEEL----QASNIRDTERAgIAIIHQELALVKELSVLENIFLGN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 102 S-RHYDRNHFDQIVqlLDLSTLLDRY--------PV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPF 171
Cdd:PRK13549 108 EiTPGGIMDYDAMY--LRAQKLLAQLkldinpatPVgNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 172 LEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:PRK13549 186 IRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-161 |
3.19e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.34 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNINIAidkrkigYVFQEARLFPHYKVKG 95
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH-------YLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515592652 96 NL-----LYGASRHydrnHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PRK13539 93 NLefwaaFLGGEEL----DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-188 |
3.37e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlydsnkniniaidkrKIGYVFQEARLFPHYKVKGNLLYGASRHYD-R 107
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI---------------KVGYLPQEPQLDPEKTVRENVEEGVAEVKAaL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 108 NHFDQIVQLL---------------------------DLSTLLDR-----------YPVD-LSGGEKQRCAIARALLSEP 148
Cdd:PRK11819 103 DRFNEIYAAYaepdadfdalaaeqgelqeiidaadawDLDSQLEIamdalrcppwdAKVTkLSGGERRRVALCRLLLEKP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515592652 149 EMLLMDEPLASLDlprkQEVMPFLEKLSQEINIPILYVTH 188
Cdd:PRK11819 183 DMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTH 218
|
|
| Mop |
TIGR00638 |
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin ... |
292-352 |
3.48e-08 |
|
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin binding proteins of about 70 amino acids in Clostridium pasteurianum, as a tandemly-repeated domain C-terminal to an unrelated domain in ModE, a molybdate transport gene repressor of E. coli, and in single or tandemly paired domains in several related proteins. [Transport and binding proteins, Anions]
Pssm-ID: 273189 [Multi-domain] Cd Length: 69 Bit Score: 50.05 E-value: 3.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515592652 292 TSMRNIIPATIVELAKvtDPTQpVSLRLSLGSGLSLWANITAWAYDDLQLKTGQKVFAQIK 352
Cdd:TIGR00638 3 TSARNQLKGKVVAIED--GDVN-AEVDLLLGGGTKLTAVITLESVAELGLKPGKEVYAVIK 60
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-259 |
4.00e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 102 SRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNI 181
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GA 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 182 PILYVTHSLEEILHLADHMLLIEDGQIKASGDIEtmwrstafqpwqknsELSTLFKGMLTEHHPKYAlsyVELARNIG 259
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD---------------ELKTKVGGRTLQIRPAHA---AELDRMVG 255
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-161 |
4.36e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 14 MLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIivgeralYDSNKNINiAIDKRKIGYVFQEARLFPHYKV 93
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI-------YYKNCNIN-NIAKPYCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 94 KGNLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PRK13541 88 FENLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
104-212 |
4.43e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 104 HYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEiNIPI 183
Cdd:PRK10938 110 VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITL 188
|
90 100
....*....|....*....|....*....
gi 515592652 184 LYVTHSLEEILHLADHMLLIEDGQIKASG 212
Cdd:PRK10938 189 VLVLNRFDEIPDFVQFAGVLADCTLAETG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-208 |
5.17e-08 |
|
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: 52.65 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 31 GRSGAGKTSIINAISglNNPDSGKIIVGErALYDSNKN-INIAIDKRKIGYVFQEARLFPHYKVKgnllygasrhydrnh 109
Cdd:cd03233 40 GRPGSGCSTLLKALA--NRTEGNVSVEGD-IHYNGIPYkEFAEKYPGEIIYVSEEDVHFPTLTVR--------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 110 fdqivQLLDLSTLL--DRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPILY-V 186
Cdd:cd03233 102 -----ETLDFALRCkgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsL 176
|
170 180
....*....|....*....|..
