|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-520 |
6.81e-95 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 298.90 E-value: 6.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVR--YLAQQLEPADYPTVAD 86
Cdd:COG0488 14 LDDVSLSINPGD-------------RIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRigYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 87 --LAGVRPWLEALARIEAGSLDAADYECLGER-------------WDIRQRLADALAAEGLGHLRADTPSERLSGGECMR 151
Cdd:COG0488 81 tvLDGDAELRALEAELEELEAKLAEPDEDLERlaelqeefealggWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 152 VALLGAFLDDADFLILDEPSNPLDgparallrARLAAW--------DGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGG 222
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLD--------LESIEWleeflknyPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 223 GYSFYaqsreeareaaerrLDQRRLERKRQTlamreqqqrqerrqasgRREGKTANQAKILLgGFRERSEVSAGKLRNAh 302
Cdd:COG0488 233 NYSAY--------------LEQRAERLEQEA-----------------AAYAKQQKKIAKEE-EFIRRFRAKARKAKQA- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 303 QAERERLDReVREAAREVEEASPLLLDSPDAELAaqRRIVELKGA-------VLphlrgpLREIDLLLSGPRRLALVGPN 375
Cdd:COG0488 280 QSRIKALEK-LEREEPPRRDKTVEIRFPPPERLG--KKVLELEGLsksygdkTL------LDDLSLRIDRGDRIGLIGPN 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 376 GSGKSTLLRLLAGQRAPLAGT--CAVTVGAAYLDQRLSLLDHGRGVLEQLLEVNRSRGESWLRTRLAQLGLPAERLAQPC 453
Cdd:COG0488 351 GAGKSTLLKLLAGELEPDSGTvkLGETVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPV 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316862561 454 ATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHDPWFLRRL 520
Cdd:COG0488 431 GVLSGGEKARLALAKLLL--SPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
36-520 |
1.28e-40 |
|
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: 154.71 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 36 GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG--RVRYLAQ--QLEPADypTVAD--LAGVRPWLEALARIEAGSL---- 105
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPgiKVGYLPQepQLDPTK--TVREnvEEGVAEIKDALDRFNEISAkyae 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 106 DAADYECLGER-------------WDIRQRLADALAAeglghLRA---DTPSERLSGGECMRVALLGAFLDDADFLILDE 169
Cdd:TIGR03719 113 PDADFDKLAAEqaelqeiidaadaWDLDSQLEIAMDA-----LRCppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 170 PSNPLDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGGGYSFYaqsreeareaaerrldqrrLE 248
Cdd:TIGR03719 188 PTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVaGWILELDRGRGIPWEGNYSSW-------------------LE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 249 RKRQTLAMreqqqrqerrqaSGRREGKTANQAKillggfRERSEV-SAGKLRNAHQAER----ERLDREVREAAREVEE- 322
Cdd:TIGR03719 249 QKQKRLEQ------------EEKEESARQKTLK------RELEWVrQSPKGRQAKSKARlaryEELLSQEFQKRNETAEi 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 323 ---ASPLLLDspdaelaaqrRIVELKGAVLPHLRGPLREiDLLLSGPRR--LALVGPNGSGKSTLLRLLAGQRAPLAGTC 397
Cdd:TIGR03719 311 yipPGPRLGD----------KVIEAENLTKAFGDKLLID-DLSFKLPPGgiVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 398 AV--TVGAAYLDQRLSLLDHGRGVLEQ------LLEVNRSRGESwlRTRLAQLGLPAERLAQPCATLSGGERLKAALALV 469
Cdd:TIGR03719 380 EIgeTVKLAYVDQSRDALDPNKTVWEEisggldIIKLGKREIPS--RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKT 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2316862561 470 LyaDRPAQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHDPWFLRRL 520
Cdd:TIGR03719 458 L--KSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
36-518 |
5.82e-39 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 151.09 E-value: 5.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 36 GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG--RVRYLAQQLEPADYPT---VADlaGVRPWLEALARIEA-------- 102
Cdd:PRK10636 31 GLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALPQPAleyVID--GDREYRQLEAQLHDanerndgh 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 103 ------GSLDAADyeclgeRWDIRQRLADALAAEGLGHLRADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLDG 176
Cdd:PRK10636 109 aiatihGKLDAID------AWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 177 PARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGGGYSFYaqsreeareaaerrlDQRRLERKRQTLA 255
Cdd:PRK10636 183 DAVIWLEKWLKSYQGTLILISHDRDFLDPIvDKIIHIEQQSLFEYTGNYSSF---------------EVQRATRLAQQQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 256 MREqqqrqerrqasgrregktANQAKIL-LGGFRERSEVSAGKLRNAhQAERERLDREVREAAREVEEASPLLLDSPDA- 333
Cdd:PRK10636 248 MYE------------------SQQERVAhLQSYIDRFRAKATKAKQA-QSRIKMLERMELIAPAHVDNPFHFSFRAPESl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 334 --ELAAQRRIVELKGAvlphlRGPLREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGA--AYLDQ- 408
Cdd:PRK10636 309 pnPLLKMEKVSAGYGD-----RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQh 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 409 RLSLLDHGRGVLEQLLEVNRSRGESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLYaDRPaQLLLLDEPDNHL 488
Cdd:PRK10636 384 QLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVW-QRP-NLLLLDEPTNHL 461
|
490 500 510
....*....|....*....|....*....|
gi 2316862561 489 DLVARQALETMLRQYRGALLVVSHDPWFLR 518
Cdd:PRK10636 462 DLDMRQALTEALIDFEGALVVVSHDRHLLR 491
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-516 |
5.40e-35 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 139.32 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 19 GSLLFSD---LDETFDTRHTG----LVGRNGVGKSLLARLLAGHLQPSSGS--------VRR---------QGRV----- 69
Cdd:PRK11147 9 AWLSFSDaplLDNAELHIEDNervcLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdliVARlqqdpprnvEGTVydfva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 70 ---RYLAQQLEpaDYPTVADLAGVRPW---LEALARIEAgSLDAADYeclgerWDIRQRLADALAAEGLGhlrADTPSER 143
Cdd:PRK11147 89 egiEEQAEYLK--RYHDISHLVETDPSeknLNELAKLQE-QLDHHNL------WQLENRINEVLAQLGLD---PDAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 144 LSGGECMRVALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGG 222
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMaTRIVDLDRGKLVSYPG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 223 GYSFYaqsreeareaaerrldqrrLERKRQTLAMREQQQRQERRQASGR----REGKTANqakillggfRERSE--VSAG 296
Cdd:PRK11147 237 NYDQY-------------------LLEKEEALRVEELQNAEFDRKLAQEevwiRQGIKAR---------RTRNEgrVRAL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 297 K-LRNAHQAERERL---DREVREAAR------EVEEASPLLldsPDAELaaqrriveLKGAVLPHLRGPlreidlllsgp 366
Cdd:PRK11147 289 KaLRRERSERREVMgtaKMQVEEASRsgkivfEMENVNYQI---DGKQL--------VKDFSAQVQRGD----------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 367 rRLALVGPNGSGKSTLLRLLAGQRAPLAGT--CAVTVGAAYLDQRLSLLDHGRGVLE------QLLEVN-RSRGE-SWLR 436
Cdd:PRK11147 347 -KIALIGPNGCGKTTLLKLMLGQLQADSGRihCGTKLEVAYFDQHRAELDPEKTVMDnlaegkQEVMVNgRPRHVlGYLQ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 437 TRLaqlgLPAERLAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHDPWF 516
Cdd:PRK11147 426 DFL----FHPKRAMTPVKALSGGERNRLLLARLFL--KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
356-520 |
2.34e-34 |
|
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: 126.79 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV--TVGAAYLDQrlslldhgrgvleqllevnrsrges 433
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 434 wlrtrlaqlglpaerlaqpcatLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHD 513
Cdd:cd03221 71 ----------------------LSGGEKMRLALAKLLL--ENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHD 126
|
....*..
gi 2316862561 514 PWFLRRL 520
Cdd:cd03221 127 RYFLDQV 133
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-520 |
1.74e-32 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 131.01 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 36 GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG--RVRYLAQ--QLEPADypTVAD--LAGVRPWLEALARIE----AGSL 105
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPgiKVGYLPQepQLDPEK--TVREnvEEGVAEVKAALDRFNeiyaAYAE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 106 DAADYECLGER-------------WDIRQRLADALAAeglghLR---ADTPSERLSGGECMRVALLGAFLDDADFLILDE 169
Cdd:PRK11819 115 PDADFDALAAEqgelqeiidaadaWDLDSQLEIAMDA-----LRcppWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 170 PSNPLDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELStlglRSYG----GGYSFYaqsreeareaaerrldq 244
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVaGWILELD----RGRGipweGNYSSW----------------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 245 rrLERKRQTLAMreqqqrqerrqasgrrEGKT-ANQAKILLggfRERSEVSAG-KLRNAHQAER-ERLDREVREAAREVE 321
Cdd:PRK11819 249 --LEQKAKRLAQ----------------EEKQeAARQKALK---RELEWVRQSpKARQAKSKARlARYEELLSEEYQKRN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 322 EaspllldspDAEL---AAQR---RIVELKGA-------VLphlrgplreID-LLLSGPRR--LALVGPNGSGKSTLLRL 385
Cdd:PRK11819 308 E---------TNEIfipPGPRlgdKVIEAENLsksfgdrLL---------IDdLSFSLPPGgiVGIIGPNGAGKSTLFKM 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 386 LAGQRAPLAGTCAV--TVGAAYLDQRLSLLDHGRGVLEQ------LLEVNRSRGESwlRTRLAQLGLPAERLAQPCATLS 457
Cdd:PRK11819 370 ITGQEQPDSGTIKIgeTVKLAYVDQSRDALDPNKTVWEEisggldIIKVGNREIPS--RAYVGRFNFKGGDQQKKVGVLS 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 458 GGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHDPWFLRRL 520
Cdd:PRK11819 448 GGERNRLHLAKTLKQG--GNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI 508
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-513 |
4.72e-31 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 128.05 E-value: 4.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 33 RHTGLVGRNGVGKSLLARLLAGHlqpSSGSVRRQGRVRYLAQQLEPADYPTV-----------------ADLAGVRPWLE 95
Cdd:PLN03073 204 RHYGLVGRNGTGKTTFLRYMAMH---AIDGIPKNCQILHVEQEVVGDDTTALqcvlntdiertqlleeeAQLVAQQRELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 96 ---ALARIEAGSLDAADYECLGERW-DIRQRL-------ADALAAEGLGHLrADTP------SERLSGGECMRVALLGAF 158
Cdd:PLN03073 281 fetETGKGKGANKDGVDKDAVSQRLeEIYKRLelidaytAEARAASILAGL-SFTPemqvkaTKTFSGGWRMRIALARAL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 159 LDDADFLILDEPSNPLDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGGGYSFYaqsreearea 237
Cdd:PLN03073 360 FIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVvTDILHLHGQKLVTYKGDYDTF---------- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 238 aerrldqrrlERKRqtlamreqqqrqerrqasgrrEGKTANQAKILLGGFRERSEVSAGKLRNAHQAERERLDREVREAA 317
Cdd:PLN03073 430 ----------ERTR---------------------EEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKAL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 318 REVEEASPLLLDS------PDAELAAQRRIVELKGAVLPHLRGPL--REIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQ 389
Cdd:PLN03073 479 DRLGHVDAVVNDPdykfefPTPDDRPGPPIISFSDASFGYPGGPLlfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 390 RAPLAGTC--AVTVGAAYLDQ-RLSLLDHGRGVLEQLLEVNRSRGESWLRTRLAQLGLPAERLAQPCATLSGGERLKAAL 466
Cdd:PLN03073 559 LQPSSGTVfrSAKVRMAVFSQhHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAF 638
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2316862561 467 ALVLYaDRPaQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHD 513
Cdd:PLN03073 639 AKITF-KKP-HILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHD 683
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-227 |
1.35e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.40 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLpDGSLLFSDLDETFDT--RhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVR--YLAQ---QLEPA 79
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRgdR-IGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKigYFDQhqeELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 80 DypTVadlagvrpwLEALARIEAGsldaadyeclGERWDIRQRLADAL-AAEglghlRADTPSERLSGGECMRVALLGAF 158
Cdd:COG0488 394 K--TV---------LDELRDGAPG----------GTEQEVRGYLGRFLfSGD-----DAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 159 LDDADFLILDEPSNPLDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGGGYSFY 227
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVaTRILEFEDGGVREYPGGYDDY 517
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
356-521 |
1.23e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.51 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTC-----AVTVGA--------AYLDQRLSLLDHgrGVLEQ 422
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAMPppewrrqvAYVPQEPALWGG--TVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 LLEVNRSRGESWLRTR----LAQLGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALET 498
Cdd:COG4619 94 LPFPFQLRERKFDRERalelLERLGLPPDILDKPVERLSGGERQRLALIRAL-LLQP-DVLLLDEPTSALDPENTRRVEE 171
|
170 180
....*....|....*....|....*..
