|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-572 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 531.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 1 MLNVFKKIWNFSKEEQVNIKKSILAGFLHAVFNALEFGAIYYMLVNIFSKTlDYKAIFICLGILVISLVGKIMTLKISQM 80
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 81 AQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLLVLVLGGVLnTLVFVLGTLI-FNVK 159
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV-TLIGALVVLFvIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 160 VGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEK 239
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 240 SVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAETILMIMASFIIFEGLIGAGSNMAILRACENAIDSV-GFIDSMP 318
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIfELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 319 DMRE--GSITEPIKNHDIVFKNVSFSYD-DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK 395
Cdd:COG1132 323 EIPDppGAVPLPPVRGEIEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 396 NIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEK 475
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 476 QRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLI 555
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
570
....*....|....*..
gi 1317668753 556 ENNGLYSDLINAKAKAE 572
Cdd:COG1132 563 ARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
57-569 |
1.87e-119 |
|
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: 369.16 E-value: 1.87e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 57 IFICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLG----R----------LTTIAT 122
Cdd:COG2274 196 WVLAIGLLLALLFEGLLRL-LRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGdlasRfrdvesirefLTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 123 SSLSQaemwVPMllvlvlggvlnTLVFVLGTLIFNVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLA 202
Cdd:COG2274 275 TALLD----LLF-----------VLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 203 TLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELplaeTILMIM 282
Cdd:COG2274 340 TLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQL----TLGQLI 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 283 ASFII-------FEGLIGAGSNMAILRAcenAIDSVGFIDSMPDMREGSITEPIKNH---DIVFKNVSFSY--DDRPILK 350
Cdd:COG2274 416 AFNILsgrflapVAQLIGLLQRFQDAKI---ALERLDDILDLPPEREEGRSKLSLPRlkgDIELENVSFRYpgDSPPVLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 351 NVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFG 430
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 431 KQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKE 510
Cdd:COG2274 573 DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILE 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 511 AIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLINAKA 569
Cdd:COG2274 653 NLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-559 |
8.91e-117 |
|
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: 357.92 E-value: 8.91e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 22 SILAGFLHAVFNALEFGAIYYMLVNIFSKTLDYKAIFICLGILVISLVGKIMTLKISQMAQTHAGYFMAAHKRIEIGEKI 101
Cdd:COG4988 22 AVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 102 KRVPMGFFSSFSLGRLTTIATSSLSQAE-------------MWVPMLlvlvlggvlnTLVFVLGtliFNVKVGLV--AVA 166
Cdd:COG4988 102 LALGPAWLRGKSTGELATLLTEGVEALDgyfarylpqlflaALVPLL----------ILVAVFP---LDWLSGLIllVTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 167 GVIVFFIVTSMM--EKKSSANADKMTetqtRLTKEVLATLQGMQVIKSYNLGGENNRALRKSIKD----TSKIL------ 234
Cdd:COG4988 169 PLIPLFMILVGKgaAKASRRQWRALA----RLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrTMKVLrvafls 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 235 ---LDLEKSVApytviqrIVMGittvfMVYVSLKLnLSGELPLAETILMIMASFIIFEGLIGAGSNMAILRACENAIDSV 311
Cdd:COG4988 245 savLEFFASLS-------IALV-----AVYIGFRL-LGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 312 -GFIDS-MPDMREGSITEPIKN-HDIVFKNVSFSYDD-RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNS 387
Cdd:COG4988 312 fALLDApEPAAPAGTAPLPAAGpPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 388 GEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGG 467
Cdd:COG4988 392 GSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 468 ASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVE 547
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
570
....*....|..
gi 1317668753 548 RGNHEKLIENNG 559
Cdd:COG4988 552 QGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
146-564 |
1.63e-113 |
|
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: 349.45 E-value: 1.63e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 146 TLVFVLGTLIFNVKVGLV-AVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGennrALR 224
Cdd:COG4987 143 ILAAVAFLAFFSPALALVlALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALD----RAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 225 KSIKDTSKILLDLEKSVAPYTVIQR----IVMGITTVFMVYVSLKLNLSGELP---LAETILMIMASFIIFEGLIGAGSN 297
Cdd:COG4987 219 ARLDAAEARLAAAQRRLARLSALAQallqLAAGLAVVAVLWLAAPLVAAGALSgplLALLVLAALALFEALAPLPAAAQH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 298 MAILRACENAIDSVgfIDSMPDMREGSITEPI-KNHDIVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTT 374
Cdd:COG4987 299 LGRVRAAARRLNEL--LDAPPAVTEPAEPAPApGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 375 FCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEA 454
Cdd:COG4987 377 LLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAA 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 455 LPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNA 534
Cdd:COG4987 457 LPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM 536
|
410 420 430
....*....|....*....|....*....|
gi 1317668753 535 DQILVLKDGEIVERGNHEKLIENNGLYSDL 564
Cdd:COG4987 537 DRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
334-564 |
3.85e-112 |
|
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: 333.81 E-value: 3.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISM 411
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADII 491
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDL 564
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
334-564 |
2.81e-109 |
|
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: 326.88 E-value: 2.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDD-RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIII 492
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDL 564
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
334-573 |
2.61e-106 |
|
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: 332.17 E-value: 2.61e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD-DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:COG5265 358 VRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIII 492
Cdd:COG5265 438 PQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLINAKAKAE 572
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEE 597
|
.
gi 1317668753 573 S 573
Cdd:COG5265 598 E 598
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
332-559 |
1.09e-103 |
|
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: 312.24 E-value: 1.09e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 332 HDIVFKNVSFSYD-DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSIS 410
Cdd:cd03254 1 GEIEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADI 490
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNG 559
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-566 |
2.35e-100 |
|
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: 315.50 E-value: 2.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 5 FKKIWNFSKEEQVNIKKSILAGFLHAVFNALEFGAIYYMLVNIFSKTLDYKAIFICLGILVISLVGKImtlkisqmAQTH 84
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGI--------CSFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 85 AGYFMA------AHK-RIEIGEKIKRVPMGFFSSFSLGRLTTIATSslsQAEMWVPMLLVLVLGGVLNTLVfVLGTLIF- 156
Cdd:TIGR02203 74 STYLLSwvsnkvVRDiRVRMFEKLLGLPVSFFDRQPTGTLLSRITF---DSEQVASAATDAFIVLVRETLT-VIGLFIVl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 157 ---NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYnlGGE----------NNRAL 223
Cdd:TIGR02203 150 lyySWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLF--GGQayetrrfdavSNRNR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 224 RKSIKdtskilldLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAETILMIMASFIIFEGlIGAGSNMAI--- 300
Cdd:TIGR02203 228 RLAMK--------MTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRP-LKSLTNVNApmq 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 301 --LRACENAIdsvGFIDSMPDMREGSITEPIKNHDIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFC 376
Cdd:TIGR02203 299 rgLAAAESLF---TLLDSPPEKDTGTRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 377 NLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGK-QNASHEEVVQAAKKARCHEFIEAL 455
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 456 PEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNAD 535
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
570 580 590
....*....|....*....|....*....|.
gi 1317668753 536 QILVLKDGEIVERGNHEKLIENNGLYSDLIN 566
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
334-567 |
6.10e-100 |
|
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: 302.92 E-value: 6.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRP---ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSIS 410
Cdd:cd03249 1 IEFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADI 490
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLINA 567
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
147-567 |
5.53e-97 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 307.27 E-value: 5.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 147 LVFVLGTLIF-NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGENNRALRK 225
Cdd:PRK13657 144 LVVLLPLALFmNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 226 SIKDtskiLLDLEKSV----APYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAETIlmimaSFIIFegligagSNMAIL 301
Cdd:PRK13657 224 IADN----LLAAQMPVlswwALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVV-----AFVGF-------ATLLIG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 302 RacenaIDSV-GFI-----------------DSMPDMREGSITEPIKN--HDIVFKNVSFSYDD-RPILKNVSAEIKENT 360
Cdd:PRK13657 288 R-----LDQVvAFInqvfmaapkleeffeveDAVPDVRDPPGAIDLGRvkGAVEFDDVSFSYDNsRQGVEDVSFEAKPGQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 361 MTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVV 440
Cdd:PRK13657 363 TVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMR 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 441 QAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKT 520
Cdd:PRK13657 443 AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRT 522
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1317668753 521 VIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLINA 567
Cdd:PRK13657 523 TFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
162-564 |
1.09e-94 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 301.17 E-value: 1.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 162 LVAVAGVIVFFI-VTSMMEKKSSANadkMTETQTRLTKEVLATLQGMQVIKSYnlGGEN----------NRALRKSIKDT 230
Cdd:PRK11176 171 LIVIAPIVSIAIrVVSKRFRNISKN---MQNTMGQVTTSAEQMLKGHKEVLIF--GGQEvetkrfdkvsNRMRQQGMKMV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 231 SKilldlekSVAPYTVIQrIVMGITTVFMVYV----SLKLNLSgelplAETILMIMASFII----FEGLIGAGSN----M 298
Cdd:PRK11176 246 SA-------SSISDPIIQ-LIASLALAFVLYAasfpSVMDTLT-----AGTITVVFSSMIAlmrpLKSLTNVNAQfqrgM 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 299 AilrACENAIdsvGFIDSMPDMREGSITEPIKNHDIVFKNVSFSYD--DRPILKNVSAEIKENTMTAIVGPSGSGKTTFC 376
Cdd:PRK11176 313 A---ACQTLF---AILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 377 NLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNA-SHEEVVQAAKKARCHEFIEAL 455
Cdd:PRK11176 387 NLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKM 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 456 PEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNAD 535
Cdd:PRK11176 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
410 420
....*....|....*....|....*....
gi 1317668753 536 QILVLKDGEIVERGNHEKLIENNGLYSDL 564
Cdd:PRK11176 547 EILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
333-564 |
1.11e-81 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 266.95 E-value: 1.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYD---DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSI 409
Cdd:TIGR02204 337 EIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARM 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:TIGR02204 417 ALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAP 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDL 564
Cdd:TIGR02204 497 ILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-544 |
3.64e-81 |
|
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: 251.92 E-value: 3.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDR--PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISM 411
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIkfgkqnasheevvqaakkarchefiealpegydtiigeggasLSGGEKQRISIARAMLKDADII 491
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGE 544
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
334-564 |
1.93e-74 |
|
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: 237.00 E-value: 1.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISM 411
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADII 491
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDL 564
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-540 |
1.87e-72 |
|
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: 241.04 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 21 KSILAGFLHAVFNALEFGAIYYMLVNIFSKTLDYKAIFICLGILVISLVGKIMTLKISQMAQTHAGYFMAAHKRIEIGEK 100
Cdd:TIGR02857 7 LLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 101 IKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLLVLVLGGVLNTLVFVLGTLIFNVKVG---LVAVAGVIVFFIVTSM 177
Cdd:TIGR02857 87 VAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGlilLLTAPLIPIFMILIGW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 178 MekkSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGENNRALRKSIKD----TSKIL---------LDLEKSVApy 244
Cdd:TIGR02857 167 A---AQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEyrerTMRVLriaflssavLELFATLS-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 245 tviqrivmgiTTVFMVYVSLKLnLSGELPLAE--TILMIMASFiiFEGLIGAGSNMAILRACENAIDSVG-FIDSMPdmR 321
Cdd:TIGR02857 242 ----------VALVAVYIGFRL-LAGDLDLATglFVLLLAPEF--YLPLRQLGAQYHARADGVAAAEALFaVLDAAP--R 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 322 EGSITEPIKNHD---IVFKNVSFSYDDR-PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI 397
Cdd:TIGR02857 307 PLAGKAPVTAAPassLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 398 KDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQR 477
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQR 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 478 ISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVL 540
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
147-567 |
5.57e-71 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 238.64 E-value: 5.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 147 LVFVLGTLIFNVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGENNRALRKS 226
Cdd:TIGR01192 145 FLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQF 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 227 IKDtskiLLDLEKSV----APYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAETIlmimaSFIIFEGL-IGAGSNMA-- 299
Cdd:TIGR01192 225 TNN----LLSAQYPVldwwALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVI-----AFIGFANLlIGRLDQMSgf 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 300 ---ILRACENAIDSVGFIDSMPDMREGSITEPIKN--HDIVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKT 373
Cdd:TIGR01192 296 itqIFEARAKLEDFFDLEDSVFQREEPADAPELPNvkGAVEFRHITFEFaNSSQGVFDVSFEAKAGQTVAIVGPTGAGKT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 374 TFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIE 453
Cdd:TIGR01192 376 TLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFIL 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 454 ALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRN 533
Cdd:TIGR01192 456 KRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRN 535
|
410 420 430
....*....|....*....|....*....|....
gi 1317668753 534 ADQILVLKDGEIVERGNHEKLIENNGLYSDLINA 567
Cdd:TIGR01192 536 ADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
95-564 |
1.54e-70 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 240.03 E-value: 1.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 95 IEIGEKIKR----VPMGFFSSFSLGRltTIA-TSSLSQAEMWVPMLLVLVLGGVLNTLVFVL------GTLIFNVKVGLV 163
Cdd:TIGR01846 212 VELGARLYRhllgLPLGYFESRRVGD--TVArVRELEQIRNFLTGSALTVVLDLLFVVVFLAvmffysPTLTGVVIGSLV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 164 AVAgvIVFFIVTSMMEKKSSANADKMTETQTRLTKEVlatlQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAP 243
Cdd:TIGR01846 290 CYA--LLSVFVGPILRKRVEDKFERSAAATSFLVESV----TGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 244 YTVIQRIVMGITTVFMVYVSLKLNLSGELPLAETIlmimaSFIIFEGLIGAgsnmAILRACEN---------AIDSVGFI 314
Cdd:TIGR01846 364 AGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLV-----AFNMLAGRVTQ----PVLRLAQLwqdfqqtgiALERLGDI 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 315 DSMP--DMREGSITEPIKNHDIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEI 390
Cdd:TIGR01846 435 LNSPtePRSAGLAALPELRGAITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQV 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 391 LIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASL 470
Cdd:TIGR01846 515 LVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 471 SGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGN 550
Cdd:TIGR01846 595 SGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGR 674
|
490
....*....|....
gi 1317668753 551 HEKLIENNGLYSDL 564
Cdd:TIGR01846 675 HEELLALQGLYARL 688
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
146-546 |
2.78e-69 |
|
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: 233.49 E-value: 2.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 146 TLVFVLGTLIFNVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSynLG--------- 216
Cdd:COG4618 143 APIFLAVLFLFHPLLGLLALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEA--MGmlpalrrrw 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 217 -GENNRALRKSIK--DTSKILLDLEKSVApyTVIQRIVMGITTVfmvyvslkLNLSGELplaeTI-LMIMASFII----- 287
Cdd:COG4618 221 qRANARALALQARasDRAGGFSALSKFLR--LLLQSAVLGLGAY--------LVIQGEI----TPgAMIAASILMgrala 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 288 -FEGLIGAGSNMAILRACENAIDSvgFIDSMPDmREGSITEPIKNHDIVFKNVSFSY--DDRPILKNVSAEIKENTMTAI 364
Cdd:COG4618 287 pIEQAIGGWKQFVSARQAYRRLNE--LLAAVPA-EPERMPLPRPKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 365 VGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNI-KFGkqNASHEEVVQAA 443
Cdd:COG4618 364 IGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 444 KKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETL-TKNKTVI 522
Cdd:COG4618 442 KLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVV 521
|
410 420
....*....|....*....|....
gi 1317668753 523 MIAHRLKTIRNADQILVLKDGEIV 546
Cdd:COG4618 522 VITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
336-545 |
1.63e-68 |
|
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: 221.19 E-value: 1.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRP---ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:cd03248 14 FQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIII 492
Cdd:cd03248 94 GQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEI 545
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
188-561 |
1.77e-68 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 231.64 E-value: 1.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 188 KMTETQTRLTKEVLATLQGMQVIKSYNLggenNRALRKSIKDTSKILLDLEKSVAPYTVI-QRIVM---GITTVFMVYVS 263
Cdd:PRK11160 191 DLTHLRAQYRVQLTEWLQGQAELTLFGA----EDRYRQQLEQTEQQWLAAQRRQANLTGLsQALMIlanGLTVVLMLWLA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 264 LKLNLSGELP---LAETILMIMASFIIFEGLIGAGSNMAILRACENAIDSVgfIDSMPDMR-EGSITEPIKNHDIVFKNV 339
Cdd:PRK11160 267 AGGVGGNAQPgalIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEI--TEQKPEVTfPTTSTAAADQVSLTLNNV 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 340 SFSYDDR--PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVY 417
Cdd:PRK11160 345 SFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVH 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 418 LFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEAlPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEAT 497
Cdd:PRK11160 425 LFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 498 ANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLY 561
Cdd:PRK11160 504 EGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRY 567
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
89-565 |
1.60e-67 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 232.31 E-value: 1.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 89 MAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLLVLVLGgvlnTLVFVLGTLIF----NVKVGLVA 164
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLR----NLVMLLGLLGFmlwlSPRLTMVT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 165 VAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYnlGGENNRALRKSIKDTSKILLDLEKSVA-- 242
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSF--AAEEGEASRFKEALEETLQLNKRKALAya 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 243 PYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAETIlmimaSFIIFEglIGAGSNMAILRACENAI-DSVG-------FI 314
Cdd:TIGR00958 386 GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV-----SFLLYQ--EQLGEAVRVLSYVYSGMmQAVGasekvfeYL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 315 DSMPDMR-EGSITEPIKNHDIVFKNVSFSYDDRP---ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEI 390
Cdd:TIGR00958 459 DRKPNIPlTGTLAPLNLEGLIEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 391 LIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASL 470
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 471 SGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIEtlTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGN 550
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGT 696
|
490
....*....|....*
gi 1317668753 551 HEKLIENNGLYSDLI 565
Cdd:TIGR00958 697 HKQLMEDQGCYKHLV 711
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
147-565 |
1.57e-66 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 229.45 E-value: 1.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 147 LVFVLGTLIFNVKVGLVAV---AGVIVFFIVTSMMEKKSSAnadKMTETQTRLTKEVLATLQGMQVIKSYnlGGENNrAL 223
Cdd:TIGR03796 282 VFYALLMLLYDPVLTLIGIafaAINVLALQLVSRRRVDANR---RLQQDAGKLTGVAISGLQSIETLKAS--GLESD-FF 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 224 RKSIKDTSKILL---DLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELplaeTILM------IMASFII-FEGLIG 293
Cdd:TIGR03796 356 SRWAGYQAKLLNaqqELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQL----TIGMlvafqsLMSSFLEpVNNLVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 294 AGSNMAILRACENAIDSVGFIDSMPDMREGSITEPIKNHD------IVFKNVSFSYD--DRPILKNVSAEIKENTMTAIV 365
Cdd:TIGR03796 432 FGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPPrrlsgyVELRNITFGYSplEPPLIENFSLTLQPGQRVALV 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 366 GPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKK 445
Cdd:TIGR03796 512 GGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKD 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 446 ARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETltKNKTVIMIA 525
Cdd:TIGR03796 592 AAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVA 669
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1317668753 526 HRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLI 565
Cdd:TIGR03796 670 HRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-550 |
1.17e-64 |
|
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: 210.81 E-value: 1.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSIS 410
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFEDTIENNIK-FGKqnASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGN 550
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
147-528 |
7.35e-62 |
|
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: 212.99 E-value: 7.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 147 LVFVLGTLIFNVKVGLVAVAGVIVFFIVTSMMekksSANADKMTET-----QTRLTKEVLATLQGMQVIKSYnlgGENNR 221
Cdd:TIGR02868 142 AAAVAAIAVLSVPAALILAAGLLLAGFVAPLV----SLRAARAAEQalarlRGELAAQLTDALDGAAELVAS---GALPA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 222 ALRKsIKDTSKILLDLEKSVAPYTVI----QRIVMGITTVFMVYVSLKLNLSGELP---LAETILMIMASFIIFEGLIGA 294
Cdd:TIGR02868 215 ALAQ-VEEADRELTRAERRAAAATALgaalTLLAAGLAVLGALWAGGPAVADGRLApvtLAVLVLLPLAAFEAFAALPAA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 295 GSnmAILRACENAIDSVGFIDSMPDMREGSI----TEPIKNHDIVFKNVSFSYDDRPI-LKNVSAEIKENTMTAIVGPSG 369
Cdd:TIGR02868 294 AQ--QLTRVRAAAERIVEVLDAAGPVAEGSApaagAVGLGKPTLELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 370 SGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCH 449
Cdd:TIGR02868 372 SGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLA 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 450 EFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRL 528
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
340-564 |
1.86e-61 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 213.04 E-value: 1.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 340 SFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVY 417
Cdd:PRK10789 320 QFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 418 LFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEAT 497
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 498 ANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDL 564
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
104-567 |
2.49e-60 |
|
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: 212.68 E-value: 2.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 104 VPMGFFSSFSLGRLTT-----------IATSSLSQ-AEMWVpMLLVLVLGGVLNTLVFVLGtlifnvkvgLVAVAGVIVf 171
Cdd:TIGR01193 242 LPMSFFSTRRTGEIVSrftdassiidaLASTILSLfLDMWI-LVIVGLFLVRQNMLLFLLS---------LLSIPVYAV- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 172 fIVTSMMEKKSSANADKMtETQTRLTKEVLATLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIV 251
Cdd:TIGR01193 311 -IIILFKRTFNKLNHDAM-QANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVT 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 252 MGITTVFMVYVSLKLNLSGELPLAETIL--MIMASFII-FEGLIGAGSNMAILRACENAIDSVGFIDSmPDMREGSITEP 328
Cdd:TIGR01193 389 KLILNVVILWTGAYLVMRGKLTLGQLITfnALLSYFLTpLENIINLQPKLQAARVANNRLNEVYLVDS-EFINKKKRTEL 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 329 IK-NHDIVFKNVSFSYD-DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLM 406
Cdd:TIGR01193 468 NNlNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 NSISMVFQDVYLFEDTIENNIKFG-KQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAML 485
Cdd:TIGR01193 548 QFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 486 KDADIIIFDEATANIDPENEDKLKEAIETLtKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLI 565
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
..