gi 515592652 187 THSLEEILHLADHMLLIEDGQI 208
Cdd:cd03233 177 YQASDEIYDLFDKVLVLYEGRQ 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-208 |
6.07e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydsnkNINIAIDKRKIGYVF-QEAR----LFPHYKVKGNLLYG 100
Cdd:PRK11288 281 IVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-----DIRSPRDAIRAGIMLcPEDRkaegIIPVHSVADNINIS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 101 ASRHYDRNHF-----------DQIVQLLDLSTLLDRYP-VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEV 168
Cdd:PRK11288 356 ARRHHLRAGClinnrweaenaDRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEI 435
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515592652 169 MPFLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK11288 436 YNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-214 |
8.53e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISglnnpdsgkiivgeralydsnkniniaidkrkigyvfqearlfphYKVKG 95
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---------------------------------------------YASGK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 NLLYGASRHYDRNHFDQIVQLLDLSTL------LDRYPVDLSGGEKQRCAIARALLSEPE--MLLMDEPLASLDLPRKQE 167
Cdd:cd03238 48 ARLISFLPKFSRNKLIFIDQLQFLIDVglgyltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 168 VMPFLEKLSQEINiPILYVTHSlEEILHLADHMLLIEDGQIKASGDI 214
Cdd:cd03238 128 LLEVIKGLIDLGN-TVILIEHN-LDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| MopI |
COG3585 |
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism]; |
266-352 |
1.23e-07 |
|
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];
Pssm-ID: 442804 [Multi-domain] Cd Length: 141 Bit Score: 50.46 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 266 QVKKGESLRVRIHASDVSITLSQAKDTSMRNIIPATIVELakVTDPTQpVSLRLSLGSGLSLWANITAWAYDDLQLKTGQ 345
Cdd:COG3585 48 GLVGGKEVAALKKASVVILATDDAMKLSARNQLKGTVTRI--ERGAVN-SEVVLDLGGGTTLTAVITNESVEELGLKEGD 124
|
....*..
gi 515592652 346 KVFAQIK 352
Cdd:COG3585 125 EVTALFK 131
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
128-217 |
1.87e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 128 VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKLSQEINIPIlyVTHSLEEiLHLADHMLLIEDGQ 207
Cdd:PRK10789 450 VMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVII--SAHRLSA-LTEASEILVMQHGH 526
|
90
....*....|
gi 515592652 208 IKASGDIETM 217
Cdd:PRK10789 527 IAQRGNHDQL 536
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-217 |
1.88e-07 |
|
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: 53.09 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALYdsnknINIAIDKRKIGYVfqearlfPHYKVKGNLLYGASRHYDR 107
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-----TNISDVHQNMGYC-------PQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 108 NHFDQI------------VQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:TIGR01257 2037 ARLRGVpaeeiekvanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 176 SQEINIPILyVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:TIGR01257 2117 IREGRAVVL-TSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-162 |
2.78e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 31 GRSGAGKTSIINAISGLNNPDSGKIIVgeralyDSNKNINiAIDKRKIGYVFQEARLFPHYKVKGNLLYGASRHYDR--- 107
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQI------DGKTATR-GDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRakq 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 108 --NHFDQIVQLLDLSTLLDRYpvdLSGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PRK13543 117 mpGSALAIVGLAGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-161 |
5.25e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGLNnpdSGKIIVGERALYDSNKNINIAidKRKIGYVFQEARLFPHYKVKGNLLYGA---- 101
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRK---TGGYIEGDIRISGFPKKQETF--ARISGYCEQNDIHSPQVTVRESLIYSAflrl 982
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 102 ----SRHYDRNHFDQIVQLLDLSTLLDR---YP--VDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:PLN03140 983 pkevSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-214 |
1.20e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKI-IVGERALydsnkninIAIDKRKIGyvfqEARLFPHYKVK 94
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKGSAAL--------IAISSGLNG----QLTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 95 GnLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVmpfLEK 174
Cdd:PRK13545 110 G-LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC---LDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 175 LSQ--EINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDI 214
Cdd:PRK13545 186 MNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDI 227
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
24-176 |
1.24e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 24 HGITAIFGRSGAGKTSIINAI---------------SGLNNPDS------------GKIIVGERALYDSNKNINIAIDKR 76
Cdd:COG0419 23 DGLNLIVGPNGAGKSTILEAIryalygkarsrsklrSDLINVGSeeasvelefehgGKRYRIERRQGEFAEFLEAKPSER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 77 K--IGYVFQEARLFPHYKVKGNLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVD-LSGGEKQRCAIARALlsepeMLLM 153
Cdd:COG0419 103 KeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIEtLSGGERLRLALADLL-----SLIL 177
|
170 180
....*....|....*....|...