gi 2316862561 499 MLRQYR----GALLVVSHDPWFLRRLG 521
Cdd:COG4619 172 LLREYLaeegRAVLWVSHDPEQIERVA 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
356-514 |
3.01e-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: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLD-----QRLSLLDHGRG------VLEQLL 424
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAredyrRRLAYLGHADGlkpeltVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 425 EVNRSRGESWLRTR----LAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETML 500
Cdd:COG4133 98 FWAALYGLRADREAideaLEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAP--LWLLDEPFTALDAAGVALLAELI 174
|
170
....*....|....*..
gi 2316862561 501 RQYR---GALLVVSHDP 514
Cdd:COG4133 175 AAHLargGAVLLTTHQP 191
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-213 |
1.19e-23 |
|
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: 96.75 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLpDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVR--YLAQqlepadypt 83
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPgDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKigYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 84 vadlagvrpwlealarieagsldaadyeclgerwdirqrladalaaeglghlradtpserLSGGECMRVALLGAFLDDAD 163
Cdd:cd03221 71 ------------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2316862561 164 FLILDEPSNPLDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELS 213
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVaTKIIELE 141
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
356-520 |
9.13e-23 |
|
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: 96.38 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQrLSLLDHGRGV---------------- 419
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGE--VLVDGKDLTK-LSLKELRRKVglvfqnpddqffgptv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 420 -------LEQLlevNRSRGESWLRTR--LAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDL 490
Cdd:cd03225 94 eeevafgLENL---GLPEEEIEERVEeaLELVGL-EGLRDRSPFTLSGGQKQRVAIAGVL-AMDP-DILLLDEPTAGLDP 167
|
170 180 190
....*....|....*....|....*....|...
gi 2316862561 491 VARQALETMLRQYRGA---LLVVSHDPWFLRRL 520
Cdd:cd03225 168 AGRRELLELLKKLKAEgktIIIVTHDLDLLLEL 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
356-514 |
2.08e-22 |
|
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: 94.42 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGaaylDQRLSLLDHG-----RGVLEQLLEvnrsr 430
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE--ILLD----GKDLASLSPKelarkIAYVPQALE----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 431 geswlRTRLAQLglpAERlaqPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLvaRQALETM-----LRQYRG 505
Cdd:cd03214 84 -----LLGLAHL---ADR---PFNELSGGERQRVLLARALAQE--PPILLLDEPTSHLDI--AHQIELLellrrLARERG 148
|
170
....*....|
gi 2316862561 506 -ALLVVSHDP 514
Cdd:cd03214 149 kTVVMVLHDL 158
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
356-519 |
3.16e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.22 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGA--AYLDQRLSLLDHGRGVLEQLLEVNRSRGES 433
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvAYVPQRSEVPDSLPLTVRDLVAMGRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 434 WLR--TR---------LAQLGLpAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQ 502
Cdd:NF040873 88 LWRrlTRddraavddaLERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQE--ADLLLLDEPTTGLDAESRERIIALLAE 164
|
170 180
....*....|....*....|
gi 2316862561 503 YRG---ALLVVSHDPWFLRR 519
Cdd:NF040873 165 EHArgaTVVVVTHDLELVRR 184
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-175 |
3.74e-22 |
|
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: 95.88 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------------RVRYLAQQ 75
Cdd:COG1120 17 LDDVSLSLPPGEV-------------TALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 76 LEPADYPTVADLA--GVRPWLEALARieagsLDAADyeclgerwdiRQRLADALAAEGLGHLrADTPSERLSGGECMRVA 153
Cdd:COG1120 84 PPAPFGLTVRELValGRYPHLGLFGR-----PSAED----------REAVEEALERTGLEHL-ADRPVDELSGGERQRVL 147
|
170 180
....*....|....*....|..
gi 2316862561 154 LLGAFLDDADFLILDEPSNPLD 175
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLD 169
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
356-521 |
3.85e-22 |
|
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: 93.08 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTvGAAYLDQRLSLLDHGRGVLEQllevnrsrgeswl 435
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLPLEELRRRIGYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 436 rtrlaqlglpaerlaqpcatLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQYRG---ALLVVSH 512
Cdd:cd00267 81 --------------------LSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTH 138
|
....*....
gi 2316862561 513 DPWFLRRLG 521
Cdd:cd00267 139 DPELAELAA 147
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-513 |
8.89e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 98.81 E-value: 8.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 36 GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVR--YLAQ-QLEPADYpTVAD--LAGVRPWLEALA---RI------- 100
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERlgKLRQdQFAFEEF-TVLDtvIMGHTELWEVKQerdRIyalpems 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 101 EAGSLDAADYEclGERWDIRQRLADALAAEGLghLRADTPSERLSG-------GECMRVALLGAFLDDADFLILDEPSNP 173
Cdd:PRK15064 110 EEDGMKVADLE--VKFAEMDGYTAEARAGELL--LGVGIPEEQHYGlmsevapGWKLRVLLAQALFSNPDILLLDEPTNN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 174 LDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGGGYSFYAQSReeareaaerrldqrrlerkrq 252
Cdd:PRK15064 186 LDINTIRWLEDVLNERNSTMIIISHDRHFLNSVcTHMADLDYGELRVYPGNYDEYMTAA--------------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 253 TLAmreqqqrqerrqasgrREGKTANQAK----IL-LGGFRERSEVSAGKLRNA----HQAERERLDrEVREAAREveea 323
Cdd:PRK15064 245 TQA----------------RERLLADNAKkkaqIAeLQSFVSRFSANASKAKQAtsraKQIDKIKLE-EVKPSSRQ---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 324 SPLLLDSPDAELaaQRRIVELKGAVLPHLRGPL-REIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTC----A 398
Cdd:PRK15064 304 NPFIRFEQDKKL--HRNALEVENLTKGFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwseN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 399 VTVG------AAYLDQRLSLLD-----HGRGVLEQLLevnrsrgeswlRTRLAQLGLPAERLAQPCATLSGGER---LKA 464
Cdd:PRK15064 382 ANIGyyaqdhAYDFENDLTLFDwmsqwRQEGDDEQAV-----------RGTLGRLLFSQDDIKKSVKVLSGGEKgrmLFG 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2316862561 465 ALALvlyaDRPaQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHD 513
Cdd:PRK15064 451 KLMM----QKP-NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHD 494
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
356-520 |
5.21e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.46 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGA----------AYLDQRLSL------------- 412
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT--VRLFGkpprrarrriGYVPQRAEVdwdfpitvrdvvl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 413 --LDHGRGVLeqllevNRSRGESWLRTR--LAQLGLpAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHL 488
Cdd:COG1121 100 mgRYGRRGLF------RRPSRADREAVDeaLERVGL-EDLADRPIGELSGGQQQRVLLARALAQD--PDLLLLDEPFAGV 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2316862561 489 DLVARQALETMLRQYRG---ALLVVSHDPWFLRRL 520
Cdd:COG1121 171 DAATEEALYELLRELRRegkTILVVTHDLGAVREY 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-513 |
5.99e-21 |
|
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: 96.13 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 8 TLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPS---SGSVRRQGR-VRYLAQQLEPADYPT 83
Cdd:COG1123 21 AVDGVSLTIAPGETV-------------ALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdLLELSEALRGRRIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 84 V-----ADLAGVRPWLEALARIEAGSLDAADyeclgerwdIRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAF 158
Cdd:COG1123 88 VfqdpmTQLNPVTVGDQIAEALENLGLSRAE---------ARARVLELLEAVGLERRLDRYPHQ-LSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 159 LDDADFLILDEPSNPLDGPA----RALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELstlglrsygggysfyaqsree 233
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIaDRVVVM--------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 234 areaaerrldqrrlerkrqtlamreqqqrqerrqasgrregktaNQAKILLGGFRERSEVSAGKLrnahqAERERLDREV 313
Cdd:COG1123 217 --------------------------------------------DDGRIVEDGPPEEILAAPQAL-----AAVPRLGAAR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 314 REAAREVEEASPLLldspdaelaaqrrivELKGAVLPHLRGP------LREIDLLLSGPRRLALVGPNGSGKSTLLRLLA 387
Cdd:COG1123 248 GRAAPAAAAAEPLL---------------EVRNLSKRYPVRGkggvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 388 GQRAPLAGTcaVTV---------GAAYLDQR----------LSLLDHGRGVLEQL---LEVNRSRGESWLRTR----LAQ 441
Cdd:COG1123 313 GLLRPTSGS--ILFdgkdltklsRRSLRELRrrvqmvfqdpYSSLNPRMTVGDIIaepLRLHGLLSRAERRERvaelLER 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 442 LGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDL-VARQALETML---RQYRGALLVVSHD 513
Cdd:COG1123 391 VGLPPDLADRYPHELSGGQRQRVAIARAL-ALEP-KLLILDEPTSALDVsVQAQILNLLRdlqRELGLTYLFISHD 464
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
356-514 |
7.93e-21 |
|
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: 92.03 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGaaylDQRLSLLDHG-----RGVLEQLLEVN--- 427
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGE--VLLD----GRDLASLSRRelarrIAYVPQEPPAPfgl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 428 ---------RSRGESWLRTR-----------LAQLGLpaERLA-QPCATLSGGERLKAALALVLYADrpAQLLLLDEPDN 486
Cdd:COG1120 91 tvrelvalgRYPHLGLFGRPsaedreaveeaLERTGL--EHLAdRPVDELSGGERQRVLIARALAQE--PPLLLLDEPTS 166
|
170 180 190
....*....|....*....|....*....|....
gi 2316862561 487 HLDLvaRQALETM-----LRQYRG-ALLVVSHDP 514
Cdd:COG1120 167 HLDL--AHQLEVLellrrLARERGrTVVMVLHDL 198
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
9-172 |
3.37e-20 |
|
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: 87.32 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------------RVRYLAQQ 75
Cdd:pfam00005 1 LKNVSLTLNPGEIL-------------ALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 76 LEPADYPTVADLAGVRPWLEALARIEAGsldaadyeclgerwdirQRLADALAAEGLGHLRADTPSER---LSGGECMRV 152
Cdd:pfam00005 68 PQLFPRLTVRENLRLGLLLKGLSKREKD-----------------ARAEEALEKLGLGDLADRPVGERpgtLSGGQRQRV 130
|
170 180
....*....|....*....|
gi 2316862561 153 ALLGAFLDDADFLILDEPSN 172
Cdd:pfam00005 131 AIARALLTKPKLLLLDEPTA 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-513 |
4.56e-20 |
|
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: 93.70 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 35 TGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------RVR------YL----AQQLEPADYPTVADLAG------VR 91
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkRFRgtelqdYFkklaNGEIKVAHKPQYVDLIPkvfkgtVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 92 pwlEALARI-EAGSLDaadyeclgerwDIRQRLadalaaeGLGHLRaDTPSERLSGGECMRVALLGAFLDDADFLILDEP 170
Cdd:COG1245 182 ---ELLEKVdERGKLD-----------ELAEKL-------GLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 171 SNPLD--------------GPArallrarlaawDGGLLLVSHDRELLEGMQRIVELStlglrsYG--GGYSFYAQSReea 234
Cdd:COG1245 240 SSYLDiyqrlnvarlirelAEE-----------GKYVLVVEHDLAILDYLADYVHIL------YGepGVYGVVSKPK--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 235 reaaerrldqrrlerkrqtlamreqqqrqerrqasGRREGktANQakiLLGGFRERSEVsagKLRnahqaeRERLDREVR 314
Cdd:COG1245 300 -----------------------------------SVRVG--INQ---YLDGYLPEENV---RIR------DEPIEFEVH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 315 EAAREVEEasPLLLDSPDAElaaqrriVELKGAVLPHLRGPLR--EIdlllsgprrLALVGPNGSGKSTLLRLLAGQRAP 392
Cdd:COG1245 331 APRREKEE--ETLVEYPDLT-------KSYGGFSLEVEGGEIRegEV---------LGIVGPNGIGKTTFAKILAGVLKP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 393 LAGTCAVTVGAAYLDQRLSlLDHGRGVLEQLLEVNRSR-GESWLRTRLAQ-LGLpaERL-AQPCATLSGGERLKAALALV 469
Cdd:COG1245 393 DEGEVDEDLKISYKPQYIS-PDYDGTVEEFLRSANTDDfGSSYYKTEIIKpLGL--EKLlDKNVKDLSGGELQRVAIAAC 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2316862561 470 LyaDRPAQLLLLDEPDNHLD-----LVARqALETMLRQYRGALLVVSHD 513
Cdd:COG1245 470 L--SRDADLYLLDEPSAHLDveqrlAVAK-AIRRFAENRGKTAMVVDHD 515
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
356-520 |
1.11e-19 |
|
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: 88.16 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVG--------AAYLDQRLSLL----DH---GRGVL 420
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGE--VLVDgkditkknLRELRRKVGLVfqnpDDqlfAPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 421 EqllEV-----NRSRGESWLRTR----LAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLV 491
Cdd:COG1122 95 E---DVafgpeNLGLPREEIRERveeaLELVGL-EHLADRPPHELSGGQKQRVAIAGVL-AMEP-EVLVLDEPTAGLDPR 168
|
170 180 190
....*....|....*....|....*....|..