gi 1317668753 566 NA 567
Cdd:TIGR01193 707 HN 708
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
332-549 |
1.00e-58 |
|
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: 195.12 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 332 HDIVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSI 409
Cdd:cd03245 1 GRIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERG 549
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
318-561 |
8.47e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 203.41 E-value: 8.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 318 PDMREGSITEPIKNHDIVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKN 396
Cdd:PRK10790 325 PRQQYGNDDRPLQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 397 IKDYKIENLMNSISMVFQDVYLFEDTIENNIKFGKqNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQ 476
Cdd:PRK10790 405 LSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 477 RISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIE 556
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
....*
gi 1317668753 557 NNGLY 561
Cdd:PRK10790 564 AQGRY 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
341-568 |
4.00e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 201.61 E-value: 4.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 341 FSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNsGEILIGGKNIKDYKIENLMNSISMVFQDVYLFE 420
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 421 DTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANI 500
Cdd:PRK11174 437 GTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 501 DPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLINAK 568
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
148-545 |
3.49e-54 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 192.56 E-value: 3.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 148 VFVLGTLIFNVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGEnnraLRKSI 227
Cdd:TIGR01842 131 IYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGN----LTKRW 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 228 KDTSKILLDLEkSVAPYTVIqrIVMGITTVF-MVYVSLKLNLSGELPLAETI---LMIMASFII------FEGLIGAGSN 297
Cdd:TIGR01842 207 GRFHSKYLSAQ-SAASDRAG--MLSNLSKYFrIVLQSLVLGLGAYLAIDGEItpgMMIAGSILVgralapIDGAIGGWKQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 298 MAILRACENAIDsvGFIDSMPDMREG-SITEPikNHDIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTT 374
Cdd:TIGR01842 284 FSGARQAYKRLN--ELLANYPSRDPAmPLPEP--EGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKST 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 375 FCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNI-KFGkQNASHEEVVQAAKKARCHEFIE 453
Cdd:TIGR01842 360 LARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFG-ENADPEKIIEAAKLAGVHELIL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 454 ALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIR 532
Cdd:TIGR01842 439 RLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLG 518
|
410
....*....|...
gi 1317668753 533 NADQILVLKDGEI 545
Cdd:TIGR01842 519 CVDKILVLQDGRI 531
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
334-554 |
5.34e-52 |
|
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: 177.76 E-value: 5.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN-----SGEILIGGKNI--KDYKIENLM 406
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 NSISMVFQDVYLFEDTIENNIKFG-------KQNASHEEVVQAAKKArchefieALP-EGYDTIigeGGASLSGGEKQRI 478
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKA-------ALWdEVKDRL---HALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLK-TIRNADQILVLKDGEIVERGNHEKL 554
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
334-549 |
5.99e-52 |
|
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: 175.58 E-value: 5.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD--DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKiENLMNSISM 411
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIkfgkqnasheevvqaakkarchefiealpegydtiigegGASLSGGEKQRISIARAMLKDADII 491
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERG 549
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
334-557 |
1.34e-51 |
|
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: 176.75 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQ--DVYLFEDTIENNIKFGKQNA--SHEEVVQAAKKA----RCHEFIEALPegydtiigeggASLSGGEKQRISIARAM 484
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGPENLglPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
335-544 |
1.46e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 175.73 E-value: 1.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 335 VFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQ--DVYLFEDTIENNIKFGKQNA--SHEEVVQAAKKA----RCHEFIEALPEgydtiigeggaSLSGGEKQRISIARAM 484
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLglPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTIRN-ADQILVLKDGE 544
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
334-545 |
5.72e-48 |
|
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: 165.08 E-value: 5.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISM 411
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIkfgkqnasheevvqaakkarchefiealpegydtiigeggasLSGGEKQRISIARAMLKDADII 491
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTIRNADQILVLKDGEI 545
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
316-561 |
7.77e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 177.14 E-value: 7.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 316 SMPDMRE-GSITepIKNHDIV-----FKNVSFSYDDRP---ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDV- 385
Cdd:PTZ00265 1144 SNIDVRDnGGIR--IKNKNDIkgkieIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLk 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 386 -----------------------------------------------------NSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:PTZ00265 1222 ndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIV 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIII 492
Cdd:PTZ00265 1302 SQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILL 1381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRNADQILVL----KDGEIVE-RGNHEKLIE-NNGLY 561
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSvQDGVY 1458
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
334-545 |
7.54e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.37 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVF 413
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFEDTIENNIKFGKQNASheevvQAAKKARCHEFIEA--LPEGY-DTIIGEggasLSGGEKQRISIARAMLKDADI 490
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQLRE-----RKFDRERALELLERlgLPPDIlDKPVER----LSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAHRLKTI-RNADQILVLKDGEI 545
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-549 |
2.76e-45 |
|
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: 159.11 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSIS 410
Cdd:cd03369 6 EIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFEDTIENNI-KFGKQnaSHEEVVQAAKkarchefiealpegydtiIGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERG 549
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
336-544 |
4.41e-45 |
|
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: 156.64 E-value: 4.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQd 415
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 vylfedtiennikfgkqnasheevvqaakkarchefiealpegydtiigeggasLSGGEKQRISIARAMLKDADIIIFDE 495
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 496 ATANIDPENEDKLKEAIETLT-KNKTVIMIAHRLKTIRNA-DQILVLKDGE 544
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-544 |
1.69e-44 |
|
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: 156.86 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDR-----PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGknikdykienlmnS 408
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQDVYLFEDTIENNIKFGKQ--NASHEEVVQAakkarC--HEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAM 484
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKA-----CalEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKL-KEAI-ETLTKNKTVIMIAHRLKTIRNADQILVLKDGE 544
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-545 |
2.36e-43 |
|
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: 154.18 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDD----RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLM--- 406
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 -NSISMVFQDVYLFED-TIENNIKFGkqnASHEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAM 484
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRNADQILVLKDGEI 545
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
334-549 |
2.53e-42 |
|
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: 151.13 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmNSISMVF 413
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFG--KQNASHEEVvqaakKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADI 490
Cdd:cd03259 79 QDYALFPHlTVAENIAFGlkLRGVPKAEI-----RARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAHRL-KTIRNADQILVLKDGEIVERG 549
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
326-557 |
7.83e-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: 157.76 E-value: 7.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 326 TEPIknhdIVFKNVSFSYDDR-----PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDY 400
Cdd:COG1123 257 AEPL----LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 401 KIENLMN---SISMVFQDVY--LFE-DTIENNIKFGKQNasHEEVVQAAKKARCHEFIEA--LPEGYdtiIGEGGASLSG 472
Cdd:COG1123 333 SRRSLRElrrRVQMVFQDPYssLNPrMTVGDIIAEPLRL--HGLLSRAERRERVAELLERvgLPPDL---ADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 473 GEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*...
gi 1317668753 550 NHEKLIEN 557
Cdd:COG1123 488 PTEEVFAN 495
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
334-547 |
1.69e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.42 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDD----RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENL---- 405
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 406 MNSISMVFQDVYLFED-TIENNIKFG------KQNASHEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRI 478
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRNADQILVLKDGEIVE 547
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
337-549 |
6.57e-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: 146.04 E-value: 6.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFqdv 416
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 ylfedtiennikfgkqnasheevvQAAKKARCHEFIEalpEGYDTiigeggasLSGGEKQRISIARAMLKDADIIIFDEA 496
Cdd:cd03214 80 ------------------------QALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 497 TANIDPENEDKLKEAIETLTK--NKTVIMIAHRLK-TIRNADQILVLKDGEIVERG 549
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
334-556 |
1.02e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.52 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIEnLMNSISMVF 413
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFgkqNASHEEVVQAAKKARCHEFIEA--LPEGYDTIIGeggaSLSGGEKQRISIARAMLKDADI 490
Cdd:COG1131 80 QEPALYPDlTVRENLRF---FARLYGLPRKEARERIDELLELfgLTDAADRKVG----TLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKLIE 556
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
334-578 |
1.80e-40 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 157.88 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRP---ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIG-GKNIKDYKIENLMNSI 409
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFEDTIENNIKFG----------------KQNASHE------------------------------------ 437
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 438 -----EVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAI 512
Cdd:PTZ00265 543 tikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 513 ETL--TKNKTVIMIAHRLKTIRNADQILVLKDGE---------------------------------------------- 544
Cdd:PTZ00265 623 NNLkgNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnags 702
|
330 340 350
....*....|....*....|....*....|....*.
gi 1317668753 545 -IVERGNHEKLIEN-NGLYSDLINAKaKAESWKLNN 578
Cdd:PTZ00265 703 yIIEQGTHDALMKNkNGIYYTMINNQ-KVSSKKSSN 737
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
334-547 |
4.87e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.20 E-value: 4.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKN---IKDYKIENLMNSI 409
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFED-TIENNIKF-----GKQNASHEEVVQAA---------KKARCHEfiealpegydtiigeggasLSGGE 474
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREVldlvglsdkAKALPHE-------------------LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 475 KQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRNADQ-ILVLKDGEIVE 547
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
334-560 |
6.45e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 146.42 E-value: 6.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTfcnlIARFWDV----NSGEILIGGKNIKDykIENLMN 407
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKST----LAKLLNGlllpTSGKVTVDGLDTLD--EENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 ---SISMVFQ--DVYLFEDTIENNIKFGKQNA--SHEEVVQ----AAKKARCHEFIEALPegydtiigeggASLSGGEKQ 476
Cdd:TIGR04520 75 irkKVGMVFQnpDNQFVGATVEDDVAFGLENLgvPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 477 RISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAHRLKTIRNADQILVLKDGEIVERG----- 549
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtprei 223
|
250
....*....|..
gi 1317668753 550 -NHEKLIENNGL 560
Cdd:TIGR04520 224 fSQVELLKEIGL 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-557 |
8.02e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.98 E-value: 8.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN---SGEILIGGKNIKDYKIENLMNS 408
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQD--VYLFEDTIENNIKFGKQNASheeVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLK 486
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALENLG---LSRAEARARVLELLEAV--GLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 487 DADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
333-567 |
1.61e-39 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 145.05 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSIS 410
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFEDTIENNIKfGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADI 490
Cdd:cd03288 99 IILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLI-ENNGLYSDLINA 567
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
336-549 |
2.10e-39 |
|
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: 143.80 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDR----PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI--KDYKIENLM-NS 408
Cdd:cd03257 4 VKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIRrKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQDVYL-------FEDTIENNIKFGKQNASHEEVVQAAKKARCH-----EFIEALPegydtiigeggASLSGGEKQ 476
Cdd:cd03257 84 IQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYP-----------HELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 477 RISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
334-554 |
4.11e-39 |
|
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: 143.03 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI------KDYKIENLMn 407
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglseaELYRLRRRM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 siSMVFQDVYLFED-TIENNIKFG---KQNASHEEVvqaAKKARchEFIEA--LPEGYDTIIGEggasLSGGEKQRISIA 481
Cdd:cd03261 80 --GMLFQSGALFDSlTVFENVAFPlreHTRLSEEEI---REIVL--EKLEAvgLRGAEDLYPAE----LSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKL 554
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-549 |
6.48e-39 |
|
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: 143.26 E-value: 6.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVF 413
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNI---------KFGKQNASHEEVVQAA-KKARCHEFIEALpegYDTiigeggasLSGGEKQRISIAR 482
Cdd:COG1120 82 QEPPAPFGlTVRELValgryphlgLFGRPSAEDREAVEEAlERTGLEHLADRP---VDE--------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 483 AMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLK-TIRNADQILVLKDGEIVERG 549
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-558 |
1.83e-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: 141.66 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI---KDYKIENLMNSIS 410
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFED-TIENNIKFG-KQnasHEEVVQAAKKARCHEFIEA--LPEGYDTIIGEggasLSGGEKQRISIARAMLK 486
Cdd:COG1127 86 MLFQGGALFDSlTVFENVAFPlRE---HTDLSEAEIRELVLEKLELvgLPGAADKMPSE----LSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 487 DADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIENN 558
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
334-544 |
1.88e-38 |
|
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: 139.24 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMN--SISM 411
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFED-TIENNIKFGkqnasheevvqaakkarchefiealpegydtiigeggasLSGGEKQRISIARAMLKDADI 490
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAHRLK-TIRNADQILVLKDGE 544
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
349-498 |
3.20e-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: 137.78 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLF-EDTIENNI 427
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 428 KFGkqnASHEEVVQAAKKARCHEFIEALPEGY--DTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATA 498
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
334-557 |
3.66e-38 |
|
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: 140.90 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFED-TIENNIKFgkqNASHEEVVQAAKKARCHEFIEAL---PEGY-DTIIGEggasLSGGEKQRISIARAMLKD 487
Cdd:cd03295 81 IQQIGLFPHmTVEENIAL---VPKLLKWPKEKIRERADELLALVgldPAEFaDRYPHE----LSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-545 |
8.18e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 8.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKienlmNSISMVF 413
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYL---F----EDTIENNIK-----FGKQNASHEEVVQAA-KKARCHEFIealpegyDTIIGEggasLSGGEKQRISI 480
Cdd:COG1121 82 QRAEVdwdFpitvRDVVLMGRYgrrglFRRPSRADREAVDEAlERVGLEDLA-------DRPIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 481 ARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTIR-NADQILVLKDGEI 545
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
328-557 |
1.73e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 139.74 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 328 PIKNHDIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENL 405
Cdd:PRK13632 2 KNKSVMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 406 MNSISMVFQ--DVYLFEDTIENNIKFGKQNA--SHEE----VVQAAKKARCHEFIEALPEgydtiigeggaSLSGGEKQR 477
Cdd:PRK13632 82 RKKIGIIFQnpDNQFIGATVEDDIAFGLENKkvPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 478 ISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAHRLKTIRNADQILVLKDGEIVERG------ 549
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGkpkeil 230
|
....*...
gi 1317668753 550 NHEKLIEN 557
Cdd:PRK13632 231 NNKEILEK 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
320-557 |
1.82e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 139.40 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 320 MREGSITEPIKnhdIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN-----SGEILIGG 394
Cdd:COG1117 1 MTAPASTLEPK---IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 395 KNI--KDYKIENLMNSISMVFQDVYLFEDTIENNIKFG------KQNASHEEVVQAA-KKArchefieALPEGYDTIIGE 465
Cdd:COG1117 78 EDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKA-------ALWDEVKDRLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 466 GGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLK-TIRNADQILVLKDGE 544
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGE 230
|
250
....*....|...
gi 1317668753 545 IVERGNHEKLIEN 557
Cdd:COG1117 231 LVEFGPTEQIFTN 243
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
54-561 |
2.52e-37 |
|
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: 148.56 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 54 YKAIFICLGILVIslvgkimtlkISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVP 133
Cdd:TIGR00957 1011 YGALGILQGFAVF----------GYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIP 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 134 ----MLLVLVLGGVLNTLVFVLGTLIFNVkvgLVAVAGVIVFFIVTSMMekkSSANADKMTETQTR--LTKEVLATLQGM 207
Cdd:TIGR00957 1081 pvikMFMGSLFNVIGALIVILLATPIAAV---IIPPLGLLYFFVQRFYV---ASSRQLKRLESVSRspVYSHFNETLLGV 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 208 QVIKSYNlggennRALRKSIKDTSKILLDlEKSVAPYTVIQRivmgittvfmvYVSLKLNLSGE-LPLAETILMIMASFI 286
Cdd:TIGR00957 1155 SVIRAFE------EQERFIHQSDLKVDEN-QKAYYPSIVANR-----------WLAVRLECVGNcIVLFAALFAVISRHS 1216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 287 IFEGLIGAGSNMAI---------LRACENAIDSVGFIDSMPDMREGSITEPIKNHD------------IVFKNVSFSYdd 345
Cdd:TIGR00957 1217 LSAGLVGLSVSYSLqvtfylnwlVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEtappsgwpprgrVEFRNYCLRY-- 1294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 346 RP----ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFED 421
Cdd:TIGR00957 1295 REdldlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSG 1374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 TIENNIK-FGKQnaSHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANI 500
Cdd:TIGR00957 1375 SLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 501 DPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLY 561
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
334-557 |
3.77e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.82 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI--KDYKIENLMNSISM 411
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFED-TIENNIKFGK---QNASHEEvvqAAKKARCH-------EFIEALPegydtiigeggASLSGGEKQRISI 480
Cdd:COG1126 82 VFQQFNLFPHlTVLENVTLAPikvKKMSKAE---AEERAMELlervglaDKADAYP-----------AQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 481 ARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
334-545 |
9.03e-37 |
|
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: 134.45 E-value: 9.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIEnLMNSISMVF 413
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKfgkqnasheevvqaakkarchefiealpegydtiigeggasLSGGEKQRISIARAMLKDADIII 492
Cdd:cd03230 80 EEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTIRN-ADQILVLKDGEI 545
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-546 |
1.37e-35 |
|
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: 132.38 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRP-ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKienLMNSISMVFQD 415
Cdd:cd03226 3 ENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 V--YLFEDTIENNIKFGKQNAS--HEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAMLKDADII 491
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDagNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTI-RNADQILVLKDGEIV 546
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
334-545 |
1.93e-35 |
|
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: 132.27 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI--KDYKIENLMNSISM 411
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFED-TIENNIKFGK---QNASHEEVVQAA----KKARCHEFIEALPegydtiigeggASLSGGEKQRISIARA 483
Cdd:cd03262 81 VFQQFNLFPHlTVLENITLAPikvKGMSKAEAEERAlellEKVGLADKADAYP-----------AQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 484 MLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEI 545
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
336-541 |
3.51e-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: 131.50 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikdyKIENLMNSISMVFQ- 414
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 415 -DV-YLFEDTIENNIKFGkqNASHEEVVQAAKKARCHEFIEALpegyDTI---------IGEggasLSGGEKQRISIARA 483
Cdd:cd03235 77 rSIdRDFPISVRDVVLMG--LYGHKGLFRRLSKADKAKVDEAL----ERVglseladrqIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 484 MLKDADIIIFDEATANIDPENEDKLKEAIETLT-KNKTVIMIAHRLKTI-RNADQILVLK 541
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVlEYFDRVLLLN 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
334-558 |
3.77e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.19 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPilKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmNSISMVF 413
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFG-----KQNAS-HEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAMLK 486
Cdd:COG3840 78 QENNLFPHlTVAQNIGLGlrpglKLTAEqRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 487 DADIIIFDEATANIDPenedKLKEAIETLTK------NKTVIMIAHRLK-TIRNADQILVLKDGEIVERGNHEKLIENN 558
Cdd:COG3840 147 KRPILLLDEPFSALDP----ALRQEMLDLVDelcrerGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-546 |
1.16e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 134.04 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIE--NlmnsIS 410
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrN----IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFED-TIENNIKFG----KQNAS--HEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARA 483
Cdd:COG3839 79 MVFQSYALYPHmTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 484 MLKDADIIIFDEATANIDPenedKLKEAIETLTK------NKTVIMIAH------RLktirnADQILVLKDGEIV 546
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDA----KLRVEMRAEIKrlhrrlGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQ 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-554 |
4.78e-34 |
|
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: 129.54 E-value: 4.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY----DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSI 409
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYL-------FEDTIENNIKFGKQNASHEEVVQAAKKArchefieALPEGY-DTIIGEggasLSGGEKQRISIA 481
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQV-------GLPPSFlDRYPHQ----LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKL 554
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADL 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
333-549 |
5.35e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.14 E-value: 5.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIE--NlmnsIS 410
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEkrN----VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFED-TIENNIKFGkqnASHEEVVQAAKKARCHEFIE--ALpEGY-DTIIGEggasLSGGEKQRISIARAMLK 486
Cdd:COG3842 81 MVFQDYALFPHlTVAENVAFG---LRMRGVPKAEIRARVAELLElvGL-EGLaDRYPHQ----LSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 487 DADIIIFDEATANIDPenedKLKEAIETLTK------NKTVIMIAH------RLktirnADQILVLKDGEIVERG 549
Cdd:COG3842 153 EPRVLLLDEPLSALDA----KLREEMREELRrlqrelGITFIYVTHdqeealAL-----ADRIAVMNDGRIEQVG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-558 |
7.68e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 7.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISM 411
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQ--DVYLFEDTIENNIKFGKQN--ASHEEVV----QAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARA 483
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGLENigVPREEMVervdQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 484 MLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENN 558
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
334-573 |
3.73e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 135.68 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRP-ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISM 411
Cdd:PTZ00243 1309 LVFEGVQMRYrEGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIKFGKQnASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLK-DADI 490
Cdd:PTZ00243 1389 IPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGF 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIEN-NGLYSDLINAKA 569
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNrQSIFHSMVEALG 1547
|
....