gi 515592652 154 DepLASLDLPRKQEVMPFLEKLS 176
Cdd:COG0419 178 D--FGSLDEERLERLLDALEELA 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-217 |
1.25e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGERALydSNKNINiAIDKRKIGYVfQEAR----LFPHY 91
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI--TGLSPR-ERRRLGVAYI-PEDRlgrgLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 92 KVKGNLLygASRHYD--------------RNHFDQIVQLLDLSTLLDRYPVD-LSGGEKQRCAIARALLSEPEMLLMDEP 156
Cdd:COG3845 352 SVAENLI--LGRYRRppfsrggfldrkaiRAFAEELIEEFDVRTPGPDTPARsLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515592652 157 LASLDLP-----RKQevmpfLEKLSQEiNIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:COG3845 430 TRGLDVGaiefiHQR-----LLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-208 |
1.45e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGEralYDSNKnINIAIDKRKIGYVFQEARLFPHyKVKGNLlYGASRHYDRN 108
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAK-FGLTDLRRVLSIIPQSPVLFSG-TVRFNI-DPFSEHNDAD 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 109 HFDQIvQLLDLSTLLDRYPVDL-----------SGGEKQRCAIARALLSEPEMLLMDEPLASLDLprkqEVMPFLEKLSQ 177
Cdd:PLN03232 1341 LWEAL-ERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDV----RTDSLIQRTIR 1415
|
170 180 190
....*....|....*....|....*....|...
gi 515592652 178 E--INIPILYVTHSLEEILHlADHMLLIEDGQI 208
Cdd:PLN03232 1416 EefKSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-212 |
3.06e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 4 LAFKQQLEQFMLDINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsnKNINIAidkrKIGyvFQ 83
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII---------DGLNIA----KIG--LH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 84 EARLFPHYKVKGNLLYGASRHYDRNHFDQI--------VQLLDLSTLLDRYPV-----------DLSGGEKQRCAIARAL 144
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNLDPFSQYsdeevwwaLELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 145 LSEPEMLLMDEPLASLDLPRKQEVMPFLEklSQEINIPILYVTHSLEEILHLAdHMLLIEDGQIKASG 212
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-188 |
3.91e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGEralydsnkniniaidKRKIGYVFQ-EARLFPHYKVKGNL--------L 98
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT---------------KLEVAYFDQhRAELDPEKTVMDNLaegkqevmV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 99 YGASRHYdrnhfdqivqlldLSTLLD--------RYPVD-LSGGEKQRCAIARALLSEPEMLLMDEPLASLDLprkqEVM 169
Cdd:PRK11147 414 NGRPRHV-------------LGYLQDflfhpkraMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETL 476
|
170
....*....|....*....
gi 515592652 170 PFLEKLSQEINIPILYVTH 188
Cdd:PRK11147 477 ELLEELLDSYQGTVLLVSH 495
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
104-188 |
4.38e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 104 HYDRNHFD----QIVQLLDLS--TLLDrypvDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLprkqEVMPFLEKLSQ 177
Cdd:PRK11147 129 HHNLWQLEnrinEVLAQLGLDpdAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLK 200
|
90
....*....|.