gi 2316862561 492 ARQALETMLRQYRGA---LLVVSHDPWFLRRL 520
Cdd:COG1122 169 GRRELLELLKRLNKEgktVIIVTHDLDLVAEL 200
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
356-514 |
5.82e-19 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 86.45 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV-----TVGAAYLDQRLSLLDHGRG------VLEQL- 423
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvRKEPREARRQIGVLPDERGlydrltVRENIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 ---------LEVNRSRGESWLrtRLAQLGLPAERLAQpcaTLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQ 494
Cdd:COG4555 97 yfaelyglfDEELKKRIEELI--ELLGLEEFLDRRVG---ELSTGMKKKVALARALVHD--PKVLLLDEPTNGLDVMARR 169
|
170 180
....*....|....*....|...
gi 2316862561 495 ALETMLRQYRG---ALLVVSHDP 514
Cdd:COG4555 170 LLREILRALKKegkTVLFSSHIM 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-513 |
1.02e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.48 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 35 TGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG---RV--RYLAQQLEpaDYptVADLAG--VRP-----WLEALARIEA 102
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVlkRFRGTELQ--NY--FKKLYNgeIKVvhkpqYVDLIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 103 GS----LDAADyeclgERWDIRQrLADALaaeGLGHLRaDTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD--G 176
Cdd:PRK13409 178 GKvrelLKKVD-----ERGKLDE-VVERL---GLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 177 PARALLRARLAAWDGGLLLVSHDRELLEGMQRIVELStlglrsYG--GGYSFYAQSReeareaaerrldqrrlerkrqtl 254
Cdd:PRK13409 248 RLNVARLIRELAEGKYVLVVEHDLAVLDYLADNVHIA------YGepGAYGVVSKPK----------------------- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 255 amreqqqrqerrqasGRREGktANQakiLLGGFrersevsagkLRNahqaERERL-DREVR--EAAREVEEASPLLLDSP 331
Cdd:PRK13409 299 ---------------GVRVG--INE---YLKGY----------LPE----ENMRIrPEPIEfeERPPRDESERETLVEYP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 332 DAElaaqrriVELKGAVLPHLRGPLR--EIdlllsgprrLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQR 409
Cdd:PRK13409 345 DLT-------KKLGDFSLEVEGGEIYegEV---------IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 410 LSLLDHGRgVLEQLLEVNRSRGESWLRTRLAQ-LGLPaERLAQPCATLSGGERLKAALALVLyaDRPAQLLLLDEPDNHL 488
Cdd:PRK13409 409 IKPDYDGT-VEDLLRSITDDLGSSYYKSEIIKpLQLE-RLLDKNVKDLSGGELQRVAIAACL--SRDADLYLLDEPSAHL 484
|
490 500 510
....*....|....*....|....*....|
gi 2316862561 489 D-----LVARqALETMLRQYRGALLVVSHD 513
Cdd:PRK13409 485 DveqrlAVAK-AIRRIAEEREATALVVDHD 513
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
369-513 |
2.88e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 83.96 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAV--------------TVGaaYLDQRLSLLDH--GRGVLE---QLLEVNRS 429
Cdd:COG1131 29 FGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpaevrrRIG--YVPQEPALYPDltVRENLRffaRLYGLPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 RGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQYRG---A 506
Cdd:COG1131 107 EARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHD--PELLILDEPTSGLDPEARRELWELLRELAAegkT 183
|
....*..
gi 2316862561 507 LLVVSHD 513
Cdd:COG1131 184 VLLSTHY 190
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
356-514 |
8.80e-18 |
|
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: 82.20 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVgaayLDQRLSLLDHGRGVLEQLLEVNRS------ 429
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS--IRV----FGKPLEKERKRIGYVPQRRSIDRDfpisvr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 -------RGESWLRTR------------LAQLGLpAERLAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDL 490
Cdd:cd03235 89 dvvlmglYGHKGLFRRlskadkakvdeaLERVGL-SELADRQIGELSGGQQQRVLLARALV--QDPDLLLLDEPFAGVDP 165
|
170 180
....*....|....*....|....*..
gi 2316862561 491 VARQALETMLRQYRG---ALLVVSHDP 514
Cdd:cd03235 166 KTQEDIYELLRELRRegmTILVVTHDL 192
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-175 |
9.81e-18 |
|
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: 81.74 E-value: 9.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQLE----- 77
Cdd:cd03225 11 DGARPALDDISLTIKKGE-------------FVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 78 ------PAD---YPTVA-DLA-GvrpwLEALARIEAgsldaadyeclgerwDIRQRLADALAAEGLGHLRaDTPSERLSG 146
Cdd:cd03225 78 glvfqnPDDqffGPTVEeEVAfG----LENLGLPEE---------------EIEERVEEALELVGLEGLR-DRSPFTLSG 137
|
170 180
....*....|....*....|....*....
gi 2316862561 147 GECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-209 |
2.24e-17 |
|
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: 80.60 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG------------RVRYLAQQL 76
Cdd:COG4133 18 FSGLSFTLAAGEALA-------------LTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 EPADYPTVADlagvrpWLEALARIEAGSLDAADyeclgerwdirqrLADALAAEGLGHLrADTPSERLSGGECMRVALLG 156
Cdd:COG4133 85 GLKPELTVRE------NLRFWAALYGLRADREA-------------IDEALEAVGLAGL-ADLPVRQLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 157 AFLDDADFLILDEPSNPLDGPARALLRARLAAW--DGGL-LLVSHDRELLEGMQRI 209
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlaRGGAvLLTTHQPLELAAARVL 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-205 |
2.33e-17 |
|
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: 81.04 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG--------RVRYLAQQLE-PA 79
Cdd:cd03235 15 LEDVSFEVKPGEF-------------LAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSiDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 80 DYP-TVADLAGVRPWLEalaRIEAGSLDAADyeclgerwdiRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAF 158
Cdd:cd03235 82 DFPiSVRDVVLMGLYGH---KGLFRRLSKAD----------KAKVDEALERVGLSELADRQIGE-LSGGQQQRVLLARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316862561 159 LDDADFLILDEPSNPLDGPARALLRARLAAW--DG-GLLLVSHDRELLEG 205
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLE 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-175 |
2.71e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 81.29 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 1 MTNTSTLTLDGVSFQLpDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG--------RVRY 71
Cdd:COG1121 1 MMMMPAIELENLTVSY-GGRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 72 LAQQLE-PADYP-TVAD-----LAGVRPWLealarieaGSLDAADyeclgerwdiRQRLADALAAEGLGHLrADTPSERL 144
Cdd:COG1121 80 VPQRAEvDWDFPiTVRDvvlmgRYGRRGLF--------RRPSRAD----------REAVDEALERVGLEDL-ADRPIGEL 140
|
170 180 190
....*....|....*....|....*....|.
gi 2316862561 145 SGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-486 |
3.51e-17 |
|
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: 78.46 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGT-------------CAVTVGAAYLDQRLSLLDHGRgVLEQ 422
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltdderKSLRKEIGYVFQDPQLFPRLT-VREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 423 LLEVNRSRGES---------WLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDN 486
Cdd:pfam00005 80 LRLGLLLKGLSkrekdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALL--TKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-212 |
4.15e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 80.25 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLpDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------------RVRYL 72
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAgECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 73 AQqlEPADYP-TVADlagvrpwleALARIeagsldaadYECLGERWDiRQRLADALAAEGLGHLRADTPSERLSGGECMR 151
Cdd:COG4619 80 PQ--EPALWGgTVRD---------NLPFP---------FQLRERKFD-RERALELLERLGLPPDILDKPVERLSGGERQR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 152 VALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAW----DGGLLLVSHDRELLEGM-QRIVEL 212
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVaDRVLTL 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
356-513 |
5.00e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.93 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCavtvgaAYLDQRLSLLDHG-----RGVLEQ-------- 422
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV------RLNGRPLAAWSPWelarrRAVLPQhsslafpf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 -LLEVNRSRGESWLRTRLAQLGLPAERLAQ---------PCATLSGGERLKAALALVLY-----ADRPAQLLLLDEPDNH 487
Cdd:COG4559 91 tVEEVVALGRAPHGSSAAQDRQIVREALALvglahlagrSYQTLSGGEQQRVQLARVLAqlwepVDGGPRWLFLDEPTSA 170
|
170 180
....*....|....*....|....*....
gi 2316862561 488 LDLVARQALETMLRQY---RGALLVVSHD 513
Cdd:COG4559 171 LDLAHQHAVLRLARQLarrGGGVVAVLHD 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
368-520 |
6.69e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.85 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAG--------------------QRAP---LAGTC--AVTVG----AAYLDQ--RLSLL--- 413
Cdd:PRK11147 31 RVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlQQDPprnVEGTVydFVAEGieeqAEYLKRyhDISHLvet 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 414 DHGRGVLEQLLEV-------NRSRGESWLRTRLAQLGLPAErlaQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDN 486
Cdd:PRK11147 111 DPSEKNLNELAKLqeqldhhNLWQLENRINEVLAQLGLDPD---AALSSLSGGWLRKAALGRALVSN--PDVLLLDEPTN 185
|
170 180 190
....*....|....*....|....*....|....
gi 2316862561 487 HLDLVARQALETMLRQYRGALLVVSHDPWFLRRL 520
Cdd:PRK11147 186 HLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNM 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-175 |
7.73e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 80.11 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG------------RVRYLAQql 76
Cdd:COG1131 16 LDGVSLTVEPGEI-------------FGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 EPADYP--TVADLagvrpwLEALARIEAGSLDAAdyeclgerwdiRQRLADALAAEGLGHlRADTPSERLSGGECMRVAL 154
Cdd:COG1131 81 EPALYPdlTVREN------LRFFARLYGLPRKEA-----------RERIDELLELFGLTD-AADRKVGTLSGGMKQRLGL 142
|
170 180
....*....|....*....|.
gi 2316862561 155 LGAFLDDADFLILDEPSNPLD 175
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLD 163
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-175 |
1.99e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLfSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-------------VR 70
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLL-HPLSLTFPAgKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 71 YLAQQLEPADYPTVADLA--GVRPWLEALARieagsLDAADyeclgerwdiRQRLADALAAEGLGHLrADTPSERLSGGE 148
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVaiGRYPWHGALGR-----FGAAD----------REKVEEAISLVGLKPL-AHRLVDSLSGGE 152
|
170 180
....*....|....*....|....*..
gi 2316862561 149 CMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-520 |
2.19e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 78.63 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 351 HLRG-----PLREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLD------------------ 407
Cdd:COG4778 17 HLQGgkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDlaqaspreilalrrrtig 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 408 ---Q------RLSLLDHgrgVLEQLLEVNRSRGESWLRTR--LAQLGLPaERLAQ-PCATLSGGERLKAALALVLYADRP 475
Cdd:COG4778 97 yvsQflrvipRVSALDV---VAEPLLERGVDREEARARARelLARLNLP-ERLWDlPPATFSGGEQQRVNIARGFIADPP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316862561 476 aqLLLLDEPDNHLDLVARQALETMLRQY--RG-ALLVVSHDPWFLRRL 520
Cdd:COG4778 173 --LLLLDEPTASLDAANRAVVVELIEEAkaRGtAIIGIFHDEEVREAV 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-212 |
7.94e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 18 DGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG--RVRYLAQQLE-PADYP-TVADLAGVRP 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAgSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSEvPDSLPlTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 93 WLEalaRIEAGSLDAADyeclgerwdiRQRLADALAAEGLGHLrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSN 172
Cdd:NF040873 83 WAR---RGLWRRLTRDD----------RAAVDDALERVGLADL-AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316862561 173 PLDGPARALLRARLAAWDG---GLLLVSHDRELLEGMQRIVEL 212
Cdd:NF040873 149 GLDAESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
360-521 |
1.09e-15 |
|
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: 75.99 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 360 DLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTC---AVTVGAA--------YLDQRLSLLDH---------GRGV 419
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlinGVDVTAAppadrpvsMLFQENNLFAHltveqnvglGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 420 LEQLLEVNRSRGESwlrtRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETM 499
Cdd:cd03298 98 GLKLTAEDRQAIEV----ALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKP--VLLLDEPFAALDPALRAEMLDL 170
|
170 180
....*....|....*....|....*.
gi 2316862561 500 L----RQYRGALLVVSHDPWFLRRLG 521
Cdd:cd03298 171 VldlhAETKMTVLMVTHQPEDAKRLA 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-205 |
1.47e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 79.90 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 13 SFQLPDGSLLFSDLDETFD-TRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQLEPADYptvADLAgVR 91
Cdd:PLN03073 515 SFGYPGGPLLFKNLNFGIDlDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDG---LDLS-SN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 92 PWLeALARIEAGSLDaadyeclgerwdirQRLADALAAEGLGHLRADTPSERLSGGECMRVALLGAFLDDADFLILDEPS 171
Cdd:PLN03073 591 PLL-YMMRCFPGVPE--------------QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190
....*....|....*....|....*....|....