gi 1317668753 570 KAES 573
Cdd:PTZ00243 1548 RSEA 1551
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-557 |
4.06e-33 |
|
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: 126.68 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIEnlMNSISMVFQDVYLFED-TIENNI 427
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 428 KFGKQnasHEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDK 507
Cdd:cd03299 93 AYGLK---KRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 508 LKEAIETLTKNK--TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:cd03299 168 LREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-548 |
2.05e-32 |
|
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: 124.12 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDR----PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikdyKIENLMNSI 409
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFE-DTIENNIKFGkqnASHEEVVQAAKKARCHEFIEALpegydtiiGEGGAS------LSGGEKQRISIAR 482
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLELV--------GLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 483 AMLKDADIIIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAHRL-KTIRNADQILVL--KDGEIVER 548
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIdEAVFLADRVVVLsaRPGRIVAE 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
305-578 |
2.57e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.18 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 305 ENAIDSVGFIDSMPDMrEGSITEPIKNH----------DIVFKNVSFSYDDR--PILKNVSAEIKENTMTAIVGPSGSGK 372
Cdd:PLN03232 1197 ENSLNSVERVGNYIDL-PSEATAIIENNrpvsgwpsrgSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGK 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 373 TTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIENNIK-FGKQNASheEVVQAAKKARCHEF 451
Cdd:PLN03232 1276 SSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDpFSEHNDA--DLWEALERAHIKDV 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 452 IEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTI 531
Cdd:PLN03232 1354 IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI 1433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1317668753 532 RNADQILVLKDGEIVERGNHEKLIENNG-LYSDLINAKAKAESWKLNN 578
Cdd:PLN03232 1434 IDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTGPANAQYLSN 1481
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
334-557 |
1.06e-31 |
|
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: 122.69 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDR----PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMN-- 407
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 -SISMVFQDVYLFED-TIENNIKFGKQNASheeVVQAAKKARCHEFIEalpegydtIIGEGG------ASLSGGEKQRIS 479
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLEIAG---VPKAEIEERVLELLE--------LVGLEDkadaypAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 480 IARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIE 556
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 1317668753 557 N 557
Cdd:cd03258 231 N 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-559 |
1.97e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 130.63 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISM 411
Cdd:PLN03130 1238 IKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIK-FGKQNASheEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADI 490
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNLDpFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNG 559
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
318-572 |
3.64e-31 |
|
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: 129.68 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 318 PDMREGSITEPIKNHDIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGk 395
Cdd:TIGR00957 621 PDSIERRTIKPGEGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 396 nikdykienlmnSISMVFQDVYLFEDTIENNIKFGK--QNASHEEVVQAakkarCHEF--IEALPEGYDTIIGEGGASLS 471
Cdd:TIGR00957 700 ------------SVAYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEA-----CALLpdLEILPSGDRTEIGEKGVNLS 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 472 GGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAI---ETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVER 548
Cdd:TIGR00957 763 GGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
250 260
....*....|....*....|....
gi 1317668753 549 GNHEKLIENNGLYSDLINAKAKAE 572
Cdd:TIGR00957 843 GSYQELLQRDGAFAEFLRTYAPDE 866
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-557 |
5.67e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.17 E-value: 5.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN-----SGEILIGGKNIKDYKIENLMNS 408
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQ------DVYLFEDtIENNIKFGKQNASHEE----VVQAAKKARchefieaLPEGYDTIIGEGGASLSGGEKQRI 478
Cdd:PRK14247 84 VQMVFQipnpipNLSIFEN-VALGLKLNRLVKSKKElqerVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAH-RLKTIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
334-545 |
6.37e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 121.76 E-value: 6.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD---DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSIS 410
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQ--DVYLFEDTIENNIKFGKQNA--SHEE----VVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIAR 482
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENKgiPHEEmkerVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 483 AMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRNADQILVLKDGEI 545
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
334-546 |
8.20e-31 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 120.37 E-value: 8.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNS---I 409
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFED-TIENNIKFGKQNASHeeVVQA-------AKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIA 481
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRRS--TWRSlfglfpkEEKQRALAALERV--GLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAHRLKTIR-NADQILVLKDGEIV 546
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
330-556 |
8.25e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.01 E-value: 8.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 330 KNHDIVFKNVSFSY--DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMN 407
Cdd:PRK13648 4 KNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 SISMVFQ--DVYLFEDTIENNIKFGKQNAS------HEEVVQAAKKARCHEFIEALPEgydtiigeggaSLSGGEKQRIS 479
Cdd:PRK13648 84 HIGIVFQnpDNQFVGSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 480 IARAMLKDADIIIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIE 556
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-547 |
8.34e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.96 E-value: 8.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY----DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDykienLMNSI 409
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFE-DTIENNIKFGkqnASHEEVVQAAKKARCHEFIE---------ALPegydtiigeggASLSGGEKQRIS 479
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELLElvglagfedAYP-----------HQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 480 IARAMLKDADIIIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAH------RLktirnADQILVLKD--GEIVE 547
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
334-557 |
3.91e-30 |
|
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: 118.11 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKD---YKienlmNSIS 410
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHK-----RPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFED-TIENNIKFG------KQNASHEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARA 483
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 484 MLKDADIIIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAH-RLKTIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-564 |
4.22e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 119.73 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYDDRP-----ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGG----KNIKDYK-I 402
Cdd:PRK13645 6 DIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKeV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 403 ENLMNSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEVVQaakkaRCHEFIE--ALPEGYdtiIGEGGASLSGGEKQ 476
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNlgENKQEAYK-----KVPELLKlvQLPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 477 RISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEK 553
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFE 237
|
250
....*....|.
gi 1317668753 554 LIENNGLYSDL 564
Cdd:PRK13645 238 IFSNQELLTKI 248
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
334-572 |
2.65e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.88 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDR-PI----LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYK------- 401
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 402 -----------------IENLMNSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEVVQAAKKarcheFIE--ALPEG 458
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAK-----YIElvGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 459 YdtiIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTI-RNADQ 536
Cdd:PRK13651 158 Y---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKR 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1317668753 537 ILVLKDGEIVERG-------NHEKLIENNGLYSDLINAKAKAE 572
Cdd:PRK13651 235 TIFFKDGKIIKDGdtydilsDNKFLIENNMEPPKLLNFVNKLE 277
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
330-557 |
2.70e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.21 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 330 KNHDIVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFW---DVNSGEILIGGKNIKDYKIEN 404
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 405 LMNSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEVVQAAKKARCH----EFIEALPegydtiigeggASLSGGEKQ 476
Cdd:PRK13640 82 IREKVGIVFQnpDNQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADvgmlDYIDSEP-----------ANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 477 RISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKL 554
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
...
gi 1317668753 555 IEN 557
Cdd:PRK13640 231 FSK 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
334-545 |
2.82e-29 |
|
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: 115.20 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYK---IENLMNSI 409
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFED-TIENNIKFGKqnasheEVVQAAKKARCHEFIEALPE-GYDTIIGEGGASLSGGEKQRISIARAMLKD 487
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFAL------EVTGVPPREIRKRVPAALELvGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQ--ILVLKDGEI 545
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
333-554 |
2.99e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.43 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYD-----DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIG------GKNIKDYK 401
Cdd:PRK13634 2 DITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 402 ieNLMNSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEvvqAAKKARchEFIE--ALPEgydTIIGEGGASLSGGEK 475
Cdd:PRK13634 82 --PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEED---AKQKAR--EMIElvGLPE---ELLARSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 476 QRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHE 552
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
..
gi 1317668753 553 KL 554
Cdd:PRK13634 232 EI 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
334-549 |
3.18e-29 |
|
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: 115.04 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmNSISMVF 413
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFG------KQNASHEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAMLK 486
Cdd:cd03301 79 QNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 487 DADIIIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAH-RLKTIRNADQILVLKDGEIVERG 549
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
334-557 |
1.72e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.65 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYK--IENLMNSISM 411
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvdERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFED-TIENNIKFGKQNasheevVQAAKKARCHEFIEALPE--GYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:PRK09493 82 VFQQFYLFPHlTALENVMFGPLR------VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
334-549 |
2.16e-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: 112.67 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIkENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKiENLMNSISMVF 413
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QD--------VYLFEDTIennikfgkqnASHEEVVQAAKKARCHEFIEA--LPEGYDTIIGeggaSLSGGEKQRISIARA 483
Cdd:cd03264 79 QEfgvypnftVREFLDYI----------AWLKGIPSKEVKARVDEVLELvnLGDRAKKKIG----SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 484 MLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
328-549 |
2.89e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 115.33 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 328 PIKNHDIV-FKNVSFSYDDRP-----ILKNVSAEIKENTMTAIVGPSGSGKTTFCN-----LIARFWDVNSGEILIGG-- 394
Cdd:PRK13631 15 PLSDDIILrVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDkk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 395 -----------KNIKDYKieNLMNSISMVFQ--DVYLFEDTIENNIKFGKQNASHEEVvQAAKKARCH--------EFIE 453
Cdd:PRK13631 95 nnhelitnpysKKIKNFK--ELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKS-EAKKLAKFYlnkmglddSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 454 ALPEGydtiigeggasLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRL-KTI 531
Cdd:PRK13631 172 RSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMeHVL 240
|
250
....*....|....*...
gi 1317668753 532 RNADQILVLKDGEIVERG 549
Cdd:PRK13631 241 EVADEVIVMDKGKILKTG 258
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
339-549 |
3.77e-28 |
|
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: 111.82 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 339 VSFSYDDRPIlkNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKdyKIENLMNSISMVFQDVYL 418
Cdd:cd03298 6 IRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 419 FED-TIENNIKFG-----KQNASHEEVVQ-AAKKARCHEFIEALPEgydtiigeggaSLSGGEKQRISIARAMLKDADII 491
Cdd:cd03298 82 FAHlTVEQNVGLGlspglKLTAEDRQAIEvALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
334-546 |
3.83e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 110.21 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK--NIKDYKiENLMNSISM 411
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPR-DARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQdvylfedtiennikfgkqnasheevvqaakkarchefiealpegydtiigeggasLSGGEKQRISIARAMLKDADII 491
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGEIV 546
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
334-549 |
5.83e-28 |
|
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: 110.72 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD------DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIA--RFWDVNSGEILIGGKNIKDykiENL 405
Cdd:cd03213 4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 406 MNSISMVFQDVYLFED-TIENNIKFgkqnasheevvqaAKKARchefiealpegydtiigeggaSLSGGEKQRISIARAM 484
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF-------------AAKLR---------------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKT--IRNADQILVLKDGEIVERG 549
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
325-557 |
6.17e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.56 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 325 ITEPIknhdIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN-----SGEILIGGKNIKD 399
Cdd:PRK14239 1 MTEPI----LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 400 YKIE--NLMNSISMVFQDVYLFEDTIENNIKFG------KQNASHEEVVQAAKKARC--HEFIEALpegYDTIIGeggas 469
Cdd:PRK14239 77 PRTDtvDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEKSLKGASiwDEVKDRL---HDSALG----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 470 LSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTI-RNADQILVLKDGEIVER 548
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEY 228
|
....*....
gi 1317668753 549 GNHEKLIEN 557
Cdd:PRK14239 229 NDTKQMFMN 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
349-557 |
6.68e-28 |
|
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: 112.74 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMN----SISMVFQDVYLF-EDTI 423
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 424 ENNIKFGKqnasheEVVQAAKKARCHEFIEALP----EGY-DTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATA 498
Cdd:cd03294 120 LENVAFGL------EVQGVPRAEREERAAEALElvglEGWeHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 499 NIDPENEDKLKEAIETLTKN--KTVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
334-550 |
7.79e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.22 E-value: 7.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD-----DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIE--NLM 406
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 NSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEVVQAAKKArchefIEALPEGYDTIIGEGGASLSGGEKQRISIAR 482
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINlgLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 483 AMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERGN 550
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-549 |
1.34e-27 |
|
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: 110.99 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI---KDYKIENLmnSISMVFQDVYLFED-TIE 424
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPHEIARL--GIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 425 NNIKFGKQNASHEEVVQAAKK-------ARCHEFIEA--LPEGYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDE 495
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARreerearERAEELLERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 496 ATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:cd03219 170 PAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
334-550 |
1.42e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 113.63 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVS--FSYDDRPI--LKNVSAEIKENTMTAIVGPSGSGKTTF--C-NLIARFwdvNSGEILIGGKNIKDYKIENLM 406
Cdd:COG1135 2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLirCiNLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 N---SISMVFQDVYLFED-TIENNIKF-----GkqnasheeVVQAAKKARCHEFIE---------ALPegydtiigeggA 468
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENVALpleiaG--------VPKAEIRKRVAELLElvglsdkadAYP-----------S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 469 SLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDK----LKEAIETLtkNKTVIMIAHRLKTIRN-ADQILVLKDG 543
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSildlLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENG 217
|
....*..
gi 1317668753 544 EIVERGN 550
Cdd:COG1135 218 RIVEQGP 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
331-560 |
5.13e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.60 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 331 NHDIVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSI 409
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDV--YLFEDTIENNIKFGKQNA--SHEEV---VQAAKKA-RCHEFIEALPEgydtiigeggaSLSGGEKQRISIA 481
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVNMglDKDEVerrVEEALKAvRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLK-TIRNADQILVLKDGEIVERG-----NHEKL 554
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDI 230
|
....*.
gi 1317668753 555 IENNGL 560
Cdd:PRK13647 231 VEQAGL 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
334-554 |
9.40e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.25 E-value: 9.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD-----DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI----KDYKIEN 404
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 405 LMNSISMVFQ--DVYLFEDTIENNIKFGKQNASH--EEVvqaakKARCHEFIEALPEGYDtIIGEGGASLSGGEKQRISI 480
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMnlDEV-----KNYAHRLLMDLGFSRD-VMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 481 ARAMLKDADIIIFDEATANIDPENEDKLKEAIETLT--KNKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKL 554
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-557 |
1.90e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 330 KNHDIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN-----SGEILIGGKNIKDYKIE- 403
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 404 -NLMNSISMVFQDVYLFED-TIENNIKFG-------KQNASHEEVVQ-AAKKArchefieALPEGYDTIIGEGGASLSGG 473
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHlTIYDNVAIGvklnglvKSKKELDERVEwALKKA-------ALWDEVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 474 EKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHR-LKTIRNADQILVLKDGEIVERGNHE 552
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTR 233
|
....*
gi 1317668753 553 KLIEN 557
Cdd:PRK14267 234 KVFEN 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
330-554 |
2.50e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.19 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 330 KNHDIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmNSI 409
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFED-TIENNIKFG--KQNASHEEVVQAAKKARCHEFIEALPEGY-DTIigeggaslSGGEKQRISIARAML 485
Cdd:PRK11432 81 CMVFQSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYvDQI--------SGGQQQRVALARALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 486 KDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAH-RLKTIRNADQILVLKDGEIVERGNHEKL 554
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
333-549 |
4.47e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.12 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDykIENLMNSISMV 412
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFED-TIENNIKFG------KQNASHEEVVQAAKKARCHEFIEALPEgydtiigeggaSLSGGEKQRISIARAML 485
Cdd:PRK11000 81 FQSYALYPHlSVAENMSFGlklagaKKEEINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 486 KDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAH-RLKTIRNADQILVLKDGEIVERG 549
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-578 |
5.22e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.68 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD---DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCN-LIARFWDVNSGEILIGGknikdykienlmnSI 409
Cdd:PLN03130 615 ISIKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------------TV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFEDTIENNIKFGK--QNASHEEVVQAAkkARCHEfIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKD 487
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSpfDPERYERAIDVT--ALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 488 ADIIIFDEATANIDPE-NEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLIN 566
Cdd:PLN03130 759 SDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
250
....*....|..
gi 1317668753 567 AKAKAESWKLNN 578
Cdd:PLN03130 839 NAGKMEEYVEEN 850
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
349-556 |
6.02e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK--NIKDYKiENLMNSISMVFQDVYLFED-TIEN 425
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPR-DAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 426 NIKFGKQNASHEEVVQAAKKARCHEFIEAL-----PegyDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATANI 500
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRARELLARLgldidP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 501 DPENEDKLKEAIETLT-KNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERG-----NHEKLIE 556
Cdd:COG1129 172 TEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
341-544 |
7.40e-26 |
|
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: 107.25 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 341 FSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikdykienlmnsISMVFQDVYLFE 420
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 421 DTIENNIKFGkqnASHEE-----VVQAAKkarCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDE 495
Cdd:cd03291 112 GTIKENIIFG---VSYDEyryksVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1317668753 496 ATANIDPENEDKLKEA-IETLTKNKTVIMIAHRLKTIRNADQILVLKDGE 544
Cdd:cd03291 186 PFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
334-549 |
8.93e-26 |
|
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: 106.32 E-value: 8.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARF-WDVNSGEILIGGKNIKDYKIENLMNSI--- 409
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFEDTIENNI---KFGK----QNASHEEvvqaakKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIAR 482
Cdd:COG1119 84 SPALQLRFPRDETVLDVVlsgFFDSiglyREPTDEQ------RERARELLELL--GLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 483 AMLKDADIIIFDEATANIDPENEDKLKEAIETL--TKNKTVIMIAHRLKTIRNA-DQILVLKDGEIVERG 549
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
326-550 |
9.20e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.79 E-value: 9.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 326 TEPIKNHDIVFK--NVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWD-VNS----GEILIGGKNIK 398
Cdd:PRK14243 1 TSTLNGTETVLRteNLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 399 DYKIE--NLMNSISMVFQDVYLFEDTIENNIKFGKQ----NASHEEVVQAAKKArchefiEALPEGYDTIIGEGGASLSG 472
Cdd:PRK14243 81 APDVDpvEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSLRQ------AALWDEVKDKLKQSGLSLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 473 GEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGN 550
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-557 |
1.23e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 106.27 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNS-----GEILIGGKNIKDYK--IENLM 406
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRvnLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 NSISMVFQDVYLFEDTIENNIKFG------KQNASHEEVVQAAKKArchefiealPEGYDTI---IGEGGASLSGGEKQR 477
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD---------ADLWDEIkhkIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 478 ISIARAMLKDADIIIFDEATANIDPENEDKLKEAIET--LTKNKTVIMIAHRLKTI-RNADQILVLKD-----GEIVERG 549
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVEFG 238
|
....*...
gi 1317668753 550 NHEKLIEN 557
Cdd:PRK14258 239 LTKKIFNS 246
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
337-557 |
2.09e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 104.44 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKD---YKIENLmnSISMVF 413
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppHERARA--GIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFGKQNASHEEVVQAAKKA-----RCHEFIEALpegydtiigegGASLSGGEKQRISIARAMLKD 487
Cdd:cd03224 82 EGRRIFPElTVEENLLLGAYARRRAKRKARLERVyelfpRLKERRKQL-----------AGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
337-540 |
2.70e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.41 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDV 416
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLFEDTIENNIKFGKQ--NASHEEVVQAAKKARcheFieALPEgydTIIGEGGASLSGGEKQRISIARAMLKDADIIIFD 494
Cdd:PRK10247 91 TLFGDTVYDNLIFPWQirNQQPDPAIFLDDLER---F--ALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1317668753 495 EATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRNADQILVL 540
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-542 |
3.62e-25 |
|
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: 103.33 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDyKIENLMNSISMVF 413
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKF----GKQNASHEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAMLKDA 488
Cdd:COG4133 82 HADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRnADQILVLKD 542
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARgGAVLLTTHQPLELA-AARVLDLGD 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
244-543 |
7.88e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 244 YTVIQRIVMGITTVFMVYVSLKLNLSGELPLAEtILMIMASFIIFEG----LIGAGSNMAILRACENAIDsvGFIDSMPD 319
Cdd:COG4178 268 LTFFTTGYGQLAVIFPILVAAPRYFAGEITLGG-LMQAASAFGQVQGalswFVDNYQSLAEWRATVDRLA--GFEEALEA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 320 MRE----GSITEPIKNHDIVFKNVS-FSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILI-- 392
Cdd:COG4178 345 ADAlpeaASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpa 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 393 GGKnikdykienlmnsisMVF--QDVYLFEDTIENNIKF--GKQNASHEEVVQAAKKARCHEFIEALPEGYDTiigegGA 468
Cdd:COG4178 425 GAR---------------VLFlpQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQ 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 469 SLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDG 543
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-555 |
8.75e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.12 E-value: 8.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPILKNVSAEIKEntMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmNSISMVFQDVY 417
Cdd:PRK10771 6 DITWLYHHLPMRFDLTVERGE--RVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 418 LFED-TIENNIKFG-----KQNAS-HEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAMLKDADI 490
Cdd:PRK10771 82 LFSHlTVAQNIGLGlnpglKLNAAqREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 491 IIFDEATANIDPenedKLKEAIETL------TKNKTVIMIAHRLK-TIRNADQILVLKDGEIVERGNHEKLI 555
Cdd:PRK10771 151 LLLDEPFSALDP----ALRQEMLTLvsqvcqERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
334-557 |
1.07e-24 |
|
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: 102.80 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmNSISMVF 413
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFG-KQNASHEEVVQAAKKARCHEF-----IEALPEGYDtiigeggASLSGGEKQRISIARAMLK 486
Cdd:cd03296 81 QHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELlklvqLDWLADRYP-------AQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 487 DADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAH-RLKTIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-557 |
1.12e-24 |
|
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: 104.75 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPI--LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN---SGEILIGGKNIKDYKIENLM----NS 408
Cdd:COG0444 8 KVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQDVY-----------LFEDTIENNIKFGKQNAsHEEVVQAAKK-------ARC----HEFiealpegydtiigeg 466
Cdd:COG0444 88 IQMIFQDPMtslnpvmtvgdQIAEPLRIHGGLSKAEA-RERAIELLERvglpdpeRRLdrypHEL--------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 467 gaslSGGEKQRISIARAMLKDADIIIFDEATANIDPENE----DKLKEAIETLtkNKTVIMIAHRLKTIRN-ADQILVLK 541
Cdd:COG0444 152 ----SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQaqilNLLKDLQREL--GLAILFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*.