gi 515592652 178 EINIPILYVTH 188
Cdd:PRK11147 201 TFQGSIIFISH 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
29-223 |
1.11e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.39 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGEralydSNKNINIAIDKRKIGYVFQEARLFPHYKVKGNLLYGasRHYDRN 108
Cdd:cd03289 35 LLGRTGSGKSTLLSAFLRLLNTEGDIQIDGV-----SWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDPYG--KWSDEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 109 HFdQIVQLLDLSTLLDRYP-------VD----LSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPRKQEVMPflEKLSQ 177
Cdd:cd03289 108 IW-KVAEEVGLKSVIEQFPgqldfvlVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIR--KTLKQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515592652 178 EI-NIPILYVTHSLEEILHlADHMLLIEDGQIKASGDIETMWRSTAF 223
Cdd:cd03289 184 AFaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
16-212 |
1.90e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSI-------------INAIS--------GLNNPDsgkiivgeralYDSNKNIN--IA 72
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSayarqflgQMDKPD-----------VDSIEGLSpaIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 73 IDKRKIGYVfqearlfPHYKV--------KGNLLYgaSRHYDRNHFDQIVQL-LDLSTLlDRYPVDLSGGEKQRCAIARA 143
Cdd:cd03270 82 IDQKTTSRN-------PRSTVgtvteiydYLRLLF--ARVGIRERLGFLVDVgLGYLTL-SRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 144 LLSEPEMLL--MDEPLASLDLPRKQEVMPFLEKLSQEINIpILYVTHSLEEILHlADHMLLI------EDGQIKASG 212
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
23-197 |
6.90e-05 |
|
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: 42.75 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 23 QHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVgeralydsnknINIaidkrkigyvfqearlfphykvkgnllygas 102
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------IDG------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 103 rhydrNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLD-----LPRKQEVMPFLEKLSQ 177
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRLLLLLKS 113
|
170 180
....*....|....*....|
gi 515592652 178 EINIPILYVTHSLEEILHLA 197
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPAL 133
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-162 |
9.23e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 9.23e-05
10 20 30
....*....|....*....|....*....|..
gi 515592652 131 SGGEKQRCAIARALLSEPEMLLMDEPLASLDL 162
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-208 |
1.04e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 31 GRSGAGKTSIINAISGLNNPDSGKIIVGERALYDSNKNiniaiDKRK-IGYVFQEARLFPHykvkgnLLYGASRHYDRNH 109
Cdd:PRK10522 356 GGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-----DYRKlFSAVFTDFHLFDQ------LLGPEGKPANPAL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 110 FDQIVQLLDLS--------TLLDrypVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlP--RK---QEVMPFLekls 176
Cdd:PRK10522 425 VEKWLERLKMAhkleledgRISN---LKLSKGQKKRLALLLALAEERDILLLDEWAADQD-PhfRRefyQVLLPLL---- 496
|
170 180 190
....*....|....*....|....*....|..
gi 515592652 177 QEINIPILYVTHSlEEILHLADHMLLIEDGQI 208
Cdd:PRK10522 497 QEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-215 |
1.11e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGeralydsnKNIniaidkrKIGYVFQEARLFphYKVKGNLLYGASRHYDRN 108
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGLA--------KGI-------KLGYFAQHQLEF--LRADESPLQHLARLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 109 HFDQIVQLL--------DLSTLLDRYpvdlSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLeklsQEIN 180
Cdd:PRK10636 406 LEQKLRDYLggfgfqgdKVTEETRRF----SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL----IDFE 477
|
170 180 190
....*....|....*....|....*....|....*.
gi 515592652 181 IPILYVTHSLEEILHLADHMLLIEDGQIKA-SGDIE 215
Cdd:PRK10636 478 GALVVVSHDRHLLRSTTDDLYLVHDGKVEPfDGDLE 513
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-217 |