gi 2316862561 172 NPLDGPARALLRARLAAWDGGLLLVSHDRELLEG 205
Cdd:PLN03073 656 NHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG 689
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
356-513 |
1.81e-15 |
|
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: 74.36 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVtvgaayldqrlslldHGRGVLEQLLEVNRsrgeswl 435
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV---------------LGKDIKKEPEEVKR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 436 rtrlaQLGLPAERLAQP-------CATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQYR---G 505
Cdd:cd03230 74 -----RIGYLPEEPSLYenltvreNLKLSGGMKQRLALAQALLHD--PELLILDEPTSGLDPESRREFWELLRELKkegK 146
|
....*...
gi 2316862561 506 ALLVVSHD 513
Cdd:cd03230 147 TILLSSHI 154
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-212 |
1.86e-15 |
|
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: 79.25 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPADYPT 83
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPgERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP---LADADADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 84 VADLAGVRPWLEA---LARIEAGSLDAADYEClgERWDIRQRLADALAAEGLG-HLRADTPSERLSGGECMRVALLGAFL 159
Cdd:TIGR02857 397 QIAWVPQHPFLFAgtiAENIRLARPDASDAEI--REALERAGLDEFVAALPQGlDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 160 DDADFLILDEPSNPLDGPARALLRARLAAWDGG--LLLVSHDRELLEGMQRIVEL 212
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAALADRIVVL 529
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-513 |
2.75e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 75.52 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGA-AYLDQRLSLLDHGRgVLEQLLEVNRSRGE-SWLRTRLAQ-LGLp 445
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvSYKPQYIKADYEGT-VRDLLSSITKDFYThPYFKTEIAKpLQI- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 446 aERLA-QPCATLSGGERLKAALALVLyaDRPAQLLLLDEPDNHLDLVARQALETMLRQY----RGALLVVSHD 513
Cdd:cd03237 106 -EQILdREVPELSGGELQRVAIAACL--SKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHD 175
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-212 |
3.88e-15 |
|
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: 78.26 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 2 TNTSTLTLDGVSFQLPDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlEPAD 80
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPgERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV--------DLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 YPTVAdlagvrpWLEALA------RIEAGSLdaADYECLGERWDIRQRLADALAAEGLGHLRA------DTP----SERL 144
Cdd:COG4988 404 LDPAS-------WRRQIAwvpqnpYLFAGTI--RENLRLGRPDASDEELEAALEAAGLDEFVAalpdglDTPlgegGRGL 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 145 SGGECMRVALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAWDGG--LLLVSHDRELLEGMQRIVEL 212
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQADRILVL 544
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-175 |
5.61e-15 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 74.51 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG------------RVRYLAQQL 76
Cdd:COG4555 17 LKDVSFTAKDGEI-------------TGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 EPADYPTVadlagvRPWLEALARIeAGSLDAAdyeclgerwdIRQRLADALAAEGLGHLRaDTPSERLSGGECMRVALLG 156
Cdd:COG4555 84 GLYDRLTV------RENIRYFAEL-YGLFDEE----------LKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALAR 145
|
170
....*....|....*....
gi 2316862561 157 AFLDDADFLILDEPSNPLD 175
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLD 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
358-514 |
7.41e-15 |
|
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: 73.48 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 358 EIDLLLSGPRrLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV--TV---------------GAAYLDQRLSLLDHgRGVL 420
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngTVlfdsrkkinlppqqrKIGLVFQQYALFPH-LNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 421 EQLLEVNRSRGESWLRTRLAQ----LGLpAERLAQPCATLSGGERLKAALALVLyADRPAqLLLLDEP----DNHLDLVA 492
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDElldlLGL-DHLLNRYPAQLSGGEKQRVALARAL-AAQPE-LLLLDEPfsalDRALRLQL 170
|
170 180
....*....|....*....|..
gi 2316862561 493 RQALETMLRQYRGALLVVSHDP 514
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDL 192
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
311-514 |
9.75e-15 |
|
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: 77.11 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 311 REVREAAR---EVEEASPLLLDSPDAELAAQRRIVELKGAVLPHLRGP---LREIDLLLSGPRRLALVGPNGSGKSTLLR 384
Cdd:COG4987 300 GRVRAAARrlnELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGrpvLDGLSLTLPPGERVAIVGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 385 LLAGQRAPLAGTcaVTVG---------------AAYLDQRLSLLDHgrGVLEQLLEVNRSRGESWLRTRLAQLGLpAERL 449
Cdd:COG4987 380 LLLRFLDPQSGS--ITLGgvdlrdldeddlrrrIAVVPQRPHLFDT--TLRENLRLARPDATDEELWAALERVGL-GDWL 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316862561 450 AQPC-----------ATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLV-ARQALETMLRQYRG-ALLVVSHDP 514
Cdd:COG4987 455 AALPdgldtwlgeggRRLSGGERRRLALARALLRDAP--ILLLDEPTEGLDAAtEQALLADLLEALAGrTVLLITHRL 530
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-176 |
1.10e-14 |
|
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: 73.06 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 8 TLDGVSFQLPDGSLLFSDLDetFDTRH---TGLVGRNGVGKSLLARLLAGHLQPSSGSV----------RRQGRVRYLAQ 74
Cdd:cd03226 1 RIENISFSYKKGTEILDDLS--LDLYAgeiIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikakERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 75 qlEPADYptvadLAGVRPWLEALARIEAGSLDAADYECLGERWDIRQrLADAlaaeglgHLRAdtpserLSGGECMRVAL 154
Cdd:cd03226 79 --DVDYQ-----LFTDSVREELLLGLKELDAGNEQAETVLKDLDLYA-LKER-------HPLS------LSGGQKQRLAI 137
|
170 180
....*....|....*....|..
gi 2316862561 155 LGAFLDDADFLILDEPSNPLDG 176
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDY 159
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-175 |
1.19e-14 |
|
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: 73.00 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLfSDLDETFDTRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG------------RVRYLAQ 74
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 75 QLEPadYPTVADLAGVRpWLEALARIEAGsldaadyeclgerwDIRQRLADALAAEGLGHlRADTPSERLSGGECMRVAL 154
Cdd:cd03264 80 EFGV--YPNFTVREFLD-YIAWLKGIPSK--------------EVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGI 141
|
170 180
....*....|....*....|.
gi 2316862561 155 LGAFLDDADFLILDEPSNPLD 175
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLD 162
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
356-520 |
1.46e-14 |
|
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: 73.68 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV---------------TVGAAYLDQRLSLldHGR-GV 419
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrrkafrrRVQMVFQDPYASL--HPRhTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 420 LEQLLEVNRSRGESWLRTR----LAQLGLPAERLAQPCATLSGGERLKAAL--ALVLyadRPaQLLLLDEPDNHLDLVAr 493
Cdd:COG1124 99 DRILAEPLRIHGLPDREERiaelLEQVGLPPSFLDRYPHQLSGGQRQRVAIarALIL---EP-ELLLLDEPTSALDVSV- 173
|
170 180 190
....*....|....*....|....*....|..
gi 2316862561 494 QA-----LETMLRQYRGALLVVSHDPWFLRRL 520
Cdd:COG1124 174 QAeilnlLKDLREERGLTYLFVSHDLAVVAHL 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-212 |
1.53e-14 |
|
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: 76.34 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGS-LLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqQLEPADYPT 83
Cdd:COG4987 333 SLELEDVSFRYPGAGrPVLDGLSLTLPPgERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV------DLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 84 VADLAGV---RPWLEA--------LARIEAGslDAAdyeclgerwdirqrLADALAAEGLGHLRADTPS----------E 142
Cdd:COG4987 407 LRRRIAVvpqRPHLFDttlrenlrLARPDAT--DEE--------------LWAALERVGLGDWLAALPDgldtwlgeggR 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 143 RLSGGECMRVALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAWDGG--LLLVSHDRELLEGMQRIVEL 212
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLERMDRILVL 542
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
360-513 |
1.53e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.51 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 360 DLLLSGP--RRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV------TVGAAYLDQRLSLLDHGRGVLE-----QLLEV 426
Cdd:PRK11231 20 DLSLSLPtgKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgdkpisMLSSRQLARRLALLPQHHLTPEgitvrELVAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 427 NRSrgeSWL-------------------RTRLAQLglpAERlaqPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNH 487
Cdd:PRK11231 100 GRS---PWLslwgrlsaednarvnqameQTRINHL---ADR---RLTDLSGGQRQRAFLAMVLAQDTP--VVLLDEPTTY 168
|
170 180
....*....|....*....|....*....
gi 2316862561 488 LDLVARQALETMLRQYRGA---LLVVSHD 513
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQgktVVTVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-175 |
1.91e-14 |
|
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: 71.70 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptvaDLA 88
Cdd:cd03214 15 LDDLSLSIEAGEI-------------VGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK-----------------DLA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPwlEALARIEAgsldaadYeclgerwdirqrLADALAAEGLGHLrADTPSERLSGGECMRVALLGAFLDDADFLILD 168
Cdd:cd03214 65 SLSP--KELARKIA-------Y------------VPQALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
....*..
gi 2316862561 169 EPSNPLD 175
Cdd:cd03214 123 EPTSHLD 129
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
356-514 |
3.28e-14 |
|
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: 70.49 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGaaylDQRLSLLDHGR-----GVLEQllevnrsr 430
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE--ILID----GVDLRDLDLESlrkniAYVPQ-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 431 gESWLRTrlaqlGLPAERLaqpcatLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQYRG--ALL 508
Cdd:cd03228 84 -DPFLFS-----GTIRENI------LSGGQRQRIAIARALLRDPP--ILILDEATSALDPETEALILEALRALAKgkTVI 149
|
....*.
gi 2316862561 509 VVSHDP 514
Cdd:cd03228 150 VIAHRL 155
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
369-514 |
4.12e-14 |
|
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: 71.37 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAV-------------------TVGaaYLDQRLSLLDHgRGVLE------QL 423
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdisklsekelaafrrrHIG--FVFQSFNLLPD-LTALEnvelplLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 LEVNRSRGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLR-- 501
Cdd:cd03255 110 AGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARAL-ANDP-KIILADEPTGNLDSETGKEVMELLRel 186
|
170
....*....|....*
gi 2316862561 502 --QYRGALLVVSHDP 514
Cdd:cd03255 187 nkEAGTTIVVVTHDP 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
356-514 |
4.31e-14 |
|
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: 74.79 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGA---------------AYLDQRlSLLDHGRgVL 420
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS--ILINGvdlsdldpaswrrqiAWVPQN-PYLFAGT-IR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 421 EQLLEVNRSRGESWLRTRLAQLGLPA--ERLAQPCAT--------LSGGERLKAALALVLYADRPaqLLLLDEPDNHLDL 490
Cdd:COG4988 429 ENLRLGRPDASDEELEAALEAAGLDEfvAALPDGLDTplgeggrgLSGGQAQRLALARALLRDAP--LLLLDEPTAHLDA 506
|
170 180
....*....|....*....|....*.
gi 2316862561 491 VARQAL-ETMLRQYRGA-LLVVSHDP 514
Cdd:COG4988 507 ETEAEIlQALRRLAKGRtVILITHRL 532
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
369-513 |
4.45e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.11 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTvGAAYLDQRLSLLDHGRGVLEQ---------LLEVNRSRGESWLRTRL 439
Cdd:PRK13548 31 VAILGPNGAGKSTLLRALSGELSPDSGEVRLN-GRPLADWSPAELARRRAVLPQhsslsfpftVEEVVAMGRAPHGLSRA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 440 AQLGLPAERLAQ---------PCATLSGGERLKAALALVL----YADRPAQLLLLDEPDNHLDLVARQALETMLRQY--- 503
Cdd:PRK13548 110 EDDALVAAALAQvdlahlagrDYPQLSGGEQQRVQLARVLaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLahe 189
|
170
....*....|.
gi 2316862561 504 -RGALLVVSHD 513
Cdd:PRK13548 190 rGLAVIVVLHD 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-170 |
4.62e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.43 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG--------RVRYLAQqlEPAD 80
Cdd:COG1116 27 LDDVSLTVAAGEF-------------VALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQ--EPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 YPtvadlagvrpWLEALARIEAGsLDAADYEclgeRWDIRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAFLD 160
Cdd:COG1116 92 LP----------WLTVLDNVALG-LELRGVP----KAERRERARELLELVGLAGFEDAYPHQ-LSGGMRQRVAIARALAN 155
|
170
....*....|
gi 2316862561 161 DADFLILDEP 170
Cdd:COG1116 156 DPEVLLMDEP 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
367-517 |
5.66e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.82 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 367 RRLALVGPNGSGKSTLLRLLAGQRAPLAG--TCAVTVGAAYLDQRLSLLDHG------------RGVLEQLLEVN-RSRG 431
Cdd:PRK10636 28 QKVGLVGKNGCGKSTLLALLKNEISADGGsyTFPGNWQLAWVNQETPALPQPaleyvidgdreyRQLEAQLHDANeRNDG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 432 -------------ESW-LRTRLAQL----GLPAERLAQPCATLSGG--ERLKAALALVLYADrpaqLLLLDEPDNHLDLV 491
Cdd:PRK10636 108 haiatihgkldaiDAWtIRSRAASLlhglGFSNEQLERPVSDFSGGwrMRLNLAQALICRSD----LLLLDEPTNHLDLD 183
|
170 180
....*....|....*....|....*.