gi 1317668753 542 DGEIVERGNHEKLIEN 557
Cdd:COG0444 226 AGRIVEEGPVEELFEN 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
345-546 |
2.28e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 101.58 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 345 DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIA---RFWDVNSGEILIGGKNIKDYKIEnlmNSISMVFQDVYLFED 421
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 -TIENNIKFGKQNASHEEVVQAAKKARchEFIEALPEGYDTIIG----EGgasLSGGEKQRISIARAMLKDADIIIFDEA 496
Cdd:cd03234 96 lTVRETLTYTAILRLPRKSSDAIRKKR--VEDVLLRDLALTRIGgnlvKG---ISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 497 TANIDPENEDKLkeaIETL----TKNKTVIMIAH--RLKTIRNADQILVLKDGEIV 546
Cdd:cd03234 171 TSGLDSFTALNL---VSTLsqlaRRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-552 |
2.61e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGG------KNIKDYKIENLMN 407
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 SISMVFQDVYLF------EDTIENNIKFGKQNASH--EEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRIS 479
Cdd:COG4161 83 KVGMVFQQYNLWphltvmENLIEAPCKVLGLSKEQarEKAMKLLARLRLTDKADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 480 IARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHE 552
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
337-559 |
2.96e-24 |
|
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: 100.29 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWD--VNSGEILIGGKNIKDYKI-ENLMNSISMVF 413
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeERARLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFEdtiennikfGKQNAsheevvqaakkarchEFIEALPEGydtiigeggasLSGGEKQRISIARAMLKDADIIIF 493
Cdd:cd03217 84 QYPPEIP---------GVKNA---------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 494 DEATANIDPENEDKLKEAIETL-TKNKTVIMIAHR---LKTIRnADQILVLKDGEIVERGNHE--KLIENNG 559
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHYqrlLDYIK-PDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
334-557 |
3.05e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.75 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIG------GKNIKDYK--IENL 405
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 406 MNSISMVFQDVYLF-EDTIENNIKFGKQNASHEEVVQAAKKARchefiEALPEgydtiIGEGGAS------LSGGEKQRI 478
Cdd:PRK11264 84 RQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARAR-----ELLAK-----VGLAGKEtsyprrLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIE 556
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
.
gi 1317668753 557 N 557
Cdd:PRK11264 234 D 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
334-560 |
5.82e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDY-KIENLMNSISM 411
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQ--DVYLFEDTIENNIKFGKQNASHEEVVQAAKKARchefieALPE-GYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDR------ALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGL 560
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-568 |
8.72e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 101.33 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDV-----NSGEILIGGKNIKDYK-IENLMNSISM 411
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIKFGKQnaSHEEV----VQAAKKARCHEFieALPEGYDTIIGEGGASLSGGEKQRISIARAMLKD 487
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVR--AHKLVprkeFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEKLIEN--------- 557
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSpkhaetary 261
|
250
....*....|..
gi 1317668753 558 -NGLYSDLINAK 568
Cdd:PRK14271 262 vAGLSGDVKDAK 273
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
336-543 |
8.73e-24 |
|
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: 106.53 E-value: 8.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNvsFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikdykienlmnsISMVFQD 415
Cdd:TIGR01271 431 FSN--FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 VYLFEDTIENNIKFGkqnASHEEV--VQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIF 493
Cdd:TIGR01271 496 SWIMPGTIKDNIIFG---LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 494 DEATANIDPENEDKLKEA-IETLTKNKTVIMIAHRLKTIRNADQILVLKDG 543
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
334-557 |
1.28e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.15 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIA--RFWDvnSGEILIGGkniKDYKIeNLmnS--- 408
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAglETPD--SGRIVLNG---RDLFT-NL--Ppre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 --ISMVFQDVYLFED-TIENNIKFGkqnASHEEVVQAAKKARCHEFIEAL---------PegydtiigeggASLSGGEKQ 476
Cdd:COG1118 75 rrVGFVFQHYALFPHmTVAENIAFG---LRVRPPSKAEIRARVEELLELVqlegladryP-----------SQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 477 RISIARAMLKDADIIIFDEATANID----PENEDKLKEAIETLtkNKTVIMIAH-RLKTIRNADQILVLKDGEIVERGNH 551
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTP 218
|
....*.
gi 1317668753 552 EKLIEN 557
Cdd:COG1118 219 DEVYDR 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
334-557 |
1.71e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD-----DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIK----DYKIEN 404
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 405 LMNSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEVVQAAKKarcheFIE--ALPEgydTIIGEGGASLSGGEKQRI 478
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKALK-----WLKkvGLSE---DLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIE 556
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
.
gi 1317668753 557 N 557
Cdd:PRK13641 235 D 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
334-573 |
1.86e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 105.44 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD---DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCN-LIARFWDVNSGEILIGGknikdykienlmnSI 409
Cdd:PLN03232 615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------------SV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFEDTIENNIKFGKQNAShEEVVQAAKKARCHEFIEALPeGYD-TIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFGSDFES-ERYWRAIDVTALQHDLDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEA-IETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLINA 567
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN 839
|
....*.
gi 1317668753 568 KAKAES 573
Cdd:PLN03232 840 AGKMDA 845
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
338-557 |
2.08e-23 |
|
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: 99.15 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKI-ENLMNSISMVFQDV 416
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLFED-TIENNIKfgkqnASHEEvvQAAKKARCHEFIEALPE--GYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIF 493
Cdd:cd03218 85 SIFRKlTVEENIL-----AVLEI--RGLSKKEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 494 DEATANIDPENEDKLKEAIETLTKNKTVIMIA-HRLK-TIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
349-546 |
2.33e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.57 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikDYKIEN----LMNSISMVFQDVYLFED-TI 423
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 424 ENNIKFGkqNASHEEVVQAAKKARchEFIEALPEGY------DTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEAT 497
Cdd:COG3845 98 AENIVLG--LEPTKGGRLDRKAAR--ARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 498 ANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIR-NADQILVLKDGEIV 546
Cdd:COG3845 170 AVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
333-555 |
5.07e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 333 DIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFED-TIENNIKFGKQ----------NASHEEVVQAAKKARCHEFIEALPEgydtiigeggaSLSGGEKQRISIA 481
Cdd:PRK11231 82 PQHHLTPEGiTVRELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEKLI 555
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
334-549 |
6.57e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.66 E-value: 6.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD-----DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI----KDYKIEN 404
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 405 LMNSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEVVQAAKKARchefieALPEGYDTIIGEGGASLSGGEKQRISI 480
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKL------ALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 481 ARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
330-550 |
1.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 330 KNHDIVFKNVSFSYDD------RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYK-I 402
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 403 ENLMNSISMVFQ--DVYLFEDTIENNIKFGKQNAS------HEEVVQAAKKARCHEFIEALPEgydtiigeggaSLSGGE 474
Cdd:PRK13633 81 WDIRNKAGMVFQnpDNQIVATIVEEDVAFGPENLGippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 475 KQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRNADQILVLKDGEIVERGN 550
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
334-543 |
1.46e-22 |
|
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: 96.25 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFcnLIARFWDVN--SGEILIGGKNIKDYKIENLMN--- 407
Cdd:cd03290 1 VQVTNGYFSWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNKNESEPSFEATRSrnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 -SISMVFQDVYLFEDTIENNIKFGK--QNASHEEVVQAAKkarCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAM 484
Cdd:cd03290 79 ySVAYAAQKPWLLNATVEENITFGSpfNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKLKEA--IETLTKNK-TVIMIAHRLKTIRNADQILVLKDG 543
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
337-549 |
1.80e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.46 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKdYKIENLMN---SISMV 412
Cdd:PRK13639 5 RDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEvrkTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQ--DVYLFEDTIENNIKFGKQNA--SHEEVvqaakKARCHEFIEALP-EGYDTiigEGGASLSGGEKQRISIARAMLKD 487
Cdd:PRK13639 84 FQnpDDQLFAPTVEEDVAFGPLNLglSKEEV-----EKRVKEALKAVGmEGFEN---KPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGiTIIISTHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
334-566 |
2.14e-22 |
|
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: 97.23 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDD--RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNsGEILIGGKNIKDYKIENLMNSISM 411
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFEDTIENNIK-FGKQnaSHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADI 490
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLIN 566
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
334-546 |
4.44e-22 |
|
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: 94.88 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVS--FSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKdYKIENLMNSISM 411
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFED-TIENNIKF-----GKqnaSHEEVvqaakKARCHEFIEA--LPEGYDTIIGEggasLSGGEKQRISIARA 483
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGL---PKSEI-----KEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 484 MLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRN-ADQILVLKDGEIV 546
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
334-545 |
4.99e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmNSISMVF 413
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFG--KQNASHEE----VVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAMLK 486
Cdd:PRK09452 93 QSYALFPHmTVFENVAFGlrMQKTPAAEitprVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 487 DADIIIFDEATANID----PENEDKLKEAIETLtkNKTVIMIAH-RLKTIRNADQILVLKDGEI 545
Cdd:PRK09452 162 KPKVLLLDESLSALDyklrKQMQNELKALQRKL--GITFVFVTHdQEEALTMSDRIVVMRDGRI 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-554 |
2.40e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.57 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 327 EPIKNHDIVFkNVSFSY---DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNS------GEILIGGKNI 397
Cdd:PRK14246 2 EAGKSAEDVF-NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 398 KDYKIENLMNSISMVFQDVYLFED-TIENNIKFGKQNASHEEVVQAAK-KARCHEFIEALPEGYDTIiGEGGASLSGGEK 475
Cdd:PRK14246 81 FQIDAIKLRKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYDRL-NSPASQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 476 QRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKL 554
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
332-554 |
2.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.10 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 332 HDIVFKNVSFSYD-DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSIS 410
Cdd:PRK13652 2 HLIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQ--DVYLFEDTIENNIKFGKQNASHEEvvqAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:PRK13652 82 LVFQnpDDQIFSPTVEQDIAFGPINLGLDE---ETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKL 554
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-552 |
4.14e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFC---NL--IARfwdvnSGEILIGG------KNIKDYKI 402
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLleMPR-----SGTLNIAGnhfdfsKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 403 ENLMNSISMVFQDVYLF------EDTIENNIK---FGKQNAsHEEVVQAAKKARCHEFIEALPegydtiigeggASLSGG 473
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWphltvqQNLIEAPCRvlgLSKDQA-LARAEKLLERLRLKPYADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 474 EKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNH 551
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
.
gi 1317668753 552 E 552
Cdd:PRK11124 226 S 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
351-549 |
5.12e-21 |
|
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: 91.59 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 351 NVSAEIKENTmTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNS----ISMVFQDVYLFED-TIEN 425
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 426 NIKFGKQNASheevvQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENE 505
Cdd:cd03297 95 NLAFGLKRKR-----NREDRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1317668753 506 DKLKEAIETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:cd03297 168 LQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-549 |
6.12e-21 |
|
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: 94.41 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 352 VSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLM----NSISMVFQDVYLFED-TIENN 426
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppekRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 427 IKFGKQNASHEEvvqaaKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENED 506
Cdd:TIGR02142 96 LRYGMKRARPSE-----RRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1317668753 507 KLKEAIETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:TIGR02142 169 EILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAG 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
337-558 |
7.14e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.52 E-value: 7.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNS---ISMVF 413
Cdd:PRK11831 11 RGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFGKQNASH--EEVVQAAKKARchefIEAlpegydtiIGEGGAS------LSGGEKQRISIARAM 484
Cdd:PRK11831 91 QSGALFTDmNVFDNVAYPLREHTQlpAPLLHSTVMMK----LEA--------VGLRGAAklmpseLSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIENN 558
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANP 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
337-557 |
7.63e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.59 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRP---------ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMN 407
Cdd:COG4167 8 RNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 SISMVFQDVylfEDTIENNIKFGKQ-------------NASHEEVVQAAKKarchefIEALPEGYDTIIGEggasLSGGE 474
Cdd:COG4167 88 HIRMIFQDP---NTSLNPRLNIGQIleeplrlntdltaEEREERIFATLRL------VGLLPEHANFYPHM----LSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 475 KQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTV--IMIAHRLKTIRN-ADQILVLKDGEIVERGNH 551
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKT 234
|
....*.
gi 1317668753 552 EKLIEN 557
Cdd:COG4167 235 AEVFAN 240
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
337-557 |
1.74e-20 |
|
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: 90.81 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNS-ISMVFQD 415
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 VYLFED-TIENNIKFGkqnasheevvqAAKKARCHEFIEALPEGYDT--IIGE----GGASLSGGEKQRISIARAMLKDA 488
Cdd:COG0410 87 RRIFPSlTVEENLLLG-----------AYARRDRAEVRADLERVYELfpRLKErrrqRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLAD 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-526 |
2.44e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD----DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmnsi 409
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFE--DTIENnIKFGKQNASheeVVQAAKKARCHEFIEalpegydtIIGEGGA------SLSGGEKQRISIA 481
Cdd:COG4525 79 GVVFQKDALLPwlNVLDN-VAFGLRLRG---VPKAERRARAEELLA--------LVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAH 526
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
339-572 |
2.84e-20 |
|
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: 95.75 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 339 VSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNsGEILIGGKNIKDYKIENLMNSISMVFQDVYL 418
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 419 FEDTIENNIKFGKQnASHEEVVQAAKKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATA 498
Cdd:TIGR01271 1304 FSGTFRKNLDPYEQ-WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 499 NIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNGLYSDLINAKAKAE 572
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLK 1456
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
337-557 |
2.91e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDykIENLMNSISMVFQDV 416
Cdd:PRK11607 23 RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLFED-TIENNIKFG-KQnashEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFD 494
Cdd:PRK11607 101 ALFPHmTVEQNIAFGlKQ----DKLPKAEIASRVNEMLGLV--HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 495 EATANIDPENEDKLK-EAIETLTK-NKTVIMIAH-RLKTIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK11607 175 EPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
334-549 |
3.82e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.79 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD--DRPI--LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLM--- 406
Cdd:PRK11153 2 IELKNISKVFPqgGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 NSISMVFQDVYLFED-TIENNIKFG--KQNASHEEVvqaakKARCHEFIE--ALPEGYDTIigegGASLSGGEKQRISIA 481
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPleLAGTPKAEI-----KARVTELLElvGLSDKADRY----PAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDK----LKEAIETLtkNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSilelLKDINREL--GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
337-549 |
3.95e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.22 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDV 416
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YL-FEDTIENNIKFGK-----QNASHEEVVQAA-KKARCHEFIEALpegYdtiigeggASLSGGEKQRISIARAM--LKD 487
Cdd:PRK13548 86 SLsFPFTVEEVVAMGRaphglSRAEDDALVAAAlAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLaqLWE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 488 AD----IIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLK-TIRNADQILVLKDGEIVERG 549
Cdd:PRK13548 155 PDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
331-554 |
8.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.77 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 331 NHDIVFKNVSFSYD---DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMN 407
Cdd:PRK13642 2 NKILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 408 SISMVFQ--DVYLFEDTIENNIKFGKQNAS--HEEVVQAAKKA----RCHEFIEALPegydtiigeggASLSGGEKQRIS 479
Cdd:PRK13642 82 KIGMVFQnpDNQFVGATVEDDVAFGMENQGipREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 480 IARAMLKDADIIIFDEATANIDPENEDKLKEAIETLtKNK---TVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKL 554
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
337-559 |
1.09e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 88.93 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARF--WDVNSGEILIGGKNIKDYKIENLMN-SISMVF 413
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAHlGIFLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QdvYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTI----------IGEGgasLSGGEKQRISIARA 483
Cdd:CHL00131 91 Q--YPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVgmdpsflsrnVNEG---FSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 484 MLKDADIIIFDEATANIDPeneDKLK---EAIETL-TKNKTVIMIAH--RLKTIRNADQILVLKDGEIVERGNHE--KLI 555
Cdd:CHL00131 166 ALLDSELAILDETDSGLDI---DALKiiaEGINKLmTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKEL 242
|
....
gi 1317668753 556 ENNG 559
Cdd:CHL00131 243 EKKG 246
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
336-549 |
1.31e-19 |
|
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: 87.34 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIkDYKIENLMNsismvfqd 415
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 vYLFED--------TIENNIKFGK-QNASHEEvvqAAKKARchEFIEALP-EGYDTIIGEggaSLSGGEKQRISIARAML 485
Cdd:cd03269 74 -YLPEErglypkmkVIDQLVYLAQlKGLKKEE---ARRRID--EWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 486 KDADIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
334-557 |
1.72e-19 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 88.35 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIEN--------- 404
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 405 ----LMNSISMVFQDVYLF-EDTIENNIKFGKQNAshEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRIS 479
Cdd:TIGR03005 81 hlrqMRNKIGMVFQSFNLFpHKTVLDNVTEAPVLV--LGMARAEAEKRAMELLDMV--GLADKADHMPAQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 480 IARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIE 556
Cdd:TIGR03005 157 IARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASehDLTMLLVTHEMGFAREfADRVCFFDKGRIVEQGKPDEIFR 236
|
.
gi 1317668753 557 N 557
Cdd:TIGR03005 237 Q 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
349-557 |
1.81e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLM----NSISMVFQDVYLFED-TI 423
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 424 ENNIKFGKQNA--SHEEVVQAAKKARCHEFIEALPEGYDTiigeggaSLSGGEKQRISIARAMLKDADIIIFDEATANID 501
Cdd:PRK10070 124 LDNTAFGMELAgiNAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 502 PENEDKLKEAIETL--TKNKTVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK10070 197 PLIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
334-547 |
3.90e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIgGKNIKdykienlmnsISMVF 413
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLF--EDTIENNIKFGKQNASHEEVVQaakkarcheFIEAL---PEGYDTIIGeggaSLSGGEKQRISIARAMLKDA 488
Cdd:COG0488 385 QHQEELdpDKTVLDELRDGAPGGTEQEVRG---------YLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 489 DIIIFDEATANIDPEnedkLKEAIETLTKN--KTVIMIAH-R--LKTIrnADQILVLKDGEIVE 547
Cdd:COG0488 452 NVLLLDEPTNHLDIE----TLEALEEALDDfpGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-544 |
4.82e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 83.65 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikdykienlmNSISMVF 413
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QdvylfedtiennikfgkqnasheevvqaakkarchefiealpegydtiigeggasLSGGEKQRISIARAMLKDADIIIF 493
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 494 DEATANIDPENEDKLKEAIETLtkNKTVIMIAHRLKTIRN-ADQILVLKDGE 544
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
343-557 |
5.04e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.95 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 343 YDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIK-------------DYKIENLMNSI 409
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLF------EDTIENNIK---FGKQNASHEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISI 480
Cdd:PRK10619 95 TMVFQHFNLWshmtvlENVMEAPIQvlgLSKQEARERAVKYLAKVGIDERAQGKYP-----------VHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 481 ARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
351-549 |
9.16e-19 |
|
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: 87.85 E-value: 9.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 351 NVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK---------NIKDYKienlmNSISMVFQDVYLFED 421
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiFLPPHR-----RRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 -TIENNIKFGKQNASheevvQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANI 500
Cdd:COG4148 92 lSVRGNLLYGRKRAP-----RAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 501 DpeneDKLKEAI----ETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:COG4148 165 D----LARKAEIlpylERLRDelDIPILYVSHSLDEVaRLADHVVLLEQGRVVASG 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
334-549 |
9.71e-19 |
|
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: 84.96 E-value: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI-KDYKIENLMNSIsmv 412
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEALRRIGAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 fqdvylfedtIENNIKFGKQNASHEEVVQAA----KKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:cd03268 78 ----------IEAPGFYPNLTARENLRLLARllgiRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
334-549 |
1.06e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVF 413
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYL-FEDTIENNIKFGKQ-NASHEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADII 491
Cdd:PRK09536 84 QDTSLsFEFDVRQVVEMGRTpHRSRFDTWTETDRAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLK-TIRNADQILVLKDGEIVERG 549
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
334-549 |
1.25e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD-DRPI----LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGG----KNIKDYKIEN 404
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 405 LMNSISMVFQ--DVYLFEDTIENNIKFGKQN--ASHEEVVQ-AAKKAR----CHEFIEALPegydtiigeggASLSGGEK 475
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgIPKEKAEKiAAEKLEmvglADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 476 QRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
348-545 |
1.66e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.87 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 348 ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDY----KIENLMNSISMVFQDVYLFED-- 421
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLLPDft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 TIEN---NIKFGKQNASheevvQAAKKARchEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATA 498
Cdd:PRK11629 104 ALENvamPLLIGKKKPA-----EINSRAL--EMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1317668753 499 NIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRNADQILVLKDGEI 545
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
334-556 |
1.67e-18 |
|
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: 88.71 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLI--ARFWDVNSGEIL-----------------IG- 393
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 394 -----GKNIKDYKIE----------NLMNSISMVFQDVY-LFED--TIENNIKfgkqnaSHEEVVQAAKKA--RCHEFIE 453
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDfwnlsdklrrRIRKRIAIMLQRTFaLYGDdtVLDNVLE------ALEEIGYEGKEAvgRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 454 ALPEGYDtiIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMI--AHRLKTI 531
Cdd:TIGR03269 155 MVQLSHR--ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWPEVI 232
|
250 260
....*....|....*....|....*.