1.36e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIivgERALYDSNKNINIAIDKRKIGYVFQEARLfphykvkg 95
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAISAGLSGQLTGIENIEFKM-------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 96 nLLYGASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLEKL 175
Cdd:PRK13546 111 -LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515592652 176 sQEINIPILYVTHSLEEILHLADHMLLIEDGQIKASGDIETM 217
Cdd:PRK13546 190 -KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-196 |
1.69e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.07 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIpQHGITAIFGRSGAGKTSIINAISGLNNPDSGKIIVGE---------------------------RALYDSNKN 68
Cdd:COG3593 16 DLSIEL-SDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEdfylgddpdlpeieieltfgsllsrllRLLLKEEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 69 INIAIDKRKIGYVFQEA-----RLFPHYKVKGNLLYGASRHYDRNHFDQIVQLLDLsTLLDRYPVDLSG-GEKQRCAIAR 142
Cdd:COG3593 95 EELEEALEELNEELKEAlkalnELLSEYLKELLDGLDLELELSLDELEDLLKSLSL-RIEDGKELPLDRlGSGFQRLILL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515592652 143 ALLS---------EPEMLLMDEPLASLDlPRKQEVmpFLEKLSQEINIP--ILYVTHS--------LEEILHL 196
Cdd:COG3593 174 ALLSalaelkrapANPILLIEEPEAHLH-PQAQRR--LLKLLKELSEKPnqVIITTHSphllsevpLENIRRL 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-222 |
1.71e-04 |
|
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: 43.75 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFGRSGAGKTSIINAISGLNNPDSGKIIVGEralydSNKNINIAIDKRKIGYVFQEARLFPHyKVKGNLlyGASRHYDRN 108
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLSTEGEIQIDGV-----SWNSVTLQTWRKAFGVIPQKVFIFSG-TFRKNL--DPYEQWSDE 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 109 HFDQIVQLLDLSTLLDRYP-------VD----LSGGEKQRCAIARALLSEPEMLLMDEPLASLDlPRKQEVMPflEKLSQ 177
Cdd:TIGR01271 1322 EIWKVAEEVGLKSVIEQFPdkldfvlVDggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQIIR--KTLKQ 1398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515592652 178 EI-NIPILYVTHSLEEILHlADHMLLIEDGQIKASGDIETMWRSTA 222
Cdd:TIGR01271 1399 SFsNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
24-126 |
2.40e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.71 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 24 HGITAIFGRSGAGKTSIINAI--------SGLNNPDSGKIIVGERALYDSNKNINIAidkrKIGYVFQEARLFPHYKVKG 95
Cdd:pfam13476 18 KGLTLITGPNGSGKTTILDAIklalygktSRLKRKSGGGFVKGDIRIGLEGKGKAYV----EITFENNDGRYTYAIERSR 93
|
90 100 110
....*....|....*....|....*....|.
gi 515592652 96 NLLYGASRHYDrNHFDQIVQLLDLSTLLDRY 126
Cdd:pfam13476 94 ELSKKKGKTKK-KEILEILEIDELQQFISEL 123
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-208 |
3.05e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGERAlydsnkniniaidkrKIGYVFQE-ARLFPHYKvkgNLLYGASRHYD 106
Cdd:PRK15064 349 AIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA---------------NIGYYAQDhAYDFENDL---TLFDWMSQWRQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 107 RNHFDQIV-----QLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDlprkqevMPFLEKLSQEINI 181
Cdd:PRK15064 411 EGDDEQAVrgtlgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMALEK 483
|
170 180 190
....*....|....*....|....*....|
gi 515592652 182 ---PILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PRK15064 484 yegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-208 |
3.27e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKIIVGER---ALYDSNKNINIAIDKRKIGYVfqeARLFPhykvkgnllyGASRH 104
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmAVFSQHHVDGLDLSSNPLLYM---MRCFP----------GVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 105 YDRNHFDQivqlLDLSTLLDRYPV-DLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLPRkqevmpfLEKLSQEINI-- 181
Cdd:PLN03073 606 KLRAHLGS----FGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA-------VEALIQGLVLfq 674
|
170 180
....*....|....*....|....*...