gi 2316862561 492 ARQALETMLRQYRGALLVVSHDPWFL 517
Cdd:PRK10636 184 AVIWLEKWLKSYQGTLILISHDRDFL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-175 |
6.38e-14 |
|
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: 70.96 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR--------VRYLAQQlepad 80
Cdd:cd03293 20 LEDISLSVEEGEFV-------------ALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQ----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 yptvadlAGVRPWLEALARIEAGsldaadYECLGERWDIRQRLADALAAE-GLGHLRADTPSErLSGGECMRVALLGAFL 159
Cdd:cd03293 82 -------DALLPWLTVLDNVALG------LELQGVPKAEARERAEELLELvGLSGFENAYPHQ-LSGGMRQRVALARALA 147
|
170
....*....|....*.
gi 2316862561 160 DDADFLILDEPSNPLD 175
Cdd:cd03293 148 VDPDVLLLDEPFSALD 163
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-175 |
1.05e-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: 70.90 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 36 GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-RVRYLAQQLEPaDYP-TVADLagvrpwleaLARIEAGSLDAADYecl 113
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKA-DYEgTVRDL---------LSSITKDFYTHPYF--- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 114 gerwdiRQRLADALAAEGLghlrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03237 96 ------KTEIAKPLQIEQI----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
356-513 |
1.44e-13 |
|
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: 70.19 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV--------TVGAAYLDQRLSLLDHgRGVLEQL---L 424
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtgpGPDRGYVFQQDALLPW-LTVLDNValgL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 425 EVNR-SRGESWLRTR--LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLD----LVARQALE 497
Cdd:cd03293 99 ELQGvPKAEARERAEelLELVGLSGFENAYP-HQLSGGMRQRVALARAL-AVDP-DVLLLDEPFSALDaltrEQLQEELL 175
|
170
....*....|....*.
gi 2316862561 498 TMLRQYRGALLVVSHD 513
Cdd:cd03293 176 DIWRETGKTVLLVTHD 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
358-514 |
1.44e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.17 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 358 EIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGT---CAVTVGAAYLDQR-LSLL--DH--------------GR 417
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilwNGQDLTALPPAERpVSMLfqENnlfphltvaqniglGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 418 GVLEQLLEVNRSRgeswLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEP---------DNHL 488
Cdd:COG3840 97 RPGLKLTAEQRAQ----VEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRP--ILLLDEPfsaldpalrQEML 169
|
170 180
....*....|....*....|....*.
gi 2316862561 489 DLVARQALETMLrqyrgALLVVSHDP 514
Cdd:COG3840 170 DLVDELCRERGL-----TVLMVTHDP 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-175 |
1.53e-13 |
|
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: 70.44 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRV------RYLAQ-------- 74
Cdd:cd03267 37 LKGISFTIEKGEIV-------------GFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkKFLRRigvvfgqk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 75 -QLepadyptVADLAgVRPWLEALARIEagSLDAADYeclGERwdiRQRLADALAaegLGHLrADTPSERLSGGECMRVA 153
Cdd:cd03267 104 tQL-------WWDLP-VIDSFYLLAAIY--DLPPARF---KKR---LDELSELLD---LEEL-LDTPVRQLSLGQRMRAE 163
|
170 180
....*....|....*....|..
gi 2316862561 154 LLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLD 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-213 |
2.16e-13 |
|
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: 69.77 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 2 TNTSTLT-LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaQQLEPAD 80
Cdd:COG4181 20 TGAGELTiLKGISLEVEAGESV-------------AIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG------QDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 YptvadlagvrpwlEALARIEAG-------------SLDAADY-----ECLGERwDIRQRLADALAAEGLGHLRADTPSE 142
Cdd:COG4181 81 E-------------DARARLRARhvgfvfqsfqllpTLTALENvmlplELAGRR-DARARARALLERVGLGHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 143 rLSGGECMRVALLGAFLDDADFLILDEPSNPLDGPArallrarlaawdgG-----------------LLLVSHDRELLEG 205
Cdd:COG4181 147 -LSGGEQQRVALARAFATEPAILFADEPTGNLDAAT-------------GeqiidllfelnrergttLVLVTHDPALAAR 212
|
....*...
gi 2316862561 206 MQRIVELS 213
Cdd:COG4181 213 CDRVLRLR 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
356-521 |
2.37e-13 |
|
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: 68.37 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYL-DQRLSLLDHGR--GVLEQLLEVNrsrge 432
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS--ILIDGEDLtDLEDELPPLRRriGMVFQDFALF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 433 SWLrTRLAQLGLPaerlaqpcatLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQYRG----ALL 508
Cdd:cd03229 89 PHL-TVLENIALG----------LSGGQQQRVALARALAMD--PDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVV 155
|
170
....*....|...
gi 2316862561 509 VVSHDPWFLRRLG 521
Cdd:cd03229 156 LVTHDLDEAARLA 168
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-213 |
3.38e-13 |
|
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: 69.06 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlePADYP 82
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVA-------------IVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT---------DISKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADLAGVR--------------PWLEALARIEAGSLDAADyeclgERWDIRQRLADALAAEGLGHLRADTPSErLSGGE 148
Cdd:cd03255 72 SEKELAAFRrrhigfvfqsfnllPDLTALENVELPLLLAGV-----PKKERRERAEELLERVGLGDRLNHYPSE-LSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 149 CMRVALLGAFLDDADFLILDEPSNPLD---GPARALLRARLAAWDG-GLLLVSHDRELLEGMQRIVELS 213
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDsetGKEVMELLRELNKEAGtTIVVVTHDPELAEYADRIIELR 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-175 |
3.55e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.14 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqQLEPAD-------- 80
Cdd:COG4152 17 VDDVSFTVPKGEI-------------FGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE------PLDPEDrrrigylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 -----YP--TVADLagvrpwLEALARIEaGsLDAAdyeclgerwDIRQRLADALAAEGLGHlRADTPSERLSGGECMRVA 153
Cdd:COG4152 78 eerglYPkmKVGEQ------LVYLARLK-G-LSKA---------EAKRRADEWLERLGLGD-RANKKVEELSKGNQQKVQ 139
|
170 180
....*....|....*....|..
gi 2316862561 154 LLGAFLDDADFLILDEPSNPLD 175
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLD 161
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
356-514 |
3.94e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.92 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVG----AAYLDQRLSLLdhgRG------------- 418
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE--VLIDgqdiSSLSERELARL---RRrhigfvfqffnll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 419 ----VLE------QLLEVNRSRGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHL 488
Cdd:COG1136 99 peltALEnvalplLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALVNR--PKLILADEPTGNL 175
|
170 180 190
....*....|....*....|....*....|
gi 2316862561 489 DLV-ARQALETML---RQYRGALLVVSHDP 514
Cdd:COG1136 176 DSKtGEEVLELLRelnRELGTTIVMVTHDP 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-212 |
4.42e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.54 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVR---------RQGRVRYLAQQLEP- 78
Cdd:COG2884 18 LSDVSLEIEKGEFVF-------------LTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIPYLRRRIGVv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 79 -ADYP-----TVAD---LAgvrpwLEALARIEAgsldaadyeclgerwDIRQRLADALAAEGLGHlRADTPSERLSGGEC 149
Cdd:COG2884 85 fQDFRllpdrTVYEnvaLP-----LRVTGKSRK---------------EIRRRVREVLDLVGLSD-KAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 150 MRVALLGAFLDDADFLILDEPSNPLDgparallrarlaaWDGGL----------------LLVSHDRELLEGMQ-RIVEL 212
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLD-------------PETSWeimelleeinrrgttvLIATHDLELVDRMPkRVLEL 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
356-514 |
4.87e-13 |
|
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: 68.31 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGT---CAVTVGA--------AYLDQRLSLLDHgRGVLEQL- 423
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEiliDGRDVTGvpperrniGMVFQDYALFPH-LTVAENIa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 --LEVNRSRGESW---LRTRLAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALET 498
Cdd:cd03259 95 fgLKLRGVPKAEIrarVRELLELVGLEGLLNRYP-HELSGGQQQRVALARAL-AREP-SLLLLDEPLSALDAKLREELRE 171
|
170 180
....*....|....*....|
gi 2316862561 499 MLRQYRGAL----LVVSHDP 514
Cdd:cd03259 172 ELKELQRELgittIYVTHDQ 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
368-520 |
5.20e-13 |
|
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: 68.69 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGA---AYLDQRL----------------SLLDHGRGVLEQLLEVNR 428
Cdd:cd03257 33 TLGLVGESGSGKSTLARAILGLLKPTSGS--IIFDGkdlLKLSRRLrkirrkeiqmvfqdpmSSLNPRMTIGEQIAEPLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 429 SRGESWLRTR--------LAQLGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLD-LVARQALETM 499
Cdd:cd03257 111 IHGKLSKKEArkeavlllLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL-ALNP-KLLIADEPTSALDvSVQAQILDLL 188
|
170 180
....*....|....*....|....
gi 2316862561 500 LR---QYRGALLVVSHDPWFLRRL 520
Cdd:cd03257 189 KKlqeELGLTLLFITHDLGVVAKI 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
311-514 |
5.60e-13 |
|
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: 71.24 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 311 REVREAAREVEEASPLLLDSPDAELAAQRRIV------ELKGAVLPHLRGP--LREIDLLLSGPRRLALVGPNGSGKSTL 382
Cdd:TIGR02868 298 TRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGlgkptlELRDLSAGYPGAPpvLDGVSLDLPPGERVAILGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 383 LRLLAGQRAPLAGT-------------CAVTVGAAYLDQRLSLLD----------HGRGVLEQLLEVNRSRG-ESWLRTR 438
Cdd:TIGR02868 378 LATLAGLLDPLQGEvtldgvpvssldqDEVRRRVSVCAQDAHLFDttvrenlrlaRPDATDEELWAALERVGlADWLRAL 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316862561 439 LAQLGlpaERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDL-VARQALETMLRQYRG-ALLVVSHDP 514
Cdd:TIGR02868 458 PDGLD---TVLGEGGARLSGGERQRLALARALLADAP--ILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHHL 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-230 |
5.73e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.08 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLpDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVR--RQGRVRYLAQQLEpADYP- 82
Cdd:PRK15064 320 LEVENLTKGF-DNGPLFKNLNLLLEAgERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsENANIGYYAQDHA-YDFEn 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 --TVADlagvrpWLEalarieagsldaadyeclgeRWdiRQRLADALAAEG-LGHL-----RADTPSERLSGGECMRVaL 154
Cdd:PRK15064 398 dlTLFD------WMS--------------------QW--RQEGDDEQAVRGtLGRLlfsqdDIKKSVKVLSGGEKGRM-L 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316862561 155 LGAF-LDDADFLILDEPSNPLDGPARALLRARLAAWDGGLLLVSHDRELLEGM-QRIVELSTLGLRSYGGGYSFYAQS 230
Cdd:PRK15064 449 FGKLmMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLaTRIIEITPDGVVDFSGTYEEYLRS 526
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-212 |
6.52e-13 |
|
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: 67.82 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG---------RVRYLAQQL 76
Cdd:cd03292 14 TAALDGINISISAGEFVF-------------LVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 EPA--DYPTVADLAGVRPWLEALARIEAGsldaadyeclgeRWDIRQRLADALAAEGLGHLRADTPSErLSGGECMRVAL 154
Cdd:cd03292 81 GVVfqDFRLLPDRNVYENVAFALEVTGVP------------PREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 155 LGAFLDDADFLILDEPSNPLDGPARALLRARLAAWD--GGLLLVS-HDRELLEGMQ-RIVEL 212
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRhRVIAL 209
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
370-514 |
9.50e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQRLSLLDH--GRGVLEQLLEVnrsrgeswlrtrLAQLGL--P 445
Cdd:COG2401 60 LIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAigRKGDFKDAVEL------------LNAVGLsdA 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 446 AERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLD-----LVARqALETMLRQYRGALLVVSHDP 514
Cdd:COG2401 128 VLWLRRF-KELSTGQKFRFRLALLL-AERP-KLLVIDEFCSHLDrqtakRVAR-NLQKLARRAGITLVVATHHY 197
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-212 |
9.80e-13 |
|
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: 68.29 E-value: 9.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVR-------------RQGRVRYLAQQ 75
Cdd:COG1124 21 LKDVSLEVAPG--------ESF-----GLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrkaFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 76 LEPADYP--TVADLAGvrpwlEALArieagsldaadyeCLGERwDIRQRLADALAAEGLG-HLRADTPSErLSGGECMRV 152
Cdd:COG1124 88 PYASLHPrhTVDRILA-----EPLR-------------IHGLP-DREERIAELLEQVGLPpSFLDRYPHQ-LSGGQRQRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLDGPARAL----LRARLAAWDGGLLLVSHDRELLEGM-QRIVEL 212
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEilnlLKDLREERGLTYLFVSHDLAVVAHLcDRVAVM 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
368-529 |
1.03e-12 |
|
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: 68.19 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGtCAVTV-----------------G------AAYLDQRLSLLD------HG-R 417
Cdd:COG1119 31 HWAILGPNGAGKSTLLSLITGDLPPTYG-NDVRLfgerrggedvwelrkriGlvspalQLRFPRDETVLDvvlsgfFDsI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 418 GVLEQLLEVNRSRGESWLrtrlAQLGLpAERLAQPCATLSGGERLKAALALVLYADrPaQLLLLDEPDNHLDLVARQALE 497
Cdd:COG1119 110 GLYREPTDEQRERARELL----ELLGL-AHLADRPFGTLSQGEQRRVLIARALVKD-P-ELLILDEPTAGLDLGARELLL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316862561 498 TMLRQYRG----ALLVVSHD-----PWFLRRLGLD--GVLAAG 529
Cdd:COG1119 183 ALLDKLAAegapTLVLVTHHveeipPGITHVLLLKdgRVVAAG 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-212 |
1.06e-12 |
|
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: 66.25 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGS-LLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGsvrrqgrvrylaqqlepadyptv 84
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPgEKVAIVGPSGSGKSTLLKLLLRLYDPTSG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 85 adlagvrpwlealaRIEAGSLDAADYEclgeRWDIRQRLA----DAlaaeglgHLRADTPSER-LSGGECMRVALLGAFL 159
Cdd:cd03228 58 --------------EILIDGVDLRDLD----LESLRKNIAyvpqDP-------FLFSGTIRENiLSGGQRQRIAIARALL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 160 DDADFLILDEPSNPLDGPARALLRARLAAWDGG--LLLVSHDRELLEGMQRIVEL 212
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRDADRIIVL 167
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
369-513 |
1.24e-12 |
|
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: 67.70 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVgaayLDQRLSLLDHGR--------GVLEQ---L-------------L 424
Cdd:COG1127 34 LAIIGGSGSGKSVLLKLIIGLLRPDSGE--ILV----DGQDITGLSEKElyelrrriGMLFQggaLfdsltvfenvafpL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 425 EVNRSRGESWLRTR----LAQLGL-------PAErlaqpcatLSGGERLKAALA--LVLyadRPaQLLLLDEPDNHLDLV 491
Cdd:COG1127 108 REHTDLSEAEIRELvlekLELVGLpgaadkmPSE--------LSGGMRKRVALAraLAL---DP-EILLYDEPTAGLDPI 175
|
170 180
....*....|....*....|....*.