gi 1317668753 532 RN-ADQILVLKDGEIVERGNHEKLIE 556
Cdd:TIGR03269 233 EDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
337-546 |
1.91e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSY----DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLM----NS 408
Cdd:PRK10535 8 KDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrrEH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQDVYLFED-TIENNIKFgkqNASHEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKD 487
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRNADQILVLKDGEIV 546
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
351-553 |
2.08e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 351 NVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDykIENLMN------SISMVFQDVYLFED-TI 423
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD--AEKGIClppekrRIGYVFQDARLFPHyKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 424 ENNIKFG--KQNASH-EEVVQAAKkarchefIEALPEGYDtiigeggASLSGGEKQRISIARAMLKDADIIIFDEATANI 500
Cdd:PRK11144 94 RGNLRYGmaKSMVAQfDKIVALLG-------IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 501 DPENEDKLKEAIETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEK 553
Cdd:PRK11144 160 DLPRKRELLPYLERLAReiNIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
338-548 |
4.12e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.37 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmnsiSMVFQDVY 417
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 418 LFE-DTIENNIKFGKQNASheeVVQAAKKARCHEFIEalpegydtIIGEGGA------SLSGGEKQRISIARAMLKDADI 490
Cdd:PRK11248 81 LLPwRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLK--------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAHRL-KTIRNADQILVLK--DGEIVER 548
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIeEAVFMATELVLLSpgPGRVVER 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
348-549 |
4.77e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 348 ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIArFWDVN----SGEILIGGKNIKDYKienlMNSISMVFQDVYLF--ED 421
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKE----MRAISAYVQQDDLFipTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 TIENNIKFGKQNASHEEVVQAAKKARCHEFIEA--LPEGYDTIIGEGGA--SLSGGEKQRISIARAMLKDADIIIFDEAT 497
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQAlgLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 498 ANIDPENEDKLKEAIETL-TKNKTVIMIAHR--LKTIRNADQILVLKDGEIVERG 549
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLaQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
334-545 |
5.29e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI-----KDYKienlmns 408
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlhaRDRK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQDVYLFED-TIENNIKFG-KQNASHEEVVQAAKKARCHEFIEA-----LPEGYDtiigeggASLSGGEKQRISIA 481
Cdd:PRK10851 76 VGFVFQHYALFRHmTVFDNIAFGlTVLPRRERPNAAAIKAKVTQLLEMvqlahLADRYP-------AQLSGGQKQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 482 RAMLKDADIIIFDEATANIDPENEDKLKEAIETL---TKNKTVIMIAHRLKTIRNADQILVLKDGEI 545
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
334-550 |
7.09e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.39 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENlmnsISmvf 413
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 qdvYLFED-------TIENNIKF-----GKQNAsheevvQAAKKARchEFIEA--LPEGYDTIIGEggasLSGGEKQRIS 479
Cdd:COG4152 75 ---YLPEErglypkmKVGEQLVYlarlkGLSKA------EAKRRAD--EWLERlgLGDRANKKVEE----LSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 480 IARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTI-RNADQILVLKDGEIVERGN 550
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-564 |
9.44e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.53 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 348 ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGgknikdykienlmNSISMVFQDVYLFEDTIENNI 427
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 428 KFGKQnashEEVVQAAKKARCHEfIEA----LPEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPE 503
Cdd:PTZ00243 742 LFFDE----EDAARLADAVRVSQ-LEAdlaqLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 504 -NEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHEKLIENNgLYSDL 564
Cdd:PTZ00243 817 vGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATL 877
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
336-572 |
1.01e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIgGKNIKdykienlmnsISMVFQD 415
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR----------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 VYLFED-TIENNIKfgkqnASHEEVVQAAKK------------------ARCHEFIEALpEGYD------TIIGEGG--- 467
Cdd:COG0488 70 PPLDDDlTVLDTVL-----DGDAELRALEAEleeleaklaepdedlerlAELQEEFEAL-GGWEaearaeEILSGLGfpe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 468 -------ASLSGGEKQRISIARAMLKDADIIIFDEATANIDpenedklKEAIETLTK-----NKTVIMIAH-R--LKTIr 532
Cdd:COG0488 144 edldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEEflknyPGTVLVVSHdRyfLDRV- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1317668753 533 nADQILVLKDGEIVE-RGNhekliennglYSDLINAKAKAE 572
Cdd:COG0488 216 -ATRILELDRGKLTLyPGN----------YSAYLEQRAERL 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
334-542 |
1.07e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.66 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSF-SYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikdykiENLMnsisMV 412
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-------EDLL----FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTIEnnikfgkqnasheEVVqaakkarchefieALPegYDTIigeggasLSGGEKQRISIARAMLKDADIII 492
Cdd:cd03223 70 PQRPYLPLGTLR-------------EQL-------------IYP--WDDV-------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 493 FDEATANIDPENEDKLKEAIET-LTknkTVIMIAHRLKTIRNADQILVLKD 542
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKElGI---TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
337-555 |
1.55e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDV 416
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLFED-TIENNIK---------FGKQNASHEEVVQAAKKArchefiealpEGYDTIIGEGGASLSGGEKQRISIARAMLK 486
Cdd:PRK10253 91 TTPGDiTVQELVArgryphqplFTRWRKEDEEAVTKAMQA----------TGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 487 DADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEKLI 555
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
334-554 |
1.58e-17 |
|
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: 81.65 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI-KDYKieNLMNSISMV 412
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPR--EVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTI--ENNIKFGK-QNASHEEvvqaaKKARCHEFIE--ALPEGYDTIIGeggaSLSGGEKQRISIARAMLKD 487
Cdd:cd03265 79 FQDLSVDDELTgwENLYIHARlYGVPGAE-----RRERIDELLDfvGLLEAADRLVK----TYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKL 554
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
342-557 |
2.68e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 81.77 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 342 SYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTF---CNLIArfwDVNSGEILIGGKNIK------------DYK-IENL 405
Cdd:COG4598 17 SFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFlrcINLLE---TPDSGEIRVGGEEIRlkpdrdgelvpaDRRqLQRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 406 MNSISMVFQDVYLFED-TIENNIKFGKQNasheevVQAAKKARCHEFIEALPEGydtiIGEGG------ASLSGGEKQRI 478
Cdd:COG4598 94 RTRLGMVFQSFNLWSHmTVLENVIEAPVH------VLGRPKAEAIERAEALLAK----VGLADkrdaypAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIE 556
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEgRTMLVVTHEMGFARDvSSHVVFLHQGRIEEQGPPAEVFG 243
|
.
gi 1317668753 557 N 557
Cdd:COG4598 244 N 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
334-551 |
2.80e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI---KDYKIENLMNSI 409
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SMVFQDVYLFED-TIENNIKFGK--QNASHEEV---VQAA-KKARCHEFIEALPegydtiigeggASLSGGEKQRISIAR 482
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLiiAGASGDDIrrrVSAAlDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 483 AMLKDADIIIFDEATANIDpeneDKLKEAIETLTK--NK---TVIMIAHRLKTI-RNADQILVLKDGEIVerGNH 551
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD----DALSEGILRLFEefNRvgvTVLMATHDIGLIsRRSYRMLTLSDGHLH--GGV 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
334-545 |
3.37e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKienlmNSISMVF 413
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-----EDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFE-DTIENNIKFGkqnasheevVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIII 492
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLG---------LKGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRL-KTIRNADQILVLKDGEI 545
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
334-501 |
3.87e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.97 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYD-DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDykIENLMNSISMV 412
Cdd:PRK11650 4 LKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFED-TIENNIKFGKQNA--SHEE----VVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAML 485
Cdd:PRK11650 82 FQNYALYPHmSVRENMAYGLKIRgmPKAEieerVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIV 150
|
170
....*....|....*.
gi 1317668753 486 KDADIIIFDEATANID 501
Cdd:PRK11650 151 REPAVFLFDEPLSNLD 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-547 |
4.07e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 84.46 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 8 IWNFSKEEQVNIKKSILAGFLHAVFNALEFGAIYYMLVNIFSKTLDYKAIFIclGILVISLVGKImtlkISQMAQTHAGY 87
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFA--GLLVLLLLSRL----ASQLLLTRLGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 88 FMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATS---SLSQAEMWVPMLLVLvlggvlntLVFVLGTLIF----NVKV 160
Cdd:COG4615 78 HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEdvrTISQAFVRLPELLQS--------VALVLGCLAYlawlSPPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 161 GLVAVA----GVIVFFIVTSMMEKKSsanaDKMTETQTRLTKEVLATLQGmqvIKSYNLGGENNRALRKS-IKDTSKILL 235
Cdd:COG4615 150 FLLTLVllglGVAGYRLLVRRARRHL----RRAREAEDRLFKHFRALLEG---FKELKLNRRRRRAFFDEdLQPTAERYR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 236 DLEKSVAPYTVIQrIVMGITTVF-----MVYVslkLNLSGELPLAE------TILMIMASFiifEGLIGA-----GSNMA 299
Cdd:COG4615 223 DLRIRADTIFALA-NNWGNLLFFaliglILFL---LPALGWADPAVlsgfvlVLLFLRGPL---SQLVGAlptlsRANVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 300 IlraceNAIDSVGfiDSMPDMREGSITEPIKN-----HDIVFKNVSFSY----DDRP-ILKNVSAEIKENTMTAIVGPSG 369
Cdd:COG4615 296 L-----RKIEELE--LALAAAEPAAADAAAPPapadfQTLELRGVTYRYpgedGDEGfTLGPIDLTIRRGELVFIVGGNG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 370 SGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDVYLFEDTIennikfGKQNASHEEVVQaakkarch 449
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLL------GLDGEADPARAR-------- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 450 EFIEALpeGYDTIIG-EGGA----SLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDK--------LKEaietlt 516
Cdd:COG4615 435 ELLERL--ELDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVfytellpeLKA------ 506
|
570 580 590
....*....|....*....|....*....|.
gi 1317668753 517 KNKTVIMIAHRLKTIRNADQILVLKDGEIVE 547
Cdd:COG4615 507 RGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
337-550 |
4.26e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDD-RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIkDYKIENLMN---SISMV 412
Cdd:PRK13636 9 EELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKlreSVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQ--DVYLFEDTIENNIKFGKQNAS------HEEVVQAAKKArchefiealpeGYDTIIGEGGASLSGGEKQRISIARAM 484
Cdd:PRK13636 88 FQdpDNQLFSASVYQDVSFGAVNLKlpedevRKRVDNALKRT-----------GIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 485 LKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIR-NADQILVLKDGEIVERGN 550
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
347-547 |
7.08e-17 |
|
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: 81.00 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 347 PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIEN---LMNSISMVFQDVYLF---E 420
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDSPSAvnpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 421 DTIENNIkfGKQNASHEEVVQAAKKARCHEFIEALpEGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANI 500
Cdd:TIGR02769 105 MTVRQII--GEPLRHLTSLDESEQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 501 DPENEdklKEAIETLTKNK-----TVIMIAHRLKTI-RNADQILVLKDGEIVE 547
Cdd:TIGR02769 182 DMVLQ---AVILELLRKLQqafgtAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-549 |
8.31e-17 |
|
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: 79.72 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNsISMVFQDVYLFE--DTIENN 426
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYDrlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 427 IKFG-----KQNASHEEVVQAAKKARCHEFIEalpegydtiigEGGASLSGGEKQRISIARAMLKDADIIIFDEATANID 501
Cdd:cd03266 100 EYFAglyglKGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1317668753 502 PENEDKLKEAIETLTK-NKTVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:cd03266 169 VMATRALREFIRQLRAlGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-557 |
8.50e-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: 83.58 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTF----CNLIArfwdvNSGEILIGGKNIKDYKIENLM---NSISMVFQDVY---- 417
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDPFgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 418 ---LFEDTIENNIKFGKQNASHEEVVQAAKKA------------RC-HEFiealpegydtiigeggaslSGGEKQRISIA 481
Cdd:COG4172 377 prmTVGQIIAEGLRVHGPGLSAAERRARVAEAleevgldpaarhRYpHEF-------------------SGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 482 RAMLKDADIIIFDEAT--------ANIdpenEDKLKEaietLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGN 550
Cdd:COG4172 438 RALILEPKLLVLDEPTsaldvsvqAQI----LDLLRD----LQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
....*..
gi 1317668753 551 HEKLIEN 557
Cdd:COG4172 510 TEQVFDA 516
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
334-547 |
1.01e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.48 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPI-LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTIennikfGKQNasheevvQAAKKARCHEFIEALPEGYDTIIGEGGAS---LSGGEKQRISIARAMLKDAD 489
Cdd:PRK10522 403 FTDFHLFDQLL------GPEG-------KPANPALVEKWLERLKMAHKLELEDGRISnlkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 490 IIIFDEATANIDP--------ENEDKLKEaietltKNKTVIMIAHRLKTIRNADQILVLKDGEIVE 547
Cdd:PRK10522 470 ILLLDEWAADQDPhfrrefyqVLLPLLQE------MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-560 |
1.05e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.44 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 341 FSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTT-FCNLiARFWDVNSGEILIGGKNIkDYKIENLM---NSISMVFQD- 415
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTlFMNL-SGLLRPQKGAVLWQGKPL-DYSKRGLLalrQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 -VYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTIigeggASLSGGEKQRISIARAMLKDADIIIFD 494
Cdd:PRK13638 87 eQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 495 EATANIDPENEDKLKEAIETLT-KNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGN------HEKLIENNGL 560
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGApgevfaCTEAMEQAGL 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
337-546 |
1.33e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK---NIKDYKIENLmnSISMVF 413
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcaRLTPAKAHQL--GIYLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFG--KQNASHEEVVQAAKKARCHEFIEALpegydtiigegGASLSGGEKQRISIARAMLKDADI 490
Cdd:PRK15439 93 QEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQLDLDSS-----------AGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 491 IIFDEATANIDP-ENEDKLKEAIETLTKNKTVIMIAHRLKTIRN-ADQILVLKDGEIV 546
Cdd:PRK15439 162 LILDEPTASLTPaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
351-567 |
1.87e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.26 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 351 NVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIK---DYKIENLmnSISMVFQDVYLFED--TIEN 425
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQIARM--GVVRTFQHVRLFREmtVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 426 NIKfgkqnASHEEV--------------VQAAKKA--RCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:PRK11300 101 LLV-----AQHQQLktglfsgllktpafRRAESEAldRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKlIENNglySDLIN 566
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE-IRNN---PDVIK 249
|
.
gi 1317668753 567 A 567
Cdd:PRK11300 250 A 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
313-556 |
3.17e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 313 FIDSMPDMREGSITEpIKNHDIVFKNVSFSY--DDRPILK---NVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNS 387
Cdd:TIGR03269 260 FMEGVSEVEKECEVE-VGEPIIKVRNVSKRYisVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 388 GEILIG-GKNIKDYKIENLMNS------ISMVFQ--DVYLFEDTIENNIK---------FGKQNASHEEVVQAAKKARCH 449
Cdd:TIGR03269 339 GEVNVRvGDEWVDMTKPGPDGRgrakryIGILHQeyDLYPHRTVLDNLTEaiglelpdeLARMKAVITLKMVGFDEEKAE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 450 EFIEALPEgydtiigeggaSLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHR 527
Cdd:TIGR03269 419 EILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHD 487
|
250 260 270
....*....|....*....|....*....|
gi 1317668753 528 LKTIRN-ADQILVLKDGEIVERGNHEKLIE 556
Cdd:TIGR03269 488 MDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
341-549 |
4.94e-16 |
|
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: 77.57 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 341 FSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGknikdyKIENLMNsISMVFQDvylfE 420
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLG-LGGGFNP----E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 421 DTIENNIKFGK--QNASHEEVvqAAKKARCHEFIEaLPEGYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATA 498
Cdd:cd03220 99 LTGRENIYLNGrlLGLSRKEI--DEKIDEIIEFSE-LGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 499 NIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
317-547 |
5.17e-16 |
|
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: 77.47 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 317 MPDMregsiTEPIknhdIVFKNVSFSYDDR----PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILI 392
Cdd:COG4181 1 MSSS-----SAPI----IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 393 GGKNIkdykieNLMN----------SISMVFQDVYLFED-TIENNIKFGKQNASHEEVVQAAKKA--------RCHefie 453
Cdd:COG4181 72 AGQDL------FALDedararlrarHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARALlervglghRLD---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 454 ALPegydtiigeggASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTI 531
Cdd:COG4181 142 HYP-----------AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALA 210
|
250
....*....|....*.
gi 1317668753 532 RNADQILVLKDGEIVE 547
Cdd:COG4181 211 ARCDRVLRLRAGRLVE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
338-557 |
1.59e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 79.34 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDR--PILKNVSAEIKENTMTAIVGPSGSGKT----TFCNLIARFWDVNSGEILIGGKNIKDYKiENLM----- 406
Cdd:COG4172 13 SVAFGQGGGtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS-ERELrrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 NSISMVFQD-------VYlfedTIennikfGKQNAS----HEEVVQAAKKARChefIEAL-------PEgydTIIGEGGA 468
Cdd:COG4172 92 NRIAMIFQEpmtslnpLH----TI------GKQIAEvlrlHRGLSGAAARARA---LELLervgipdPE---RRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 469 SLSGGEKQRISIARAMLKDADIIIFDEAT--------ANIdpenEDKLKEaietLTK--NKTVIMIAHRLKTIRN-ADQI 537
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTtaldvtvqAQI----LDLLKD----LQRelGMALLLITHDLGVVRRfADRV 227
|
250 260
....*....|....*....|
gi 1317668753 538 LVLKDGEIVERGNHEKLIEN 557
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAA 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
338-554 |
1.61e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPI--LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWD-----VNSGEILIGGKNIKDYKIENLMNS-- 408
Cdd:PRK10261 19 NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglVQCDKMLLRRRSRQVIELSEQSAAqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 -------ISMVFQD-------VYLFEDTIENNIKFgKQNASHEEVVQAAKkaRCHEFIEaLPEGyDTIIGEGGASLSGGE 474
Cdd:PRK10261 99 rhvrgadMAMIFQEpmtslnpVFTVGEQIAESIRL-HQGASREEAMVEAK--RMLDQVR-IPEA-QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 475 KQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKT--VIMIAHRLKTIRN-ADQILVLKDGEIVERGNH 551
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSV 253
|
...
gi 1317668753 552 EKL 554
Cdd:PRK10261 254 EQI 256
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
348-547 |
1.71e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.97 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 348 ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI----KDYKIENLMNSISMVFQDVYLFE--D 421
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQSFMLIPtlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 TIENN-----IKFGKQNASHEEVVQAAKKARCHEFIEALPegydtiigeggASLSGGEKQRISIARAMLKDADIIIFDEA 496
Cdd:PRK10584 105 ALENVelpalLRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 497 TANIDPENEDKLKEAIETLTKN--KTVIMIAHRLKTIRNADQILVLKDGEIVE 547
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
336-562 |
4.00e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLM-NSISMVFQ 414
Cdd:PRK11614 8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrEAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 415 DVYLFED-TIENNIKFGKQNASHEEVVQaakkaRCHEFIEALPEGYDTIIGEGGaSLSGGEKQRISIARAMLKDADIIIF 493
Cdd:PRK11614 88 GRRVFSRmTVEENLAMGGFFAERDQFQE-----RIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 494 DEATANIDPENEDKLKEAIETLTKNKTVIMIAHR--LKTIRNADQILVLKDGEIVERGNHEKLIENNGLYS 562
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDTGDALLANEAVRS 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-557 |
6.27e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.92 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 351 NVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMN---SISMVFQDVY--L-----FE 420
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPYasLnprmtVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 421 DTIENNIKFgkqnasHEEVVQAAKKARCHEFIEAL---PEGYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEAT 497
Cdd:COG4608 116 DIIAEPLRI------HGLASKAERRERVAELLELVglrPEHADRYPHE----FSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 498 --------ANI-----DPENEDKLkeaietltknkTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:COG4608 186 saldvsiqAQVlnlleDLQDELGL-----------TYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
334-556 |
8.35e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDyKIENLMNSISMVF 413
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 Q-DVYLFEDTI-ENNIKFGKQNASHEEVVQAAKKARChEFIEaLPEGYDTIIgeggASLSGGEKQRISIARAMLKDADII 491
Cdd:PRK13536 121 QfDNLDLEFTVrENLLVFGRYFGMSTREIEAVIPSLL-EFAR-LESKADARV----SDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 492 IFDEATANIDPENEDKLKEAIET-LTKNKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKLIE 556
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
334-549 |
1.18e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK--NIKDYKIENlMNSISM 411
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAA-QLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLF-EDTIENNIKFGKQNASHEEVVQAA--KKARCHEFIEALPEGYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:PRK09700 85 IYQELSVIdELTVLENLYIGRHLTKKVCGVNIIdwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGEIVERG 549
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
344-554 |
1.54e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.28 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 344 DDRPILKNVSAEIKENTMTAIVGPSGSGKTT----FCNLIArfwdvNSGEILIGGKNIKDYKIENLM---NSISMVFQDV 416
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLFED---TIENNIKFGKQnaSHEEVVQAAkkARCHEFIEALPE-GYDTIIGEG-GASLSGGEKQRISIARAMLKDADII 491
Cdd:PRK15134 372 NSSLNprlNVLQIIEEGLR--VHQPTLSAA--QREQQVIAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 492 IFDEATANIDPENEDKLKEAIETLTKNKTV--IMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKL 554
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
346-545 |
2.71e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.59 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 346 RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIkDYKIENLMNSISMVFQDVYLFED-TIE 424
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 425 NNIKFGKQnasheevVQAAKKARCHEFIEALPE--GYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDP 502
Cdd:TIGR01257 1022 EHILFYAQ-------LKGRSWEEAQLEMEAMLEdtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1317668753 503 ENEDKLKEAIETLTKNKTVIMIAHRLKTIRN-ADQILVLKDGEI 545
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
337-557 |
5.45e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKI-ENLMNSISMVFQD 415
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 VYLFED-TIENNIKFGKQnaSHEEVVQAAKKARCHEFIEALPEGY--DTIigegGASLSGGEKQRISIARAMLKDADIII 492
Cdd:PRK10895 87 ASIFRRlSVYDNLMAVLQ--IRDDLSAEQREDRANELMEEFHIEHlrDSM----GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTKNKTVIMIA-HRLK-TIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVReTLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
349-542 |
6.08e-14 |
|
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: 71.34 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMnsismVFQDVYLFE-DTIENNI 427
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 428 KFGKQNASHEeVVQAAKKARCHEFIE--ALPEGYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATANIDPENE 505
Cdd:TIGR01184 76 ALAVDRVLPD-LSKSERRAIVEEHIAlvGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1317668753 506 DKLKEAIETLTKNK--TVIMIAHrlktirNADQILVLKD 542
Cdd:TIGR01184 151 GNLQEELMQIWEEHrvTVLMVTH------DVDEALLLSD 183
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
349-538 |
9.48e-14 |
|
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: 69.66 E-value: 9.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIarfwdvnsgeiliggknIKDYKIENLMNSISMVFQDVYLFEDTIENNIK 428
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPKFSRNKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 429 FGKqnasheevvqaakkarchefiealpeGYDTIiGEGGASLSGGEKQRISIARAMLKDAD--IIIFDEATANIDPENED 506
Cdd:cd03238 74 VGL--------------------------GYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|...