gi 515592652 182 -PILYVTHSLEEILHLADHMLLIEDGQI 208
Cdd:PLN03073 675 gGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-156 |
3.40e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 29 IFG---RSGAGKTSIINAISGLNNPDSGKI-IVGERAlyDSNkniNIAIDKRkIGYVFQEARLFPHYKVKGNL-----LY 99
Cdd:NF033858 294 IFGflgSNGCGKSTTMKMLTGLLPASEGEAwLFGQPV--DAG---DIATRRR-VGYMSQAFSLYGELTVRQNLelharLF 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 515592652 100 GASRHYDRNHFDQIVQLLDLSTLLDRYPVDLSGGEKQRCAIARALLSEPEMLLMDEP 156
Cdd:NF033858 368 HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-215 |
4.67e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGlnNPdSGKIIVGErALYdsnKNINI------AIDKRKIGYVFQearlFP 89
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HP-AYKILEGD-ILF---KGESIldlepeERAHLGIFLAFQ----YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 90 hYKVKG-------NLLYGASR-HYDRNHFDQ------IVQLLDL----STLLDRYPVD-LSGGEKQRCAIARALLSEPEM 150
Cdd:CHL00131 94 -IEIPGvsnadflRLAYNSKRkFQGLPELDPlefleiINEKLKLvgmdPSFLSRNVNEgFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 151 LLMDEPLASLDLPRKQEVMPFLEKLSQEINiPILYVTHS---LEEIlhLADHMLLIEDGQIKASGDIE 215
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYqrlLDYI--KPDYVHVMQNGKIIKTGDAE 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-217 |
5.76e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAISGLNNPDS--GKIIV-GERALYdsnKNINiaiDKRKIGYVF--QEARLFPH 90
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFdGEVCRF---KDIR---DSEALGIVIihQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 91 YKVKGNLLYG---ASRHY-DRNH-FDQIVQLL-------DLSTLLDrypvDLSGGEKQRCAIARALLSEPEMLLMDEPLA 158
Cdd:NF040905 93 LSIAENIFLGnerAKRGViDWNEtNRRARELLakvgldeSPDTLVT----DIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515592652 159 SLDLPRKQEVMPFLEKLSQEINIPILyVTHSLEEILHLADHMLLIEDGQIkasgdIETM 217
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRT-----IETL 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
112-188 |
5.83e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 41.66 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 112 QIVQLLDLSTLLDR---------YPVDLSGGEKQRCAIARALLSEPEMLLMDEPLASLDLprkqEVMPFLEKLSQEINIP 182
Cdd:TIGR00954 556 QILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGIT 631
|
....*.
gi 515592652 183 ILYVTH 188
Cdd:TIGR00954 632 LFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
16-103 |
9.45e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 16 DINVDIPQHGITAIFGRSGAGKTSIINAI------SGLN----NPDSGKIIVGERALydsNKNINiaIDKRKIG------ 79
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLINDTlypalaNRLNgaktVPGRYTSIEGLEHL---DKVIH--IDQSPIGrtprsn 700
|
90 100 110
....*....|....*....|....*....|...
gi 515592652 80 ---Y--VFQEAR-LF---PHYKVKGnllYGASR 103
Cdd:TIGR00630 701 patYtgVFDEIReLFaetPEAKVRG---YTPGR 730
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-161 |
1.94e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 26 ITAIFGRSGAGKTSIINAISGlnNPDSGKIIVGERALYDSnknINIA-IDKRKIGYVFQEARL---FPHYKVKGNLLYGA 101
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVITYDG---ITPEeIKKHYRGDVVYNAETdvhFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515592652 102 ------------SRHYDRNHF-DQIVQLLDLSTLLDRYPVD-----LSGGEKQRCAIARALLSEPEMLLMDEPLASLD 161
Cdd:TIGR00956 164 rcktpqnrpdgvSREEYAKHIaDVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
28-48 |
2.03e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 38.38 E-value: 2.03e-03
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
28-55 |
4.89e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 37.44 E-value: 4.89e-03
10 20
....*....|....*....|....*...
gi 515592652 28 AIFGRSGAGKTSIINAISGLNNPDSGKI 55
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDV 28
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| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
130-198 |
6.41e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 6.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515592652 130 LSGGEKQ------RCAIARALLSEPEMLLMDEPLASLDLPRKQEVMPFLE-KLSQEINIPILYVTHSLEEILHLAD 198
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIPQVIMISHHRELLSVAD 877
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| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-206 |
7.92e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515592652 117 LDLSTL-LDRYPVDLSGGEKQRCAIARALLSEPE--MLLMDEPLASLDLPRKQEVMPFLEKLSQEINiPILYVTHSlEEI 193
Cdd:PRK00635 463 LGLPYLtPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQM 540
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90
....*....|...
gi 515592652 194 LHLADHMLLIEDG 206
Cdd:PRK00635 541 ISLADRIIDIGPG 553
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| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
28-46 |
8.81e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.67 E-value: 8.81e-03
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| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
28-46 |
9.99e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 37.44 E-value: 9.99e-03
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