gi 2316862561 492 ARQALETMLRQYRGAL----LVVSHD 513
Cdd:COG1127 176 TSAVIDELIRELRDELgltsVVVTHD 201
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-169 |
1.54e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLaqqLEPAdyptvadlA 88
Cdd:COG1134 42 LKDVSFEVERG--------ESV-----GIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL---LELG--------A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPWL------EALARIeagsldaadyecLG-ERWDIRQRLADALAAEGLG-HLraDTPSERLSGGecMRVALlgAF-- 158
Cdd:COG1134 98 GFHPELtgreniYLNGRL------------LGlSRKEIDEKFDEIVEFAELGdFI--DQPVKTYSSG--MRARL--AFav 159
|
170
....*....|....
gi 2316862561 159 ---LdDADFLILDE 169
Cdd:COG1134 160 ataV-DPDILLVDE 172
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
356-530 |
1.56e-12 |
|
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: 65.70 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQrLSLLDHGR--GVLEQLLEvnrsrges 433
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGR--VRLDGADISQ-WDPNELGDhvGYLPQDDE-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 434 wlrtrlaqlgLPAERLAQpcATLSGGERLKAALALVLYADRpaQLLLLDEPDNHLDLVARQALETMLRQYRGA---LLVV 510
Cdd:cd03246 87 ----------LFSGSIAE--NILSGGQRQRLGLARALYGNP--RILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVI 152
|
170 180
....*....|....*....|
gi 2316862561 511 SHDPWFLRRLGLDGVLAAGA 530
Cdd:cd03246 153 AHRPETLASADRILVLEDGR 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
369-513 |
1.64e-12 |
|
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: 67.14 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLD--QRLSLLDHGR--GVLEQ----------------LLEVNR 428
Cdd:cd03261 29 LAIIGPSGSGKSTLLRLIVGLLRPDSGE--VLIDGEDISglSEAELYRLRRrmGMLFQsgalfdsltvfenvafPLREHT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 429 SRGESWLRTR----LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLRQYR 504
Cdd:cd03261 107 RLSEEEIREIvlekLEAVGLRGAEDLYP-AELSGGMKKRVALARAL-ALDP-ELLLYDEPTAGLDPIASGVIDDLIRSLK 183
|
170
....*....|...
gi 2316862561 505 GAL----LVVSHD 513
Cdd:cd03261 184 KELgltsIMVTHD 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-175 |
1.64e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.09 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylAQQLEPADYPTVADL 87
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKgEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-----IDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 88 AGV---RPWLEALAR-IEAGSLDAADYECLGERwDIRQRLADALAAEGLGHLRADTPsERLSGGECMRVALLGAFLDDAD 163
Cdd:PRK13644 79 VGIvfqNPETQFVGRtVEEDLAFGPENLCLPPI-EIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPE 156
|
170
....*....|..
gi 2316862561 164 FLILDEPSNPLD 175
Cdd:PRK13644 157 CLIFDEVTSMLD 168
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-175 |
2.36e-12 |
|
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: 65.50 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqLEPADYPTvadla 88
Cdd:cd03230 16 LDDISLTVEKGEIY-------------GLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG--------KDIKKEPE----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 gvrpwlEALARIeaGSL--DAADYEclgerwdirqrladalaaeglgHLradTPSE--RLSGGECMRVALLGAFLDDADF 164
Cdd:cd03230 70 ------EVKRRI--GYLpeEPSLYE----------------------NL---TVREnlKLSGGMKQRLALAQALLHDPEL 116
|
170
....*....|.
gi 2316862561 165 LILDEPSNPLD 175
Cdd:cd03230 117 LILDEPTSGLD 127
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-175 |
2.42e-12 |
|
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: 66.76 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptvaDLA 88
Cdd:cd03257 21 LDDVSFSIKKGETL-------------GLVGESGSGKSTLARAILGLLKPTSGSIIFDGK-----------------DLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPWLEALARIEAG--------SLDAA------------DYECLGERWDIRQRLADALAAEGLGHLRADT-PSErLSGG 147
Cdd:cd03257 71 KLSRRLRKIRRKEIQmvfqdpmsSLNPRmtigeqiaeplrIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHE-LSGG 149
|
170 180
....*....|....*....|....*...
gi 2316862561 148 ECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALD 177
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
356-514 |
2.55e-12 |
|
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: 66.69 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVtvgaayLDQRLSLLDH-GRGVL-----------EQL 423
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL------AGQDLFALDEdARARLrarhvgfvfqsFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 -------------LEVnrsRGESWLRTR----LAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPAqLLLLDEPDN 486
Cdd:COG4181 102 lptltalenvmlpLEL---AGRRDARARaralLERVGL-GHRLDHYPAQLSGGEQQRVALARAF-ATEPA-ILFADEPTG 175
|
170 180 190
....*....|....*....|....*....|..
gi 2316862561 487 HLDLVARQA----LETMLRQYRGALLVVSHDP 514
Cdd:COG4181 176 NLDAATGEQiidlLFELNRERGTTLVLVTHDP 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-201 |
2.63e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLL--FSDLDETFDtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR--VRYLAQQLEPADyP-- 82
Cdd:PRK11147 322 MENVNYQIDGKQLVkdFSAQVQRGD--KIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQHRAELD-Pek 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVAD-LAgvrpwlEALARIEAGSldaadyeclgerwdiRQRLAdalaaegLGHL--------RADTPSERLSGGECMRVA 153
Cdd:PRK11147 399 TVMDnLA------EGKQEVMVNG---------------RPRHV-------LGYLqdflfhpkRAMTPVKALSGGERNRLL 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316862561 154 LLGAFLDDADFLILDEPSNPLDGPARALLRARLAAWDGGLLLVSHDRE 201
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQ 498
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-213 |
3.37e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLFSDLDETFDTRHTGLV-GRNGVGKSLLARLLAGHLQPSSGSVRR--QGRVRYLAQqlepady 81
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLItGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQ------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 82 ptvadlagvRPWLEAlarieaGSL-DAADYECLGERWDiRQRLADALAAEGLGHL--RADTP---SERLSGGECMRVALL 155
Cdd:COG4178 434 ---------RPYLPL------GTLrEALLYPATAEAFS-DAELREALEAVGLGHLaeRLDEEadwDQVLSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 156 GAFLDDADFLILDEPSNPLDGPARAL--LRARLAAWDGGLLLVSHDRELLEGMQRIVELS 213
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAAlyQLLREELPGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
356-512 |
4.02e-12 |
|
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: 65.76 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLD----QRLSLLDHGRG------VLEQLLE 425
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE--VLFDGKPLDiaarNRIGYLPEERGlypkmkVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 VNRSRG------ESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETM 499
Cdd:cd03269 94 LAQLKGlkkeeaRRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAV-IHDP-ELLILDEPFSGLDPVNVELLKDV 170
|
170
....*....|....*.
gi 2316862561 500 LRQYRGA---LLVVSH 512
Cdd:cd03269 171 IRELARAgktVILSTH 186
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
367-513 |
4.07e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.40 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 367 RRLALVGPNGSGKSTLLRLLAGQrapLAGtcavtVGAAYLDQR------LSLLDHGRGVLEQ------------LLEVNR 428
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGL---LPG-----QGEILLNGRplsdwsAAELARHRAYLSQqqsppfampvfqYLALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 429 SRG--ESWLRTRLAQ----LGLpAERLAQPCATLSGGE----RLKAALALVLYADRP-AQLLLLDEPDNHLDLVARQALE 497
Cdd:COG4138 95 PAGasSEAVEQLLAQlaeaLGL-EDKLSRPLTQLSGGEwqrvRLAAVLLQVWPTINPeGQLLLLDEPMNSLDVAQQAALD 173
|
170
....*....|....*....
gi 2316862561 498 TMLRQYR---GALLVVSHD 513
Cdd:COG4138 174 RLLRELCqqgITVVMSSHD 192
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
356-517 |
5.37e-12 |
|
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: 64.97 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQRLSL-------LDH---GRGVLEQLLE 425
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSigyvmqdVDYqlfTDSVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 VNRSRGESWLRTR--LAQLGLPAERLAQPcATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQY 503
Cdd:cd03226 96 GLKELDAGNEQAEtvLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERVGELIREL 172
|
170
....*....|....*..
gi 2316862561 504 RG---ALLVVSHDPWFL 517
Cdd:cd03226 173 AAqgkAVIVITHDYEFL 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-204 |
5.68e-12 |
|
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: 63.80 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldetfdtRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaQQLEPADYPTVADLA 88
Cdd:cd00267 15 LDNVSLTLKAG-------------EIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG------KDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPwlealarieagsldaadyeclgerwdirQrladalaaeglghlradtpserLSGGECMRVALLGAFLDDADFLILD 168
Cdd:cd00267 76 GYVP----------------------------Q----------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316862561 169 EPSNPLDGPARALLRARLAAW-DGG--LLLVSHDRELLE 204
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELaEEGrtVIIVTHDPELAE 144
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-175 |
9.99e-12 |
|
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: 65.53 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 2 TNTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaQQLEPADY 81
Cdd:TIGR04520 11 PESEKPALKNVSLSIEKGEFV-------------AIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL-----DTLDEENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 82 PTVADLAG----------VRPWLEAlarieagslDAA-DYECLG-ERWDIRQRLADALAAEGLGHLRADTPSeRLSGGEC 149
Cdd:TIGR04520 73 WEIRKKVGmvfqnpdnqfVGATVED---------DVAfGLENLGvPREEMRKRVDEALKLVGMEDFRDREPH-LLSGGQK 142
|
170 180
....*....|....*....|....*.
gi 2316862561 150 MRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLD 168
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
371-513 |
1.05e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQrapLAGTCAVTV-GAAYLDQRLSLLDHGRGVLEQ-----------------LLEVNRSRGE 432
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL---LPGSGSIQFaGQPLEAWSAAELARHRAYLSQqqtppfampvfqyltlhQPDKTRTEAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 433 SWLRTRLAQLGLPAERLAQPCATLSGGE----RLKAALALVLYADRP-AQLLLLDEPDNHLDLVARQALETMLRQYR--- 504
Cdd:PRK03695 104 ASALNEVAEALGLDDKLGRSVNQLSGGEwqrvRLAAVVLQVWPDINPaGQLLLLDEPMNSLDVAQQAALDRLLSELCqqg 183
|
....*....