gi 1317668753 507 KLKEAIETLTKNK-TVIMIAHRLKTIRNADQIL 538
Cdd:cd03238 127 QLLEVIKGLIDLGnTVILIEHNLDVLSSADWII 159
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
334-556 |
1.13e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNsISMVF 413
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED--TIENNIKFGKqnasHEEVVQAAKKARCHEFIE--ALPEGYDTIIGEggasLSGGEKQRISIARAMLKDAD 489
Cdd:PRK13537 87 QFDNLDPDftVRENLLVFGR----YFGLSAAAARALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKLIE 556
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
337-557 |
1.48e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.44 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKienlMNS-----ISM 411
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----MHKrarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 VFQDVYLFED-TIENNIKfgkqnASHE--EVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:COG1137 83 LPQEASIFRKlTVEDNIL-----AVLElrKLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIA-HRLK-TIRNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNVReTLGICDRAYIISEGKVLAEGTPEEILNN 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
334-549 |
1.84e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIarfwdvnSGeiLIGGKNIKDYKIENLMNSIS--- 410
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SG--LITGDKSAGSHIELLGRTVQreg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 --------------MVFQDVYLFED-TIENNIKFGKQNASH--EEVVQAAKKARCHEFIEALPE-GYDTIIGEGGASLSG 472
Cdd:PRK09984 76 rlardirksrantgYIFQQFNLVNRlSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 473 GEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLK-TIRNADQILVLKDGEIVERG 549
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-545 |
2.02e-13 |
|
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: 68.61 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNS-ISMVFQD---VYLFED-TI 423
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDrkrEGLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 424 ENNIkfgkqnasheevvqaakkarchefieALPegydtiigeggASLSGGEKQRISIARAMLKDADIIIFDEATANIDPE 503
Cdd:cd03215 96 AENI--------------------------ALS-----------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1317668753 504 NedklKEAI-----ETLTKNKTVIMIAHRLKTI-RNADQILVLKDGEI 545
Cdd:cd03215 139 A----KAEIyrlirELADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
355-544 |
2.63e-13 |
|
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: 69.74 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 355 EIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKdYKIENLMNSISMVFQDvYLFEDTIEnnikFGKQNA 434
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRD-LLSSITKD----FYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 435 SHEEVVQAAKkarchefIEALpegYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIE- 513
Cdd:cd03237 95 FKTEIAKPLQ-------IEQI---LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRr 160
|
170 180 190
....*....|....*....|....*....|...
gi 1317668753 514 -TLTKNKTVIMIAHRLKTIRN-ADQILVLkDGE 544
Cdd:cd03237 161 fAENNEKTAFVVEHDIIMIDYlADRLIVF-EGE 192
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
322-543 |
2.79e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 322 EGSITEPIKNHDIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNS--GEILIGGKNIKd 399
Cdd:PLN03211 57 KGSNIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 400 ykiENLMNSISMVFQDVYLFED-TIENNIKF----------GKQNASH--EEVVQAAKKARCHefiealpegyDTIIGEG 466
Cdd:PLN03211 136 ---KQILKRTGFVTQDDILYPHlTVRETLVFcsllrlpkslTKQEKILvaESVISELGLTKCE----------NTIIGNS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 467 GA-SLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLT-KNKTVIMIAHR--LKTIRNADQILVLKD 542
Cdd:PLN03211 203 FIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQpsSRVYQMFDSVLVLSE 282
|
.
gi 1317668753 543 G 543
Cdd:PLN03211 283 G 283
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
336-547 |
2.92e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK-----NIKDykieNLMNSIS 410
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTTA----ALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLF-EDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYDTiiGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:PRK11288 83 IIYQELHLVpEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDP--DTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTI-RNADQILVLKDGEIVE 547
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
349-550 |
5.07e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIK--DYKIENlmNSISMVFQDV---------- 416
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRS--QRIRMIFQDPstslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 -YLFEDTIENNIKFGKQnASHEEVVQAAKKarchefIEALPEG---YDTIigeggasLSGGEKQRISIARAMLKDADIII 492
Cdd:PRK15112 107 sQILDFPLRLNTDLEPE-QREKQIIETLRQ------VGLLPDHasyYPHM-------LAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 493 FDEATANIDPENEDKLKEAIETLTKNKTV--IMIAHRLKTIRN-ADQILVLKDGEIVERGN 550
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
334-569 |
8.75e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY----------------------DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEIL 391
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 392 IGGknikdyKIENLMnSISMVFQDvylfEDTIENNIKFgkqNA-----SHEEVvqAAKKARCHEFIEaLPEGYDTIIGeg 466
Cdd:COG1134 85 VNG------RVSALL-ELGAGFHP----ELTGRENIYL---NGrllglSRKEI--DEKFDEIVEFAE-LGDFIDQPVK-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 467 gaSLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRN-ADQILVLKDGE 544
Cdd:COG1134 146 --TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGR 223
|
250 260
....*....|....*....|....*
gi 1317668753 545 IVERGNHEKLIEnngLYSDLINAKA 569
Cdd:COG1134 224 LVMDGDPEEVIA---AYEALLAGRE 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
334-546 |
1.02e-12 |
|
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: 67.29 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSF----SYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN---SGEILIGGKNIKD----YKI 402
Cdd:cd03233 4 LSWRNISFttgkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfaekYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 403 ENLMNSIsmvfQDVYLFEDTIENNIKFgkqnasheevvqaAKKARCHEFIEALpegydtiigeggaslSGGEKQRISIAR 482
Cdd:cd03233 84 EIIYVSE----EDVHFPTLTVRETLDF-------------ALRCKGNEFVRGI---------------SGGERKRVSIAE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 483 AMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHR--LKTIRNADQILVLKDGEIV 546
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
315-501 |
1.13e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 315 DSMPDMREGSITEPIKNHDIVF-KNVSF----SYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWD---VN 386
Cdd:TIGR00956 740 DESDDVNDEKDMEKESGEDIFHwRNLTYevkiKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvIT 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 387 SGEILIGGKNIKdykiENLMNSISMVFQ-DVYLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFIEALP-EGY-DTII 463
Cdd:TIGR00956 820 GGDRLVNGRPLD----SSFQRSIGYVQQqDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEmESYaDAVV 895
|
170 180 190
....*....|....*....|....*....|....*....
gi 1317668753 464 GEGGASLSGGEKQRISIARAMLKDADIIIF-DEATANID 501
Cdd:TIGR00956 896 GVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLD 934
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
337-526 |
1.88e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMnsismvfqdV 416
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC---------H 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLF-------EDTIENNIKFGKQ-NASHEEVVQAAKKARCHEFIEALPEGYdtiigeggasLSGGEKQRISIARAMLKDA 488
Cdd:PRK13539 77 YLGhrnamkpALTVAENLEFWAAfLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNR 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIET-LTKNKTVIMIAH 526
Cdd:PRK13539 147 PIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATH 185
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
349-550 |
2.87e-12 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 67.25 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCN----------LIARFWDVNSGEILIGGKNIkDYKIE--------------- 403
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrLHLKKEQPGNHDRIEGLEHI-DKVIVidqspigrtprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 404 ---NLMNSISMVFQDV-----YLfEDTIEnnIKF-GKQNAsheEVVQ-AAKKArcHEFIEALPE-------------GYD 460
Cdd:cd03271 90 tytGVFDEIRELFCEVckgkrYN-RETLE--VRYkGKSIA---DVLDmTVEEA--LEFFENIPKiarklqtlcdvglGYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 461 TIiGEGGASLSGGEKQRISIARAMLKDAD---IIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRNADQ 536
Cdd:cd03271 162 KL-GQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCADW 240
|
250 260
....*....|....*....|
gi 1317668753 537 ILVL------KDGEIVERGN 550
Cdd:cd03271 241 IIDLgpeggdGGGQVVASGT 260
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
337-526 |
3.48e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.46 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDV 416
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLFEDTIENNIKF------GKQNASHEEVVQAAKKARCHefieaLPegydtiigegGASLSGGEKQRISIARAMLKDADI 490
Cdd:TIGR01189 84 LKPELSALENLHFwaaihgGAQRTIEDALAAVGLTGFED-----LP----------AAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIET-LTKNKTVIMIAH 526
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-557 |
3.70e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDY---KIENLMNSISMVFQDVY-------- 417
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNPYgslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 418 ---LFEDTIENNIKFGKqnasheevvqAAKKARCHEFIEAL---PEGYDTIigegGASLSGGEKQRISIARAMLKDADII 491
Cdd:PRK11308 111 vgqILEEPLLINTSLSA----------AERREKALAMMAKVglrPEHYDRY----PHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 492 IFDEATANIDPENEDK-------LKEAIETltknkTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK11308 177 VADEPVSALDVSVQAQvlnlmmdLQQELGL-----SYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
334-526 |
4.94e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVF--KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKnikdykienlmnsism 411
Cdd:PRK11147 318 IVFemENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK---------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 vfQDVYLF---------EDTIENNIKFGKQNasheevVQAAKKARcHefieALpeGY--DTIIGEGGA-----SLSGGEK 475
Cdd:PRK11147 382 --LEVAYFdqhraeldpEKTVMDNLAEGKQE------VMVNGRPR-H----VL--GYlqDFLFHPKRAmtpvkALSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 476 QRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTknKTVIMIAH 526
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ--GTVLLVSH 495
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
57-276 |
4.97e-12 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 66.81 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 57 IFICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLL 136
Cdd:cd07346 39 LWIALLLLLLALLRALLSY-LRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 137 VLVLGGVLnTLVFVLGTLIF-NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYNL 215
Cdd:cd07346 118 LQLLSDVL-TLIGALVILFYlNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 216 GGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAE 276
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE 257
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
331-560 |
5.01e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 331 NHDIVF--KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNS 408
Cdd:PRK10575 7 HSDTTFalRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQDVYLFED-TIENNIKFGK----------QNASHEEVVQAAKKARCHEFIEALPEgydtiigeggaSLSGGEKQR 477
Cdd:PRK10575 87 VAYLPQQLPAAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 478 ISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLK-TIRNADQILVLKDGEIVERGNHEKL 554
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEL 235
|
....*.
gi 1317668753 555 IENNGL 560
Cdd:PRK10575 236 MRGETL 241
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
337-559 |
6.99e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.58 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIA--RFWDVNSGEILIGGKNIKDYKIENLM-NSISMVF 413
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QdvYLFEDTIENNiKFGKQNAsheevVQAAKKARCHE---------FIEA------LPEgyDTIIGEGGASLSGGEKQRI 478
Cdd:PRK09580 85 Q--YPVEIPGVSN-QFFLQTA-----LNAVRSYRGQEpldrfdfqdLMEEkiallkMPE--DLLTRSVNVGFSGGEKKRN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAH--RLKTIRNADQILVLKDGEIVERGNHE--K 553
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvK 234
|
....*.
gi 1317668753 554 LIENNG 559
Cdd:PRK09580 235 QLEEQG 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
347-543 |
9.22e-12 |
|
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: 65.15 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 347 PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILI---GGK----NIKDYKIENLM-NSISMVFQ---- 414
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvdlaQASPREILALRrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 415 -------DVY---LFEdtiennikfgkQNASHEEvvqAAKKARchEFIEAL--PEgydtiigeggaSL--------SGGE 474
Cdd:COG4778 105 iprvsalDVVaepLLE-----------RGVDREE---ARARAR--ELLARLnlPE-----------RLwdlppatfSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 475 KQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKT-VIMIAHRLKTI-RNADQILVLKDG 543
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVReAVADRVVDVTPF 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-557 |
1.17e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI---KDYKIENLMNSISMVFQDVYLFED---T 422
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 423 IENNIKfgKQNASHEEVVQAAKKARCHEFIEA---LPEGYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATAN 499
Cdd:PRK10261 420 VGDSIM--EPLRVHGLLPGKAAAARVAWLLERvglLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 500 IDPENEDKLKEAIETLTKNKTV--IMIAHRLKTI-RNADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
348-547 |
1.66e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.09 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 348 ILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIEN---LMNSISMVFQDvylfedtie 424
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQD--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 425 nniKFGKQNASHE--EVV-----------QAAKKARCHEFIEA--LPegyDTIIGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:PRK10419 98 ---SISAVNPRKTvrEIIreplrhllsldKAERLARASEMLRAvdLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 490 IIIFDEATANIDPENEdklKEAIETLTK-----NKTVIMIAHRLKTI-RNADQILVLKDGEIVE 547
Cdd:PRK10419 172 LLILDEAVSNLDLVLQ---AGVIRLLKKlqqqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
337-546 |
1.78e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK--NIKDYKiENLMNSISMVFQ 414
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSK-EALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 415 DVYLF-EDTIENNIKFGKQN-----ASHEEVVQAAKKARCHEFIEALPEgydtiigEGGASLSGGEKQRISIARAMLKDA 488
Cdd:PRK10982 81 ELNLVlQRSVMDNMWLGRYPtkgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKNKT-VIMIAHRLKTIRN-ADQILVLKDGEIV 546
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
334-552 |
7.94e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSY-DDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV 412
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFEDTIENNIKFGKQnaSHEEVVQAAKkARCHEFIEALPEGYDTI------IGEggasLSGGEKQRISIARAMLK 486
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMGRY--GHMGWLRRAK-KRDRQIVTAALARVDMVefrhrqIGE----LSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 487 DADIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRNADQILVLKDGEIVERGNHE 552
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
352-560 |
8.35e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 352 VSAEIKENTMTAIVGPSGSGKTTfcnLIARFWDV--NSGEILIGGKNIKDYKIENL-----------MNSISM-VFQdvY 417
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELarhraylsqqqTPPFAMpVFQ--Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 418 LfedtiennikfgkQNASHEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLK-------DADI 490
Cdd:PRK03695 90 L-------------TLHQPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRL-KTIRNADQILVLKDGEIVERGNHEKLIENNGL 560
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
352-557 |
8.58e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 8.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 352 VSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI---KDYKIENLMNSISMVFQDV-------YLFED 421
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPlaslnprMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 TIENNIKFGKQNASHEEVVQAAKKARC-------------HEFiealpegydtiigeggaslSGGEKQRISIARAMLKDA 488
Cdd:PRK15079 120 IIAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinrypHEF-------------------SGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIEN 557
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
331-543 |
9.32e-11 |
|
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: 61.11 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 331 NHDIVFKNVSFSYD----DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIA--RFWDVNSGEILIGGKNIKdykiEN 404
Cdd:cd03232 1 GSVLTWKNLNYTVPvkggKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD----KN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 405 LMNSISMVFQ-DVYLFEDTIENNIKFgkqnasheevvqaakkarchefiEALPEGydtiigeggasLSGGEKQRISIARA 483
Cdd:cd03232 77 FQRSTGYVEQqDVHSPNLTVREALRF-----------------------SALLRG-----------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 484 MLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHR--LKTIRNADQILVLKDG 543
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
334-540 |
2.61e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEIliggknIKDYKIEnlmnsISMVF 413
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLR-----IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYL---FEDTIENNIKFgKQNASHEEVVQAAKKARCHEFIEALPEgydtiigeggaSLSGGEKQRISIARAMLKDADI 490
Cdd:PRK09544 74 QKLYLdttLPLTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIR-NADQILVL 540
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
337-544 |
2.66e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNS--GEILIGGKNIKDYKI-ENLMNSISMVF 413
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIrDTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QDVYLFED-TIENNIKFGKQNASHEEVVQAAKKARCHEFIEALPEGYD--TIIGEggasLSGGEKQRISIARAMLKDADI 490
Cdd:PRK13549 89 QELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGN----LGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 491 IIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRN-ADQILVLKDGE 544
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLkAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-544 |
2.91e-10 |
|
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: 62.88 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 355 EIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEIligGKNIK-DYK------------IENLMNSISMVFQDVYLFED 421
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKiSYKpqyispdydgtvEEFLRSANTDDFGSSYYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 TIEnniKFGkqnasheevvqaakkarchefIEALpegYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATANID 501
Cdd:COG1245 439 IIK---PLG---------------------LEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1317668753 502 PENEDKLKEAIETLTKN--KTVIMIAHRLKTIRN-ADQILVLkDGE 544
Cdd:COG1245 488 VEQRLAVAKAIRRFAENrgKTAMVVDHDIYLIDYiSDRLMVF-EGE 532
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
345-554 |
3.64e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.87 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 345 DRPILKNVSAEIKENTMTAIVGPSGSGKTTFCnliARFWDV-------NSGEILIGGKNI-----KDYKIENLMNSISMV 412
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTC---AAALGIlpagvrqTAGRVLLDGKPVapcalRGRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYlfedTIennikfgkqnASH--EEVVQAAKKARCHEFIEALP----EGYDTIIGEGGASLSGGEKQRISIARAMLK 486
Cdd:PRK10418 92 FNPLH----TM----------HTHarETCLALGKPADDATLTAALEavglENAARVLKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 487 DADIIIFDEATANIDPENEDKLKEAIETLTKNKT--VIMIAHRLKTI-RNADQILVLKDGEIVERGNHEKL 554
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
343-549 |
4.40e-10 |
|
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: 60.04 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 343 YDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNsISMVF-QDVYLFED 421
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 tiennIKFGKQNASHEEVVQ---AAKKARCHEFIEALPEGydTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATA 498
Cdd:cd03267 110 -----LPVIDSFYLLAAIYDlppARFKKRLDELSELLDLE--ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 499 NIDPENEDKLKEAIETLTKNK--TVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
356-528 |
4.61e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 356 IKENTMTAIVGPSGSGKTTFCNLIarfwdvnSGEILIG-GKNIKDYKIENLMNSIS-MVFQDvYlFEDTIENNIKfgkqn 433
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNlGDYEEEPSWDEVLKRFRgTELQN-Y-FKKLYNGEIK----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 434 ASH-----------------EEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEA 496
Cdd:PRK13409 162 VVHkpqyvdlipkvfkgkvrELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 1317668753 497 TANIDPENEDKLKEAIETLTKNKTVIMIAHRL 528
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
329-554 |
4.76e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 329 IKNHDIVFKNVSfsyDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVN-----SGEILIGGKNIKDYKIE 403
Cdd:PRK15134 8 IENLSVAFRQQQ---TVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 404 NLM----NSISMVFQD--VYLFE-DTIENNI-------KFGKQNASHEEVV---------QAAKkaRCHEFiealPEgyd 460
Cdd:PRK15134 85 TLRgvrgNKIAMIFQEpmVSLNPlHTLEKQLyevlslhRGMRREAARGEILncldrvgirQAAK--RLTDY----PH--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 461 tiigeggaSLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDK----LKEAIETLtkNKTVIMIAHRLKTIRN-AD 535
Cdd:PRK15134 156 --------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQilqlLRELQQEL--NMGLLFITHNLSIVRKlAD 225
|
250
....*....|....*....
gi 1317668753 536 QILVLKDGEIVERGNHEKL 554
Cdd:PRK15134 226 RVAVMQNGRCVEQNRAATL 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
355-544 |
5.93e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 355 EIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILiggKNIK-DYKIENLMNSISMVfqdVYLFEDTIENNIkfgkqN 433
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELKiSYKPQYIKPDYDGT---VEDLLRSITDDL-----G 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 434 ASHEEvvqaakkarcHEFIE--ALPEGYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEA 511
Cdd:PRK13409 430 SSYYK----------SEIIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 1317668753 512 IETLTKN--KTVIMIAHRLKTIRN-ADQILVLkDGE 544
Cdd:PRK13409 496 IRRIAEEreATALVVDHDIYMIDYiSDRLMVF-EGE 530
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
338-527 |
7.53e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIAR---------FWDVNSGEI--------LIGGKNIKDY 400
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalkgtpvagCVDVPDNQFgreaslidAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 401 KIEnLMNSISMVfqDVYLFedtiennikfgkqnasheevvqaakKARCHEfiealpegydtiigeggasLSGGEKQRISI 480
Cdd:COG2401 115 AVE-LLNAVGLS--DAVLW-------------------------LRRFKE-------------------LSTGQKFRFRL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1317668753 481 ARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHR 527
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
346-546 |
8.92e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 346 RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGK--NIKDYK--IENLMnsismvfqdVYLFED 421
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRdaIRAGI---------AYVPED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 ----------TIENNI---------KFGkqnasheeVVQAAK-KARCHEFIEAL---PEGYDTIIGeggaSLSGGEKQRI 478
Cdd:COG1129 336 rkgeglvldlSIRENItlasldrlsRGG--------LLDRRReRALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTI-RNADQILVLKDGEIV 546
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELlGLSDRILVMREGRIV 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
337-546 |
1.29e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARF-----WDvnsGEILIGGKNIKDYKI-ENLMNSIS 410
Cdd:TIGR02633 5 KGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtWD---GEIYWSGSPLKASNIrDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 411 MVFQDVYLFED-TIENNIKFGKQNASHEEVVQ-AAKKARCHEFIEALPEGYDTIIGEGGaSLSGGEKQRISIARAMLKDA 488
Cdd:TIGR02633 82 IIHQELTLVPElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRN-ADQILVLKDGEIV 546
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
449-555 |
4.36e-09 |
|
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: 59.64 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 449 HEFIEALPE-------------GYDTIiGEGGASLSGGEKQRISIARAMLKDAD---IIIFDEATANIDPENEDKLKEAI 512
Cdd:TIGR00630 797 YEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVL 875
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1317668753 513 ETLTKN-KTVIMIAHRLKTIRNADQILVL------KDGEIVERGNHEKLI 555
Cdd:TIGR00630 876 QRLVDKgNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEVA 925
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
22-289 |
4.86e-09 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 57.82 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 22 SILAGFLHAVFNALEFGAIYYMLVNIFSKTLDYKAIFICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKI 101
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASY-LQTYLMAYVGQRVVRDLRNDLFDKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 102 KRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLLVLVLGGVLnTLVFVLGTLIF-NVKVGLVAVAGVIVFFIVTSMMEK 180
Cdd:cd18552 83 LRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPL-TVIGLLGVLFYlDWKLTLIALVVLPLAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 181 KSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMV 260
Cdd:cd18552 162 RLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVL 241
|
250 260
....*....|....*....|....*....