gi 2316862561 505 GALLVVSHD 513
Cdd:PRK03695 184 IAVVMSSHD 192
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
356-513 |
1.11e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGtcAVTVGAAYL-----DQRLSLLDhgrgvlEQLL------ 424
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGTAPLaeareDTRLMFQD------ARLLpwkkvi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 425 -EVNRSRGESW---LRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYaDRPaQLLLLDEPDNHLDLVAR----QAL 496
Cdd:PRK11247 100 dNVGLGLKGQWrdaALQALAAVGL-ADRANEWPAALSGGQKQRVALARALI-HRP-GLLLLDEPLGALDALTRiemqDLI 176
|
170
....*....|....*..
gi 2316862561 497 ETMLRQYRGALLVVSHD 513
Cdd:PRK11247 177 ESLWQQHGFTVLLVTHD 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
356-520 |
1.20e-11 |
|
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: 64.48 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAyldqrlSLLDHGRGVLEQL----------LE 425
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLGLGGGFNPELtgreniylngRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 VNRSRGESWLRTR----LAQLGlpaERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEP----DNHLDLVARQALE 497
Cdd:cd03220 112 LGLSRKEIDEKIDeiieFSELG---DFIDLPVKTYSSGMKARLAFAIATALE--PDILLIDEVlavgDAAFQEKCQRRLR 186
|
170 180
....*....|....*....|...
gi 2316862561 498 TMLRQYRgALLVVSHDPWFLRRL 520
Cdd:cd03220 187 ELLKQGK-TVILVSHDPSSIKRL 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
356-512 |
1.24e-11 |
|
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: 63.49 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQRLSLLDHGRGVLEQllevnrsRGESWL 435
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE--ITLDGVPVSDLEKALSSLISVLNQ-------RPYLFD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 436 RTRLAQLGLPaerlaqpcatLSGGERLKAALALVLYADrpAQLLLLDEPDNHLD-LVARQALETMLRQYRG-ALLVVSH 512
Cdd:cd03247 89 TTLRNNLGRR----------FSGGERQRLALARILLQD--APIVLLDEPTVGLDpITERQLLSLIFEVLKDkTLIWITH 155
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
356-514 |
1.27e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQRLSLLDHGRGVLEQ---L--------- 423
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGR--IVLNGRDLFTNLPPRERRVGFVFQhyaLfphmtvaen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 ----LEVN-------RSRGESWLRtrLAQLGLPAERL-AQpcatLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLV 491
Cdd:COG1118 96 iafgLRVRppskaeiRARVEELLE--LVQLEGLADRYpSQ----LSGGQRQRVALARAL-AVEP-EVLLLDEPFGALDAK 167
|
170 180
....*....|....*....|....*..
gi 2316862561 492 ARQALETMLRQ----YRGALLVVSHDP 514
Cdd:COG1118 168 VRKELRRWLRRlhdeLGGTTVFVTHDQ 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
350-514 |
1.53e-11 |
|
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: 62.76 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 350 PHLRGPLreiDLLLSGPRRLALVGPNGSGKSTLLRllagqraplaGTCAVTVGAAYLDQRLSLLDHGRGVleqllevnrs 429
Cdd:cd03227 8 PSYFVPN---DVTFGEGSLTIITGPNGSGKSTILD----------AIGLALGGAQSATRRRSGVKAGCIV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 rgeswlrtrlaqlGLPAERLAQPCATLSGGERLKAALALVL--YADRPAQLLLLDEPDNHLDLVARQALETMLRQYRGA- 506
Cdd:cd03227 65 -------------AAVSAELIFTRLQLSGGEKELSALALILalASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKg 131
|
170
....*....|
gi 2316862561 507 --LLVVSHDP 514
Cdd:cd03227 132 aqVIVITHLP 141
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
315-520 |
1.73e-11 |
|
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: 66.54 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 315 EAAREVEEASPLLLDSPDAELAAQRRIVELKGAVL--PHLRGPLREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAP 392
Cdd:TIGR02857 295 EALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVayPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 393 LAGTCAVT-------------VGAAYLDQRLSLLDhgRGVLEQLLEVNRSRGESWLRTRLAQLGLP----------AERL 449
Cdd:TIGR02857 375 TEGSIAVNgvpladadadswrDQIAWVPQHPFLFA--GTIAENIRLARPDASDAEIREALERAGLDefvaalpqglDTPI 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 450 AQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALETMLRQYRG--ALLVVSHDPWFLRRL 520
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFL--RDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAALA 523
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
371-520 |
1.82e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.92 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGA-----------AYLDQRL-------SLLDHgRGVLEQL---LEVN-R 428
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQ--VLVNGqdlsrlkrreiPYLRRRIgvvfqdfRLLPD-RTVYENValpLRVTgK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 429 SRGEswLRTR----LAQLGLpAERLAQPCATLSGGERLKAAL--ALVlyaDRPaQLLLLDEPDNHLDlvARQALETM--- 499
Cdd:COG2884 110 SRKE--IRRRvrevLDLVGL-SDKAKALPHELSGGEQQRVAIarALV---NRP-ELLLADEPTGNLD--PETSWEIMell 180
|
170 180
....*....|....*....|...
gi 2316862561 500 --LRQYRGALLVVSHDPWFLRRL 520
Cdd:COG2884 181 eeINRRGTTVLIATHDLELVDRM 203
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
370-513 |
2.41e-11 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 64.07 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLD--------QRLSLLDH----------------GRGVLEQLLE 425
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGT--VDLAGVDLHglsrraraRRVALVEQdsdtavpltvrdvvalGRIPHRSLWA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 VNRSRGESWLRTRLAQLGLpaERLA-QPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLRQYR 504
Cdd:TIGR03873 109 GDSPHDAAVVDRALARTEL--SHLAdRDMSTLSGGERQRVHVARAL-AQEP-KLLLLDEPTNHLDVRAQLETLALVRELA 184
|
170
....*....|..
gi 2316862561 505 G---ALLVVSHD 513
Cdd:TIGR03873 185 AtgvTVVAALHD 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-212 |
2.56e-11 |
|
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: 66.40 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVR------RQGRVRYLAQQLep 78
Cdd:COG2274 487 SPPVLDNISLTIKPGE-------------RVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlRQIDPASLRRQI-- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 79 ADYP--------TVAD-LAGVRPWLEaLARIEAgsldAADYECLGErwDIRQRladalaAEGLghlraDTP-SER---LS 145
Cdd:COG2274 552 GVVLqdvflfsgTIREnITLGDPDAT-DEEIIE----AARLAGLHD--FIEAL------PMGY-----DTVvGEGgsnLS 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 146 GGECMRVALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAWDGG--LLLVSHDRELLEGMQRIVEL 212
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRLADRIIVL 682
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
368-512 |
3.49e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.45 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGT-------CAVTVGA----AYLDQRLSLLDH-------GRGvLEQLLEVNRS 429
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNLIAGFLTPASGSltlngqdHTTTPPSrrpvSMLFQENNLFSHltvaqniGLG-LNPGLKLNAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 RGESwLRTRLAQLGLPA--ERLAqpcATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETML----RQY 503
Cdd:PRK10771 106 QREK-LHAIARQMGIEDllARLP---GQLSGGQRQRVALARCLVREQP--ILLLDEPFSALDPALRQEMLTLVsqvcQER 179
|
....*....
gi 2316862561 504 RGALLVVSH 512
Cdd:PRK10771 180 QLTLLMVSH 188
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
370-512 |
4.84e-11 |
|
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: 62.77 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAG------QRAPLAGTCAVTVGAAYLdQRLSLLDHGRGVLEQL-----LE-------VNRSRG 431
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGllepdaGFATVDGFDVVKEPAEAR-RRLGFVSDSTGLYDRLtarenLEyfaglygLKGDEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 432 ESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQYRG---ALL 508
Cdd:cd03266 114 TARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPP--VLLLDEPTTGLDVMATRALREFIRQLRAlgkCIL 190
|
....
gi 2316862561 509 VVSH 512
Cdd:cd03266 191 FSTH 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-175 |
5.84e-11 |
|
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: 62.39 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvryLAQQLEPADYPT----V 84
Cdd:cd03266 21 VDGVSFTVKPGEV-------------TGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG----FDVVKEPAEARRrlgfV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 85 ADLAGVRPWLEALARIEAgsldAADYECLgERWDIRQRLADALAAEGLGHLRaDTPSERLSGGECMRVALLGAFLDDADF 164
Cdd:cd03266 84 SDSTGLYDRLTARENLEY----FAGLYGL-KGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170
....*....|.
gi 2316862561 165 LILDEPSNPLD 175
Cdd:cd03266 158 LLLDEPTTGLD 168
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-175 |
7.11e-11 |
|
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: 62.15 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-----------VRYLA 73
Cdd:cd03259 12 SVRALDDLSLTVEPGEFL-------------ALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 74 QQlePADYP--TVAD-LA-GVRPWLEALArieagsldaadyeclgerwDIRQRLADALAAEGLGHLRADTPSErLSGGEC 149
Cdd:cd03259 79 QD--YALFPhlTVAEnIAfGLKLRGVPKA-------------------EIRARVRELLELVGLEGLLNRYPHE-LSGGQQ 136
|
170 180
....*....|....*....|....*.
gi 2316862561 150 MRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALD 162
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-175 |
7.17e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.87 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlEPADYPTvADLA 88
Cdd:PRK13548 18 LDDVSLTLRPGEV-------------VAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR--------PLADWSP-AELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVR-----------PWL--E--ALARIEAGSLDAADyeclgerwdiRQRLADALAAEGLGHLrADTPSERLSGGECMRVA 153
Cdd:PRK13548 76 RRRavlpqhsslsfPFTveEvvAMGRAPHGLSRAED----------DALVAAALAQVDLAHL-AGRDYPQLSGGEQQRVQ 144
|
170 180
....*....|....*....|....*...
gi 2316862561 154 L------LGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13548 145 LarvlaqLWEPDGPPRWLLLDEPTSALD 172
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
368-517 |
8.36e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGA----------AYLDQRLslLD-----HgrgvlEQLLEVNRSR-- 430
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErlgklrqdqfAFEEFTV--LDtvimgH-----TELWEVKQERdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 431 -----------------------------GESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLYADrPaQLLLL 481
Cdd:PRK15064 102 iyalpemseedgmkvadlevkfaemdgytAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSN-P-DILLL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316862561 482 DEPDNHLDLVARQALETMLRQYRGALLVVSHDPWFL 517
Cdd:PRK15064 180 DEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
353-513 |
9.50e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 353 RGPLREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVG--AAYLDQRLSLldhgrgvlEQLLEVNRSR 430
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL--------DTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 431 gesWLR----TRLAQLGLPAER------LAQPCATLSGGERLKAALALVLYaDRPaQLLLLDEPDNHLDLVARQALETML 500
Cdd:PRK09544 89 ---FLRlrpgTKKEDILPALKRvqaghlIDAPMQKLSGGETQRVLLARALL-NRP-QLLVLDEPTQGVDVNGQVALYDLI 163
|
170
....*....|....*..
gi 2316862561 501 RQYRG----ALLVVSHD 513
Cdd:PRK09544 164 DQLRReldcAVLMVSHD 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
369-514 |
1.05e-10 |
|
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: 61.35 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTC-----AVTVGAAYLDQRLSLLDHGRG------VLEQLLEVNRSRGESWLRT 437
Cdd:cd03231 29 LQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggPLDFQRDSIARGLLYLGHAPGikttlsVLENLRFWHADHSDEQVEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 438 RLAQLGLPAERLAqPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQYR---GALLVVSHDP 514
Cdd:cd03231 109 ALARVGLNGFEDR-PVAQLSAGQQRRVALARLLLSGRP--LWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTHQD 185
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
356-514 |
1.46e-10 |
|
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: 64.08 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGaaylDQRLSLLDHGR-----GVLEQ-------- 422
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR--ILID----GIDLRQIDPASlrrqiGVVLQdvflfsgt 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 LLE----VNRSRGESWLRTRLAQLGLPAERLAQP----------CATLSGGERLKAALALVLYADrpAQLLLLDEPDNHL 488
Cdd:COG2274 565 IREnitlGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgegGSNLSGGQRQRLAIARALLRN--PRILILDEATSAL 642
|
170 180
....*....|....*....|....*...
gi 2316862561 489 DLVARQALETMLRQYRG--ALLVVSHDP 514
Cdd:COG2274 643 DAETEAIILENLRRLLKgrTVIIIAHRL 670
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
356-502 |
1.62e-10 |
|
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: 61.05 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLsGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV--------------TVGaaYLDQRLSLLDHGRgVLE 421
Cdd:cd03264 16 LDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpqklrrRIG--YLPQEFGVYPNFT-VRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 422 Q------LLEVNRSRGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQA 495
Cdd:cd03264 92 FldyiawLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD--PSILIVDEPTAGLDPEERIR 168
|
....*..