gi 1317668753 261 YVSLKLNLSGELPLAETILMIMASFIIFE 289
Cdd:cd18552 242 WYGGYQVISGELTPGEFISFITALLLLYQ 270
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-544 |
4.97e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 362 TAIVGPSGSGKTTFCNLIARFWDVNSGE-ILIGGKNIKDYKIENLMNsismvfqdvylfedtiennikfgkqnasheevv 440
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL--------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 441 qaakkarchefiealpegydTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLT---- 516
Cdd:smart00382 52 --------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllll 111
|
170 180 190
....*....|....*....|....*....|....*..
gi 1317668753 517 ---KNKTVIMIAHRLK------TIRNADQILVLKDGE 544
Cdd:smart00382 112 kseKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
337-526 |
5.04e-09 |
|
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: 56.35 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMVFQDV 416
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLFEDTIENNIKFGKQNASHEEVVQAAKKARCHEFiEALPEGYdtiigeggasLSGGEKQRISIARAMLKDADIIIFDEA 496
Cdd:cd03231 84 IKTTLSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 1317668753 497 TANIDPENEDKLKEAIET-LTKNKTVIMIAH 526
Cdd:cd03231 153 TTALDKAGVARFAEAMAGhCARGGMVVLTTH 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-528 |
6.68e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 357 KENTMTAIVGPSGSGKTTFCN-----LIARFWDVNSG----EIL--IGGKNIKDYkienlmnsismvFQDVYlfedtiEN 425
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEpswdEVLkrFRGTELQDY------------FKKLA------NG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 426 NIKfgkqnASHE-------------EVVQAAKKA----RCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:COG1245 159 EIK-----VAHKpqyvdlipkvfkgTVRELLEKVdergKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIAHRL 528
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDL 272
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
22-288 |
9.95e-09 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 56.50 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 22 SILAGFLHAVFNALeFGAIYyMLVNIFSKTLDYKAIFICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKI 101
Cdd:pfam00664 8 AILSGAISPAFPLV-LGRIL-DVLLPDGDPETQALNVYSLALLLLGLAQFILSF-LQSYLLNHTGERLSRRLRRKLFKKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 102 KRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLLVLVLGGVLNTLVFVLGTLIFNVKVGLVAVAGVIVFFIVTSMMEKK 181
Cdd:pfam00664 85 LRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 182 SSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMVY 261
Cdd:pfam00664 165 LRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALW 244
|
250 260
....*....|....*....|....*..
gi 1317668753 262 VSLKLNLSGELPLAETILMIMASFIIF 288
Cdd:pfam00664 245 FGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
334-513 |
1.01e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIgGKNIK----DYKIENLMNSI 409
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayvDQSRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 SmVFQDVYLFEDTiennIKFGKqnasheevVQAAKKARCHEFIEalpEGYD--TIIGEggasLSGGEKQRISIARAMLKD 487
Cdd:TIGR03719 402 T-VWEEISGGLDI----IKLGK--------REIPSRAYVGRFNF---KGSDqqKKVGQ----LSGGERNRVHLAKTLKSG 461
|
170 180
....*....|....*....|....*.
gi 1317668753 488 ADIIIFDEATANIDPENEDKLKEAIE 513
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
334-536 |
1.20e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIarfwdvnSGE---------ILIG-----GKNIKD 399
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGDhpqgysndlTLFGrrrgsGETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 400 YK--IENLMNSISMVFQ------DVYL--FEDTIennikfGKQNAsheevVQAAKKARCHEFIEALpeGYDTIIGEGG-A 468
Cdd:PRK10938 334 IKkhIGYVSSSLHLDYRvstsvrNVILsgFFDSI------GIYQA-----VSDRQQKLAQQWLDIL--GIDKRTADAPfH 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 469 SLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIM------------IAHRLKTIRNAD 535
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFVPDGD 480
|
.
gi 1317668753 536 Q 536
Cdd:PRK10938 481 I 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
349-547 |
1.29e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNS--GEILIGG-----KNIKDYkiENLmnSISMVFQDVYLF-E 420
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRDS--EAL--GIVIIHQELALIpY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 421 DTIENNIKFGKQNASH-----EEVVQAAKK--ARChefieALPEGYDTIIGEGGAslsgGEKQRISIARAMLKDADIIIF 493
Cdd:NF040905 93 LSIAENIFLGNERAKRgvidwNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 494 DEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVE 547
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
364-550 |
2.07e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 364 IVGPSGSGK--TTFC--NLIARFWDVnSGEILIGGKNIKDYKiENLMN-----SISMVFQD--------VYLFEDTIENN 426
Cdd:PRK09473 47 IVGESGSGKsqTAFAlmGLLAANGRI-GGSATFNGREILNLP-EKELNklraeQISMIFQDpmtslnpyMRVGEQLMEVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 427 I---KFGKQNASHEEV--------VQAAKKARC--HEFiealpegydtiigeggaslSGGEKQRISIARAMLKDADIIIF 493
Cdd:PRK09473 125 MlhkGMSKAEAFEESVrmldavkmPEARKRMKMypHEF-------------------SGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 494 DEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGN 550
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
345-570 |
2.76e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 345 DRPILKNVS------AEIkentmtAIVGPSGSGKTTFCNLIARFWDVNSGEILIGgkniKDYKI---------------- 402
Cdd:TIGR03719 17 KKEILKDISlsffpgAKI------GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIKVgylpqepqldptktvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 403 ENLMNSISMVFQDVYLFEdtiENNIKFGKQNASHEEVvqAAKKARCHEFIEA------------------LPEGyDTIIg 464
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFN---EISAKYAEPDADFDKL--AAEQAELQEIIDAadawdldsqleiamdalrCPPW-DADV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 465 eggASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTknKTVIMIAHRLKTIRNADQ-ILVLKDG 543
Cdd:TIGR03719 160 ---TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAVTHDRYFLDNVAGwILELDRG 234
|
250 260
....*....|....*....|....*...
gi 1317668753 544 E-IVERGNhekliennglYSDLINAKAK 570
Cdd:TIGR03719 235 RgIPWEGN----------YSSWLEQKQK 252
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
349-549 |
3.38e-08 |
|
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: 54.57 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTT--FCNLIA----RFWDVNSGEI--LIGGKNIKDY-KIENLMNSISmvfqdvylf 419
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlaFDTIYAegqrRYVESLSAYArqFLGQMDKPDVdSIEGLSPAIA--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 420 edtIENniKFGKQN-----ASHEEV--------VQAAKKARChEFIEALPEGYDTIIGEGGaSLSGGEKQRISIARAMLK 486
Cdd:cd03270 82 ---IDQ--KTTSRNprstvGTVTEIydylrllfARVGIRERL-GFLVDVGLGYLTLSRSAP-TLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 487 DAD--IIIFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRNADQILVL------KDGEIVERG 549
Cdd:cd03270 155 GLTgvLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
331-547 |
5.21e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 331 NHDIVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYK----IENLM 406
Cdd:PRK09700 261 AHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldaVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 407 NSISMVFQDVYLFED-------TIENNIKFGKQNAS-----HEEVVQAAKKAR------CHEFIEALPEgydtiigegga 468
Cdd:PRK09700 341 AYITESRRDNGFFPNfsiaqnmAISRSLKDGGYKGAmglfhEVDEQRTAENQRellalkCHSVNQNITE----------- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 469 sLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRNA-DQILVLKDGEIV 546
Cdd:PRK09700 410 -LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
.
gi 1317668753 547 E 547
Cdd:PRK09700 489 Q 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-556 |
6.07e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 363 AIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNI-----KDYKienlMNSISMVFQDVYLF-EDTIENNIKFGKQNASH 436
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQ----EAGIGIIHQELNLIpQLTIAENIFLGREFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 437 ------EEVVQAAKK--ARCHefieaLPEGYDTIIGEggasLSGGEKQRISIARAMLKDADIIIFDEAT-ANIDPENEDK 507
Cdd:PRK10762 110 fgridwKKMYAEADKllARLN-----LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317668753 508 LKEAIETLTKNKTVIMIAHRLKTIRN-ADQILVLKDGE-IVERG----NHEKLIE 556
Cdd:PRK10762 181 FRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAEREvadlTEDSLIE 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
339-503 |
6.65e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 339 VSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSISMV---FQD 415
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLpglKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 VylfeDTIENnIKFgkQNASHeevvqaAKKARchefieALPEGYDTIIGEGGAS------LSGGEKQRISIARAMLKDAD 489
Cdd:PRK13543 97 L----STLEN-LHF--LCGLH------GRRAK------QMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAP 157
|
170
....*....|....
gi 1317668753 490 IIIFDEATANIDPE 503
Cdd:PRK13543 158 LWLLDEPYANLDLE 171
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
470-541 |
9.91e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 9.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317668753 470 LSGGEKQRISIARAM----LKDADIIIFDEATANIDPENEDKLKEAI-ETLTKNKTVIMIAHRLKTIRNADQILVLK 541
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
336-541 |
1.03e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 336 FKNVSFSYDDRPILkNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKD-------YKIENLMNS 408
Cdd:PRK13541 4 LHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiakpyctYIGHNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMvfqdvylfedTIENNIKFGKQNASHEEVVQAAkkarCHEFiealpeGYDTIIGEGGASLSGGEKQRISIARAMLKDA 488
Cdd:PRK13541 83 LEM----------TVFENLKFWSEIYNSAETLYAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 489 DIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQILVLK 541
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSAQILQLD 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
469-544 |
1.22e-07 |
|
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: 51.80 E-value: 1.22e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 469 SLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN--KTVIMIAHRLKTIRNADQILVLKDGE 544
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
334-560 |
1.23e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEIliggknikdyK-IENlmNSISMV 412
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KwSEN--ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQD-VYLFED--TIENNIKFGKQNASHEEVVQAA------------KKARchefiealpegydtiigeggaSLSGGEKQR 477
Cdd:PRK15064 388 AQDhAYDFENdlTLFDWMSQWRQEGDDEQAVRGTlgrllfsqddikKSVK---------------------VLSGGEKGR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 478 ISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTknKTVIMIAHRLKTIRN-ADQILVLKDGEIVE-RGNHEKLI 555
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE--GTLIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYL 524
|
....*
gi 1317668753 556 ENNGL 560
Cdd:PRK15064 525 RSQGI 529
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
362-544 |
1.29e-07 |
|
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: 52.22 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 362 TAIVGPSGSGKTTF--CNLIARFWDvnsgeiliGGKNIKDYKIENLMNSISMVFQDVYL-FEDTIENNIKFGKQNASHEE 438
Cdd:cd03240 25 TLIVGQNGAGKTTIieALKYALTGE--------LPPNSKGGAHDPKLIREGEVRAQVKLaFENANGKKYTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 439 VVQaakkarCHEfiealpEGYDTIIGEGGASLSGGEKQ------RISIARAMLKDADIIIFDEATANIDPEN-EDKLKEA 511
Cdd:cd03240 97 VIF------CHQ------GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEI 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1317668753 512 IETL--TKNKTVIMIAHRLKTIRNADQIL-VLKDGE 544
Cdd:cd03240 165 IEERksQKNFQLIVITHDEELVDAADHIYrVEKDGR 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
334-527 |
1.33e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.37 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKN-VSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNikdyKIENLMNSISM- 411
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG----KLFYVPQRPYMt 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 412 --VFQDVYLFEDTIENnikFGKQNASHEEVVQAAKKARCHEFIEAlpEGYDTIIGEGGASLSGGEKQRISIARAMLKDAD 489
Cdd:TIGR00954 528 lgTLRDQIIYPDSSED---MKRRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*...
gi 1317668753 490 IIIFDEATANIDPENEDKLKEAIEtlTKNKTVIMIAHR 527
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCR--EFGITLFSVSHR 638
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
314-545 |
1.47e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 314 IDSM-PDMREGSITEPIKNHDIVFKNVSFSYDDRPIL----------KNVSAEIKENTMTAIVGPSGSGKTTFCNLIARF 382
Cdd:PRK15439 233 IQAItPAAREKSLSASQKLWLELPGNRRQQAAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTELAETLYGL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 383 WDVNSGEILIGGKNIKDYKIENLMNSismvfQDVYLFEDT------IENNIKFGKQNASHEEV---VQAAKKArchefie 453
Cdd:PRK15439 313 RPARGGRIMLNGKEINALSTAQRLAR-----GLVYLPEDRqssglyLDAPLAWNVCALTHNRRgfwIKPAREN------- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 454 ALPEGYDTIIG-------EGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK-NKTVIMIA 525
Cdd:PRK15439 381 AVLERYRRALNikfnhaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFIS 460
|
250 260
....*....|....*....|.
gi 1317668753 526 HRLKTIRN-ADQILVLKDGEI 545
Cdd:PRK15439 461 SDLEEIEQmADRVLVMHQGEI 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
344-549 |
1.73e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 344 DDRPILKNVSAEIKENTMTAIVGPSGSGKTT--------FCNLIARFWDVNSGEILIGGK---NIKDYKIENLMNSISMV 412
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTllkalagdLTGGGAPRGARVTGDVTLNGEplaAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 413 FQDVYLFE-DTIENNIKFGKQNASHEEVVQAAKKARChefieALP-EGYDTIIGEGGASLSGGEKQRISIARAMLK---- 486
Cdd:PRK13547 92 AQPAFAFSaREIVLLGRYPHARRAGALTHRDGEIAWQ-----ALAlAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 487 -----DADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLK-TIRNADQILVLKDGEIVERG 549
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
338-398 |
1.77e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 1.77e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317668753 338 NVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIK 398
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK 66
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
53-226 |
5.55e-07 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 51.64 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 53 DYKAIF-ICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLG----RLT----TIATS 123
Cdd:cd18547 40 DFSGLLrILLLLLGLYLLSALFSY-LQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGdimsRVTndvdNISQA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 124 ---SLSQAemwvpmllvlvlggvLNTLVFVLGTLIF----NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRL 196
Cdd:cd18547 119 lsqSLTQL---------------ISSILTIVGTLIMmlyiSPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGEL 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1317668753 197 TKEVLATLQGMQVIKSYNLGGEN-------NRALRKS 226
Cdd:cd18547 184 NGYIEEMISGQKVVKAFNREEEAieefdeiNEELYKA 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
339-549 |
1.25e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 339 VSFSYDDRPI--LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWD----VNSGEILIGGKN---IKDYKIENLMNS- 408
Cdd:PRK11022 11 VHFGDESAPFraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDlqrISEKERRNLVGAe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 409 ISMVFQDVYlfeDTIENNIKFGKQNASHEEVVQA-AKKARCHEFIEALpegydTIIG-EGGAS--------LSGGEKQRI 478
Cdd:PRK11022 91 VAMIFQDPM---TSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLL-----NQVGiPDPASrldvyphqLSGGMSQRV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 479 SIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTI-RNADQILVLKDGEIVERG 549
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
146-292 |
1.87e-06 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 49.79 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 146 TLVFVLGTLIFNVKVGLVAVAGVIVF-FIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYnlGGENNRalR 224
Cdd:cd18585 123 ILATILFLAFFSPALALILLAGLLLAgVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIF--GALERQ--R 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 225 KSIKDTSKILLDLEKSVAPYTVIQRIVM----GITTVFMVYVSLKLNLSGELPLAETILMIMASFIIFEGLI 292
Cdd:cd18585 199 QQLEQLSDALIKEQRRLARLSGLSQALMillsGLTVWLVLWLGAPLVQNGALDGALLAMLVFAVLASFEAVA 270
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
357-528 |
2.56e-06 |
|
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: 49.29 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 357 KENTMTAIVGPSGSGKTTFCNLIA--------RF-----WDvnsgEIL--IGGKNIKDYKIENLMNSISMVFQDVYLfeD 421
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFddppdWD----EILdeFRGSELQNYFTKLLEGDVKVIVKPQYV--D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 422 TIENNIKfGKqnaSHEEVVQAAKKARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANID 501
Cdd:cd03236 98 LIPKAVK-GK---VGELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|....*...
gi 1317668753 502 PENEDKLKEAIETLTK-NKTVIMIAHRL 528
Cdd:cd03236 172 IKQRLNAARLIRELAEdDNYVLVVEHDL 199
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
337-549 |
4.14e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNSI------- 409
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 410 --SMVFQDVylfEDTIENNIKFG------------------KQNASH--EEVVQAAKKarchefIEALPegydtiigegg 467
Cdd:PRK11701 90 ewGFVHQHP---RDGLRMQVSAGgnigerlmavgarhygdiRATAGDwlERVEIDAAR------IDDLP----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 468 ASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTK--NKTVIMIAHRLKTIRN-ADQILVLKDGE 544
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGR 229
|
....*
gi 1317668753 545 IVERG 549
Cdd:PRK11701 230 VVESG 234
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
349-576 |
4.32e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGknikdykienlmnSISMVFQDVYLfedtieNNIK 428
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------------SAALIAISSGL------NGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 429 FGKQNASHEEVVQAAKKARCHEFIEALPEGYD--TIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENED 506
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEKIKEIIPEIIEFADigKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 507 K-LKEAIETLTKNKTVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKLIENNGLYSDLINAKAKAESWKL 576
Cdd:PRK13545 181 KcLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEERKDF 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
363-567 |
5.39e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 363 AIVGPSGSGKTTFcnliARfwdVNSGE-ILIGGKNIKDYK------IENLMNSISMVFQDvylfedtieNNIK------- 428
Cdd:PRK10938 33 AFVGANGSGKSAL----AR---ALAGElPLLSGERQSQFShitrlsFEQLQKLVSDEWQR---------NNTDmlspged 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 429 -FGKQNAsheEVVQAAKK--ARCHEFIEALpeGYDTIIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENE 505
Cdd:PRK10938 97 dTGRTTA---EIIQDEVKdpARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 506 DKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKlIENNGLYSDLINA 567
Cdd:PRK10938 172 QQLAELLASLHQSGiTLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREE-ILQQALVAQLAHS 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
337-516 |
1.21e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.34 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIEnlmnsismvFQDV 416
Cdd:PRK13538 5 RNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------YHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 417 YLF---------EDTIENNIKF---GKQNASHEEVVQAAKKARCHEFiEALPEGYdtiigeggasLSGGEKQRISIARAM 484
Cdd:PRK13538 76 LLYlghqpgiktELTALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLW 144
|
170 180 190
....*....|....*....|....*....|...
gi 1317668753 485 LKDADIIIFDEA-TAnIDpenedklKEAIETLT 516
Cdd:PRK13538 145 LTRAPLWILDEPfTA-ID-------KQGVARLE 169
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
307-545 |
1.30e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 307 AIDSVGFIDSM------------PDMREGSitePIknhdIVFKNVSFSYDDRPIL-KNVSAEIKENTMTAIVGPSGSGKT 373
Cdd:PLN03073 477 ALDRLGHVDAVvndpdykfefptPDDRPGP---PI----ISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKS 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 374 TFCNLIARFWDVNSGEILIGGK----NIKDYKIENLMNSISMVFQDVYLFEDTIENNIK--FGKQNASHEEVVQAAkkar 447
Cdd:PLN03073 550 TILKLISGELQPSSGTVFRSAKvrmaVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRahLGSFGVTGNLALQPM---- 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 448 chefiealpegydtiigeggASLSGGEKQRISIARAMLKDADIIIFDEATANIDpenedklKEAIETLTKNKT-----VI 522
Cdd:PLN03073 626 --------------------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-------LDAVEALIQGLVlfqggVL 678
|
250 260
....*....|....*....|....
gi 1317668753 523 MIAHRLKTIRNA-DQILVLKDGEI 545
Cdd:PLN03073 679 MVSHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
338-556 |
2.36e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 338 NVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGgkniKDYKIENLMnsismvfQD-- 415
Cdd:PRK11147 8 GAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLQ-------QDpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 416 ------VYLF-----------------------EDTIENNIKfgkQNASHEEVVQAAK----KARCHEFIEALPEGYDTI 462
Cdd:PRK11147 77 rnvegtVYDFvaegieeqaeylkryhdishlveTDPSEKNLN---ELAKLQEQLDHHNlwqlENRINEVLAQLGLDPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 463 IgeggASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLkeaiETLTKN--KTVIMIAHRLKTIRN-ADQILV 539
Cdd:PRK11147 154 L----SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWL----EGFLKTfqGSIIFISHDRSFIRNmATRIVD 225
|
250
....*....|....*...
gi 1317668753 540 LKDGEIVE-RGNHEKLIE 556
Cdd:PRK11147 226 LDRGKLVSyPGNYDQYLL 243
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
334-513 |
3.08e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 334 IVFKNVSFSYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIgGKNIKdykienlmnsISMVF 413
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 414 QdvylFEDTIENN-------------IKFGKqnasheevVQAAKKARCHEFiealpegydtiiGEGGA-------SLSGG 473
Cdd:PRK11819 394 Q----SRDALDPNktvweeisggldiIKVGN--------REIPSRAYVGRF------------NFKGGdqqkkvgVLSGG 449
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1317668753 474 EKQRISIARaMLKD-ADIIIFDEATANIDPENEDKLKEAIE 513
Cdd:PRK11819 450 ERNRLHLAK-TLKQgGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
321-545 |
3.11e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 321 REgsITE--PIKNHDI---VF--KNVSfSYD----DRPILKNVSAEIKENTMTAIVGPSGSGKT-TFCNLIARFWDVNSG 388
Cdd:PRK13549 242 RE--LTAlyPREPHTIgevILevRNLT-AWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEG 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 389 EILIGGKNIKdykIEN----LMNSISMVFQD-----VYLFEDTIENNIKFGKQNASHEEVVQAAKKARC-HEFIEAL--- 455
Cdd:PRK13549 319 EIFIDGKPVK---IRNpqqaIAQGIAMVPEDrkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTiLESIQRLkvk 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 456 -PEGYDTIigeggASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN 533
Cdd:PRK13549 396 tASPELAI-----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELPEVLG 470
|
250
....*....|...
gi 1317668753 534 -ADQILVLKDGEI 545
Cdd:PRK13549 471 lSDRVLVMHEGKL 483
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
463-535 |
4.66e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 463 IGEGGASLSGGEKQ------RISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKT----VIMIAHRLKTIR 532
Cdd:PRK01156 795 MVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISHHRELLS 874
|
...
gi 1317668753 533 NAD 535
Cdd:PRK01156 875 VAD 877
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
337-546 |
6.09e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 337 KNVSF-SYDDRPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKIENLMNS-ISmvfq 414
Cdd:COG3845 261 ENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 415 dvYLFED----------TIENNI---KFGKQNASHEEVVQAAK-KARCHEFIEAL---PEGYDTIIGeggaSLSGGEKQR 477
Cdd:COG3845 337 --YIPEDrlgrglvpdmSVAENLilgRYRRPPFSRGGFLDRKAiRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 478 ISIARAMLKDADIIIFDE--------ATANIdpenEDKLKEAIEtltKNKTVIMIAHRLKTIRN-ADQILVLKDGEIV 546
Cdd:COG3845 411 VILARELSRDPKLLIAAQptrgldvgAIEFI----HQRLLELRD---AGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
43-297 |
7.29e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 44.86 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 43 MLVNIFSKTLDYKAIF-ICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIA 121
Cdd:cd18557 21 RLIDTIIKGGDLDVLNeLALILLAIYLLQSVFTF-VRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 122 TSSLSQAEMWVPMLLVLVLGGVLnTLVFVLGTLIF-NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEV 200
Cdd:cd18557 100 SSDTSVLQSAVTDNLSQLLRNIL-QVIGGLIILFIlSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 201 LATLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAEtilm 280
Cdd:cd18557 179 EESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGE---- 254
|
250
....*....|....*..
gi 1317668753 281 iMASFIIFEGLIGAGSN 297
Cdd:cd18557 255 -LTSFILYTIMVASSVG 270
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
470-561 |
7.72e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 470 LSGGEKQRISIARAMLKDAD---IIIFDEATANIDPENEDKLKEAIETLTKN-KTVIMIAHRLKTIRNADQILVL----- 540
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKgNTVVVIEHNLDVIKTADWIIDLgpegg 910
|
90 100
....*....|....*....|..
gi 1317668753 541 -KDGEIVERGNHEKLIENNGLY 561
Cdd:PRK00349 911 dGGGEIVATGTPEEVAKVEASY 932
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
346-545 |
8.43e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 346 RPILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYK-IENLMNSISMVFQD-----VYLF 419
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 420 EDtIENN--IKFGKQNASHEEVVQAAK-KARCHEFIEAL---PEGYDTIIGeggaSLSGGEKQRISIARAMLKDADIIIF 493
Cdd:PRK10982 341 LD-IGFNslISNIRNYKNKVGLLDNSRmKSDTQWVIDSMrvkTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 494 DEATANIDPENEDKLKEAIETLT-KNKTVIMIAHRLKTIRN-ADQILVLKDGEI 545
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
449-540 |
9.64e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 449 HEFIEALPE-GYDTI-IGEGGASLSGGEKQRISIARAML---KDADIIIFDEATANIDPENEDKLKEAIETLT-KNKTVI 522
Cdd:PRK00635 787 HEKIHALCSlGLDYLpLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVV 866
|
90
....*....|....*...
gi 1317668753 523 MIAHRLKTIRNADQILVL 540
Cdd:PRK00635 867 IIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
146-293 |
1.55e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 43.97 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 146 TLVFVLGTLIF-NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSYNLGGENNRALR 224
Cdd:cd18570 128 MVIISGIILFFyNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIE 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317668753 225 KSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAE--TILMIMASFIIF-EGLIG 293
Cdd:cd18570 208 KKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQliAFNALLGYFLGPiENLIN 279
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
355-543 |
1.60e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 355 EIKENTMTAIVGPSGSGKTTFCNLI--ARFwdvnsgeiligGKNIKDYKIENLMNSISMVfqdvylfEDTIENNIKFGKQ 432
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAItyALY-----------GKTPRYGRQENLRSVFAPG-------EDTAEVSFTFQLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 433 NASHEevVQAAKKARCHEFIEA--LPEG-YDTIIGEGGASLSGGEKQRISIARAM-LKDA---------DIIIFDEATAN 499
Cdd:cd03279 86 GKKYR--VERSRGLDYDQFTRIvlLPQGeFDRFLARPVSTLSGGETFLASLSLALaLSEVlqnrggarlEALFIDEGFGT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1317668753 500 IDPENEDKLKEAIETL-TKNKTVIMIAH--RLKTiRNADQILVLKDG 543
Cdd:cd03279 164 LDPEALEAVATALELIrTENRMVGVISHveELKE-RIPQRLEVIKTP 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
445-554 |
1.71e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 445 KARCHEFIE--ALPEGydtiIGEGGASLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKN-KTV 521
Cdd:NF000106 122 RARADELLErfSLTEA----AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATV 197
|
90 100 110
....*....|....*....|....*....|....
gi 1317668753 522 IMIAHRLKTIRN-ADQILVLKDGEIVERGNHEKL 554
Cdd:NF000106 198 LLTTQYMEEAEQlAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
361-538 |
3.61e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.07 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 361 MTAIVGPSGSGKTtfcNLI-ARFWdvnsgeiLIGGKNIKDYKIENLmnsismvfqdvylfEDTIENNIKfGKQNASHEEV 439
Cdd:cd03278 24 LTAIVGPNGSGKS---NIIdAIRW-------VLGEQSAKSLRGEKM--------------SDVIFAGSE-TRKPANFAEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 440 vqaakkarchEFIEALPEGYDTIIGEG---------G------ASLSGGEKQRISI----ARAMLKDADIIIFDEATANI 500
Cdd:cd03278 79 ----------TLTFDNSDGRYSIISQGdvseiieapGkkvqrlSLLSGGEKALTALallfAIFRVRPSPFCVLDEVDAAL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1317668753 501 DPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQIL 538
Cdd:cd03278 149 DDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
326-545 |
4.02e-04 |
|
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: 43.27 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 326 TEPIKNHDIVF--KNVSFSYDDRPILK---NVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWD-VNSGEILIGGKNIKd 399
Cdd:TIGR02633 248 HEPHEIGDVILeaRNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVD- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 400 ykIENLMNSI----SMVFQDVYlfEDTIENNIKFGK-------QNASHEEVVQAAKKARC-HEFIEAL---PEGYDTIIG 464
Cdd:TIGR02633 327 --IRNPAQAIragiAMVPEDRK--RHGIVPILGVGKnitlsvlKSFCFKMRIDAAAELQIiGSAIQRLkvkTASPFLPIG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 465 eggaSLSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRLKTIRN-ADQILVLKD 542
Cdd:TIGR02633 403 ----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGlSDRVLVIGE 478
|
...
gi 1317668753 543 GEI 545
Cdd:TIGR02633 479 GKL 481
|
|
| THEP1 |
COG1618 |
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism]; |
363-556 |
4.24e-04 |
|
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
Pssm-ID: 441225 [Multi-domain] Cd Length: 175 Bit Score: 41.43 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 363 AIVGPSGSGKTTFCNLIARFW---DVNSG-----EILIGGKNIkDYKIENLMNSISMVFqdvylfedtiennikfgkqna 434
Cdd:COG1618 4 FITGRPGVGKTTLLLKVVEELrdeGLRVGgfitpEVREGGRRV-GFKLVDLATGEEAIL--------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 435 SHEEVVQAAKKARCHEFIEALPEgydtiIGeggaslsggekqrISIARAMLKDADIIIFDEatanIDP-ENE-DKLKEAI 512
Cdd:COG1618 62 ASVDIDSGPRVGKYGVDPEALEA-----IA-------------VEALERALEEADLIVIDE----IGKmELKsKGFREAI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1317668753 513 ET-LTKNKTVIMIAHRlKTIRNADQILVLKDGEIVE--RGNHEKLIE 556
Cdd:COG1618 120 EEaLDSDKPVLATVHK-RSHPFLDEIRERGGVEVLEvtPENRDALPE 165
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
470-561 |
6.38e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 470 LSGGEKQRISIARAMLKDAD---IIIFDEATANIDPENEDKLKEAIETLT-KNKTVIMIAHRLKTIRNADQILVL----- 540
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVdKGNTVVVIEHNLDVIKTADWIIDLgpegg 906
|
90 100
....*....|....*....|..
gi 1317668753 541 -KDGEIVERGNHEKLIENNGLY 561
Cdd:COG0178 907 dGGGEIVAEGTPEEVAKVKASY 928
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
47-292 |
6.49e-04 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 42.01 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 47 IFSKTLDYKAIF-ICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATSSL 125
Cdd:cd18541 29 LTAGTLTASQLLrYALLILLLALLIGIFRF-LWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 126 SQAEMWVPMLLVLVLggvlNTLVFVLGTLIF----NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVL 201
Cdd:cd18541 108 NAVRMALGPGILYLV----DALFLGVLVLVMmftiSPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 202 ATLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELPLAEtilmi 281
Cdd:cd18541 184 ESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD----- 258
|
250
....*....|.
gi 1317668753 282 MASFIIFEGLI 292
Cdd:cd18541 259 LVAFNSYLGML 269
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
347-501 |
9.27e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 347 PILKNVSAEIKENTMTAIVGPSGSGKTTFCNLIARFWDVNSGEILIGGKNIKDYKI-ENLMNSIsmvfqdVYLFEDTIEN 425
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLANGI------VYISEDRKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 426 NIKFG---KQNAS---------------HEEVVQAAKkarchEFIEAL----PeGYDTIIGEggasLSGGEKQRISIARA 483
Cdd:PRK10762 340 GLVLGmsvKENMSltalryfsraggslkHADEQQAVS-----DFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARG 409
|
170
....*....|....*...
gi 1317668753 484 MLKDADIIIFDEATANID 501
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVD 427
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
468-558 |
9.91e-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: 42.31 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 468 ASLSGGEKQRISIAR---AMLKDAdIIIFDEATANIDPENEDKLkeaIETLT----KNKTVIMIAHRLKTIRNADQILVL 540
Cdd:TIGR00630 487 GTLSGGEAQRIRLATqigSGLTGV-LYVLDEPSIGLHQRDNRRL---INTLKrlrdLGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100
....*....|....*....|....
gi 1317668753 541 ------KDGEIVERGNHEKLIENN 558
Cdd:TIGR00630 563 gpgageHGGEVVASGTPEEILANP 586
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
349-377 |
1.09e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 1.09e-03
10 20
....*....|....*....|....*....
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCN 377
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
349-377 |
1.23e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 1.23e-03
10 20
....*....|....*....|....*....
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGKTTFCN 377
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
148-288 |
1.42e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 40.91 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 148 VFVLGTLI----FNVKVGLVAVAGVIVFFIVTSMMEKKS-SANADKMTET---QTRLtkevLATLQGMQVIKSYNLGGEN 219
Cdd:cd18567 127 LMAILTLVmmflYSPKLALIVLAAVALYALLRLALYPPLrRATEEQIVASakeQSHF----LETIRGIQTIKLFGREAER 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 220 NRALRKSIKDTSKILLDLEKSVAPYTVIQRIVMGITTVFMVYVSLKLNLSGELplaeTILMIMAsFIIF 288
Cdd:cd18567 203 EARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEF----TVGMLFA-FLAY 266
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
468-538 |
1.69e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317668753 468 ASLSGGEKQRISIARAMlkDADII----IFDEATANIDPENEDKLKEAIETL-TKNKTVIMIAHRLKTIRNADQIL 538
Cdd:PRK00635 475 ATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLrDQGNTVLLVEHDEQMISLADRII 548
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
94-213 |
1.79e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 40.54 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 94 RIEIGEKIKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLLVLVLGGVlnTLVFVLGTLIF-NVKVGLVAVAGVIVFF 172
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLL--TLVVGLVVMLVlSPPLALVALASLPPLV 152
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1317668753 173 IVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSY 213
Cdd:cd18543 153 LVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAF 193
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
112-213 |
2.12e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 40.51 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 112 FSLGRLTTIATSSLS---QAEMWVPMLLVLVLggvlnTLVFVLGTLIFNVKV------GLVAVAGVIVFFIVTSMMEKKS 182
Cdd:cd18597 97 FPNGKITNLMSTDLSridFALGFFHFLWTAPI-----QIIIAIALLIVNLGPsalvgiGVLILSIPLQGFLMKKLFKLRK 171
|
90 100 110
....*....|....*....|....*....|.
gi 1317668753 183 SANadKMTETQTRLTKEVlatLQGMQVIKSY 213
Cdd:cd18597 172 KAN--KITDKRVKLTQEI---LQGIRVIKFY 197
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
470-538 |
2.22e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 470 LSGGEKQRISIARA----MLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQIL 538
Cdd:TIGR02168 1090 LSGGEKALTALALLfaifKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLY 1162
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
47-214 |
2.29e-03 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 40.06 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 47 IFSKTLDYKAIFICLGILVISLVGKIMTLKISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATS--- 123
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNdte 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 124 SLSqaEMWVpmllvLVLGGVLNTLVFVLGTLIF----NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKE 199
Cdd:cd18544 110 ALN--ELFT-----SGLVTLIGDLLLLIGILIAmfllNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAF 182
|
170
....*....|....*
gi 1317668753 200 VLATLQGMQVIKSYN 214
Cdd:cd18544 183 LQESISGMSVIQLFN 197
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
363-387 |
2.50e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 39.44 E-value: 2.50e-03
10 20
....*....|....*....|....*
gi 1317668753 363 AIVGPSGSGKTTFCNLIARFWDVNS 387
Cdd:COG0572 11 GIAGPSGSGKTTFARRLAEQLGADK 35
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
146-294 |
2.50e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 40.28 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 146 TLVFVLGTLIFNVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKSynLGGENNRALRK 225
Cdd:cd18586 126 APLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKA--LGMLGNLRRRW 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317668753 226 SIKDTSKILLDLEKS--VAPYTVIQRIVMGITTVFMVYVSLKLNLSGELplaeTILMIMASFII-------FEGLIGA 294
Cdd:cd18586 204 EARHAETLELQIRASdlAGAISAIGKTLRMALQSLILGVGAYLVIDGEL----TIGALIAASILsgralapIDQLVGA 277
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
469-538 |
2.64e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 2.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317668753 469 SLSGGEKQRISI----ARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNKTVIMIAHRLKTIRNADQIL 538
Cdd:pfam02463 1077 LLSGGEKTLVALalifAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
22-288 |
2.89e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 40.07 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 22 SILAGFLHAVFNALEFGAIYYM--LVNIFSKTLDYKAIFICLGI-LVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIG 98
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMadIIDEGIANGDLSYILRTGLLmLLLALLGLIAGI-LAGYFAAKASQGFGRDLRKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 99 EKIKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLLVLVLGgvlnTLVFVLGTLIF----NVKVGLVAVAGVIVFFIV 174
Cdd:cd18548 80 EKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVR----APIMLIGAIIMafriNPKLALILLVAIPILALV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 175 TSMMEKKS---SANADKMTETQTRLTKEvlaTLQGMQVIKSYNLGGENNRALRKSIKDTSKILLDLEKSVAPYTVIQRIV 251
Cdd:cd18548 156 VFLIMKKAiplFKKVQKKLDRLNRVVRE---NLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1317668753 252 MGITTVFMVYVSLKLNLSGELPLAETI------LMIMASFIIF 288
Cdd:cd18548 233 MNLAIVAILWFGGHLINAGSLQVGDLVafinylMQILMSLMML 275
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
57-213 |
3.32e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 39.72 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 57 IFICLGILVISLVGKIMTLkISQMAQTHAGYFMAAHKRIEIGEKIKRVPMGFFSSFSLGRLTTIATSSLSQAEMWVPMLL 136
Cdd:cd18542 39 WLLALLILGVALLRGVFRY-LQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 137 VLVLggvlNTLVFVLGTLIF----NVKVGLVAVAGVIVFFIVTSMMEKKSSANADKMTETQTRLTKEVLATLQGMQVIKS 212
Cdd:cd18542 118 VELV----RAVLLFIGALIImfsiNWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKA 193
|
.
gi 1317668753 213 Y 213
Cdd:cd18542 194 F 194
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
468-517 |
3.50e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 3.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317668753 468 ASLSGGEKQR-ISIA-----RAMLKDAD-------IIIFDEATANIDPENedkLKEAIETLTK 517
Cdd:pfam13558 31 GGLSGGEKQLlAYLPlaaalAAQYGSAEgrppaprLVFLDEAFAKLDEEN---IRTALELLRA 90
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
470-546 |
5.28e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.51 E-value: 5.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317668753 470 LSGGEKQRISIARAMLKDADIIIFDEATANIDPENEDKLKEAIETLTKNK-TVIMIAHRL-KTIRNADQILVLKDGEIV 546
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGvAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
440-543 |
5.71e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 440 VQAAKKARCHEFIEALPegydtiIGEGGASLSGGEKQRISIARAML---KDADIIIFDEATANIDPENEDKLKEAIETL- 515
Cdd:PRK00635 1676 IQKPLQALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLv 1749
|
90 100
....*....|....*....|....*...
gi 1317668753 516 TKNKTVIMIAHRLKTIRNADQILVLKDG 543
Cdd:PRK00635 1750 SLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
359-529 |
6.16e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 39.55 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 359 NTMTAIVGPSGSGKTTFCNLIARFW----------DV-NSGEILI---GGKNIKdykienLMNSISMVFQDVYLfEDTIE 424
Cdd:COG3451 204 NGNTLILGPSGSGKSFLLKLLLLQLlrygarivifDPgGSYEILVralGGTYID------LSPGSPTGLNPFDL-EDTEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 425 nnikfgkqnasheevvqaaKKARCHEFIEALpegydtiIGEGGASLSGGEKQRISIAramlkdadiiiFDEATANIDPEN 504
Cdd:COG3451 277 -------------------KRDFLLELLELL-------LGREGEPLTPEERAAIDRA-----------VRALYRRADPEE 319
|
170 180
....*....|....*....|....*
gi 1317668753 505 EDKLKEAIETLTKNKTVIMIAHRLK 529
Cdd:COG3451 320 RTTLSDLYELLKEQPEAKDLAARLE 344
|
|
| VirB4_CagE |
TIGR00929 |
type IV secretion/conjugal transfer ATPase, VirB4 family; Type IV secretion systems are found ... |
225-380 |
6.35e-03 |
|
type IV secretion/conjugal transfer ATPase, VirB4 family; Type IV secretion systems are found in Gram-negative pathogens. They export proteins, DNA, or complexes in different systems and are related to plasmid conjugation systems. This model represents related ATPases that include VirB4 in Agrobacterium tumefaciens (DNA export) CagE in Helicobacter pylori (protein export) and plasmid TraB (conjugation).
Pssm-ID: 273346 [Multi-domain] Cd Length: 785 Bit Score: 39.61 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 225 KSIKDTSKILLDLEKSvapytviQRIVMG-ITTVFMVY-------------VSLKLNLSGELPLAETILMIMA------- 283
Cdd:TIGR00929 300 KSQIAELDEALDELTS-------GDFVMGeHHLSLVVYaedlekldaalreARSLLNACGIVAVIETLGLEAAfwsqlpg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 284 --SFIIFEGLIGAgSNMAILRACENAidSVGFIDSmpdmregsitEPIKNHDIVFKNVSFSyddrPILKNVSA-EIKENT 360
Cdd:TIGR00929 373 nfSWNPRKSLITS-RNFASLIPFHNF--NLGKLRG----------NPWGPALTLLKTQSGT----PFYFNFHVrDAKVLG 435
|
170 180
....*....|....*....|
gi 1317668753 361 MTAIVGPSGSGKTTFCNLIA 380
Cdd:TIGR00929 436 HTLIFGPTGSGKTTLLNFLL 455
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
94-294 |
9.24e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 38.23 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 94 RIEIGEKIKRVPMGFFSSFSLGRLTTIATSSLSQAEmwvPMLLVLVLGGVLNTLVFVLGTLI---FNVKVGLVAVAGVIV 170
Cdd:cd18576 72 RKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQ---DTLTTTLAEFLRQILTLIGGVVLlffISWKLTLLMLATVPV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317668753 171 FFIVTSM----MEKKSSANADKMTETQTRLTKevlaTLQGMQVIKSY-NLGGENNRAlRKSIKDTSKILLDLEKSVAPYT 245
Cdd:cd18576 149 VVLVAVLfgrrIRKLSKKVQDELAEANTIVEE----TLQGIRVVKAFtREDYEIERY-RKALERVVKLALKRARIRALFS 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1317668753 246 VIQRIVMGITTVFMVYVSLKLNLSGELPLAEtilmiMASFIIFEGLIGA 294
Cdd:cd18576 224 SFIIFLLFGAIVAVLWYGGRLVLAGELTAGD-----LVAFLLYTLFIAG 267
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
349-372 |
9.69e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 9.69e-03
10 20
....*....|....*....|....
gi 1317668753 349 LKNVSAEIKENTMTAIVGPSGSGK 372
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGK 39
|
|
| |