gi 2316862561 496 LETMLRQ 502
Cdd:cd03264 169 FRNLLSE 175
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-175 |
1.78e-10 |
|
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: 60.69 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPA--------D 80
Cdd:cd03268 16 LDDISLHVKKGEI-------------YGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS---YQKNIEAlrrigaliE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 YPTVADLAGVRPWLEALARIeagsldaadyecLGERWDIRQRLADALaaeGLGHlRADTPSERLSGGECMRVALLGAFLD 160
Cdd:cd03268 80 APGFYPNLTARENLRLLARL------------LGIRKKRIDEVLDVV---GLKD-SAKKKVKGFSLGMKQRLGIALALLG 143
|
170
....*....|....*
gi 2316862561 161 DADFLILDEPSNPLD 175
Cdd:cd03268 144 NPDLLILDEPTNGLD 158
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
369-514 |
1.80e-10 |
|
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: 60.98 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAV-----TVGAAYLDQRLSL------LDHGRGVLEQLLEVNRSRGESWLRT 437
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysiRTDRKAARQSLGYcpqfdaLFDELTVREHLRFYARLKGLPKSEI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 438 R------LAQLGLP--AERLAQpcaTLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQYRG--AL 507
Cdd:cd03263 111 KeevellLRVLGLTdkANKRAR---TLSGGMKRKLSLAIALIGGPS--VLLLDEPTSGLDPASRRAIWDLILEVRKgrSI 185
|
....*..
gi 2316862561 508 LVVSHDP 514
Cdd:cd03263 186 ILTTHSM 192
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
356-518 |
1.81e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLD-----------------------QRLSL 412
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT--IRVGDITIDtarslsqqkglirqlrqhvgfvfQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 413 LDHgRGVLEQLLE-----VNRSRGESWLRTR--LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPD 485
Cdd:PRK11264 97 FPH-RTVLENIIEgpvivKGEPKEEATARARelLAKVGLAGKETSYP-RRLSGGQQQRVAIARAL-AMRP-EVILFDEPT 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316862561 486 NHLD--LVArQALETM--LRQYRGALLVVSHDPWFLR 518
Cdd:PRK11264 173 SALDpeLVG-EVLNTIrqLAQEKRTMVIVTHEMSFAR 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
356-513 |
1.91e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 61.64 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGaaylDQRLSLLDHGRGVLEQ------------- 422
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGE--VLVD----GKPVTGPGPDRGVVFQepallpwltvldn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 ----LLEVNRSRGESWLRTR--LAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQAL 496
Cdd:COG1116 101 valgLELRGVPKAERRERARelLELVGL-AGFEDAYPHQLSGGMRQRVAIARALANDPE--VLLMDEPFGALDALTRERL 177
|
170 180
....*....|....*....|.
gi 2316862561 497 ETML----RQYRGALLVVSHD 513
Cdd:COG1116 178 QDELlrlwQETGKTVLFVTHD 198
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
368-513 |
2.15e-10 |
|
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: 60.91 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGTCA-----VTVGAAY---------------LDQRLSLLD-------HGRGVL 420
Cdd:cd03219 28 IHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGLPPHeiarlgigrtfqiprLFPELTVLEnvmvaaqARTGSG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 421 EQLLEVNRSRGESWLRTR--LAQLGLpAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALET 498
Cdd:cd03219 108 LLLARARREEREARERAEelLERVGL-ADLADRPAGELSYGQQRRLEIARALATD--PKLLLLDEPAAGLNPEETEELAE 184
|
170
....*....|....*...
gi 2316862561 499 MLRQYRG---ALLVVSHD 513
Cdd:cd03219 185 LIRELRErgiTVLLVEHD 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
373-524 |
2.17e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 373 GPNGSGKSTLLRLLAGQRAPLAG------TCAVTVGAAYLDQrLSLLDHGRGV------LEQL---LEVNRSRGESWLRT 437
Cdd:PRK13538 34 GPNGAGKTSLLRILAGLARPDAGevlwqgEPIRRQRDEYHQD-LLYLGHQPGIkteltaLENLrfyQRLHGPGDDEALWE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 438 RLAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQY--RGALLV------ 509
Cdd:PRK13538 113 ALAQVGL-AGFEDVPVRQLSAGQQRRVALARLWLTRAP--LWILDEPFTAIDKQGVARLEALLAQHaeQGGMVIltthqd 189
|
170
....*....|....*
gi 2316862561 510 VSHDPWFLRRLGLDG 524
Cdd:PRK13538 190 LPVASDKVRKLRLGQ 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-210 |
2.38e-10 |
|
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: 60.68 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrYLAQQLEPADYP 82
Cdd:cd03245 14 NQEIPALDNVSLTIRAGE-------------KVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---TDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADLAGVRPWLEAlarieaGSLdaADYECLGERWDIRQRLADALAAEGLGHLRADTP-------SER---LSGGECMRV 152
Cdd:cd03245 78 RNIGYVPQDVTLFY------GTL--RDNITLGAPLADDERILRAAELAGVTDFVNKHPngldlqiGERgrgLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAWDGG--LLLVSHDRELLEGMQRIV 210
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRII 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
16-210 |
3.00e-10 |
|
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: 60.00 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 16 LPDGSLlfsDLDETFDTRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVR-----------------RQGRVRYLAQQlep 78
Cdd:cd03297 10 LPDFTL---KIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinlppQQRKIGLVFQQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 79 adyptvadlAGVRPWLEALARIEAGSLDAADYEclgerwdIRQRLADALAAEGLGHLrADTPSERLSGGECMRVALLGAF 158
Cdd:cd03297 84 ---------YALFPHLNVRENLAFGLKRKRNRE-------DRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316862561 159 LDDADFLILDEPSNPLDGPARA----LLRARLAAWDGGLLLVSHDRELLEGM-QRIV 210
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLqllpELKQIKKNLNIPVIFVTHDLSEAEYLaDRIV 203
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
356-518 |
3.57e-10 |
|
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: 59.85 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLD-----------------QRLSLLDHgRG 418
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT--IIIDGLKLTddkkninelrqkvgmvfQQFNLFPH-LT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 419 VLEQLLEV-----NRSRGESWLRTR--LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLD-- 489
Cdd:cd03262 93 VLENITLApikvkGMSKAEAEERALelLEKVGLADKADAYP-AQLSGGQQQRVAIARAL-AMNP-KVMLFDEPTSALDpe 169
|
170 180 190
....*....|....*....|....*....|.
gi 2316862561 490 LVaRQALETM--LRQYRGALLVVSHDPWFLR 518
Cdd:cd03262 170 LV-GEVLDVMkdLAEEGMTMVVVTHEMGFAR 199
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
358-520 |
4.53e-10 |
|
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: 61.27 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 358 EIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTvGAAYLD--QRLSLLDHGRGV--------------LE 421
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG-GEVLQDsaRGIFLPPHRRRIgyvfqearlfphlsVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 422 QLLEVNRSRGESWLRT-RLAQ----LGLpAERLAQPCATLSGGERLKAALALVLYAdRPaQLLLLDEPDNHLDLVARQAL 496
Cdd:COG4148 96 GNLLYGRKRAPRAERRiSFDEvvelLGI-GHLLDRRPATLSGGERQRVAIGRALLS-SP-RLLLMDEPLAALDLARKAEI 172
|
170 180
....*....|....*....|....*...
gi 2316862561 497 ETMLRQYRGAL----LVVSHDPWFLRRL 520
Cdd:COG4148 173 LPYLERLRDELdipiLYVSHSLDEVARL 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
371-513 |
4.66e-10 |
|
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: 59.73 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRAPLAGTCAVT------------------VGAAYLDQRLsLLDhgRGVLEQL---LEVNRS 429
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlrgraipylrrkIGVVFQDFRL-LPD--RNVYENVafaLEVTGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 RGESWlRTR----LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPAqLLLLDEPDNHLDLVARQALETMLRQY-- 503
Cdd:cd03292 109 PPREI-RKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAI-VNSPT-ILIADEPTGNLDPDTTWEIMNLLKKInk 184
|
170
....*....|.
gi 2316862561 504 RGALLVVS-HD 513
Cdd:cd03292 185 AGTTVVVAtHA 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
368-513 |
4.82e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 60.44 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVG-------AAY---------------LDQRLSLLD---------HG 416
Cdd:COG0411 32 IVGLIGPNGAGKTTLFNLITGFYRPTSGR--ILFDgrditglPPHriarlgiartfqnprLFPELTVLEnvlvaaharLG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 417 RGVLEQLLEVNRSR-GESWLRTR----LAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLV 491
Cdd:COG0411 110 RGLLAALLRLPRARrEEREARERaeelLERVGL-ADRADEPAGNLSYGQQRRLEIARAL-ATEP-KLLLLDEPAAGLNPE 186
|
170 180
....*....|....*....|....*.
gi 2316862561 492 ARQALETMLRQYRG----ALLVVSHD 513
Cdd:COG0411 187 ETEELAELIRRLRDergiTILLIEHD 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-175 |
4.85e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 18 DGSLLFSDLDetFDTRHTGLV---GRNGVGKSLLARLLAGHLQPSSGSVR------RQGRVRYLAQQLepadYptVADLA 88
Cdd:PRK13538 12 DERILFSGLS--FTLNAGELVqieGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLL----Y--LGHQP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPWLEALariEAGSLDAADYECLGErwdirQRLADALAAEGLGHlRADTPSERLSGGECMRVALLGAFLDDADFLILD 168
Cdd:PRK13538 84 GIKTELTAL---ENLRFYQRLHGPGDD-----EALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
....*..
gi 2316862561 169 EPSNPLD 175
Cdd:PRK13538 155 EPFTAID 161
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
37-175 |
5.24e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVR--YLAQQ--LEPADYPTVADLAGVRP------WLEALARIEAGSLd 106
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRigYVPQKlyLDTTLPLTVNRFLRLRPgtkkedILPALKRVQAGHL- 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 107 aadyeclgerwdirqrladalaaeglghlrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK09544 114 ------------------------------IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
369-514 |
5.48e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 61.27 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGaaylDQRLS-LLDHGRGV----------------------LEQLle 425
Cdd:COG3842 34 VALLGPSGCGKTTLLRMIAGFETPDSGR--ILLD----GRDVTgLPPEKRNVgmvfqdyalfphltvaenvafgLRMR-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 vNRSRGEswLRTR----LAQLGLP--AERLAqpcATLSGGERLKAALA--LVLyadRPaQLLLLDEPDNHLDLVARQALE 497
Cdd:COG3842 106 -GVPKAE--IRARvaelLELVGLEglADRYP---HQLSGGQQQRVALAraLAP---EP-RVLLLDEPLSALDAKLREEMR 175
|
170 180
....*....|....*....|.
gi 2316862561 498 TMLRQYRGAL----LVVSHDP 514
Cdd:COG3842 176 EELRRLQRELgitfIYVTHDQ 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-72 |
5.66e-10 |
|
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: 59.47 E-value: 5.66e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 9 LDGVSFQLPDGsllfsdldetfdtRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYL 72
Cdd:cd03220 38 LKDVSFEVPRG-------------ERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL 88
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
356-513 |
6.05e-10 |
|
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: 59.66 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVT-------------VGAAYldQRLSLLDHgRGVLEQ 422
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvqernVGFVF--QHYALFRH-MTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 L---LEVNRSRG---ESWLRTR------LAQLGLPAERLAqpcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDL 490
Cdd:cd03296 95 VafgLRVKPRSErppEAEIRAKvhellkLVQLDWLADRYP---AQLSGGQRQRVALARAL-AVEP-KVLLLDEPFGALDA 169
|
170 180
....*....|....*....|....*..
gi 2316862561 491 VARQALETMLRQYRGAL----LVVSHD 513
Cdd:cd03296 170 KVRKELRRWLRRLHDELhvttVFVTHD 196
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-175 |
6.06e-10 |
|
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: 59.22 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG---------RVRYLAQqlEPA 79
Cdd:cd03269 16 LDDISFSVEKGEIF-------------GLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPE--ERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 80 DYPTV---------ADLAGVRPwLEALARIeagsldaadyeclgERWDIRQRLADalaaeglghlRADTPSERLSGGECM 150
Cdd:cd03269 81 LYPKMkvidqlvylAQLKGLKK-EEARRRI--------------DEWLERLELSE----------YANKRVEELSKGNQQ 135
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLD 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-175 |
6.16e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR----------VRYLA---QQ 75
Cdd:PRK11231 18 LNDLSLSLPTGKI-------------TALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlARRLAllpQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 76 LEPADYPTVADLA--GVRPWLEALARieagsLDAADyeclgerwdiRQRLADALAAEGLGHLrADTPSERLSGGECMRVA 153
Cdd:PRK11231 85 HLTPEGITVRELVayGRSPWLSLWGR-----LSAED----------NARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAF 148
|
170 180
....*....|....*....|..
gi 2316862561 154 LLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLD 170
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-175 |
6.55e-10 |
|
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: 59.69 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 35 TGLVGRNGVGKSLLARLLAGHLQPSsgsvrrqgrvryLAQQLEPADYPTVADLAGVRPWLEALARIEAGSLDAA------ 108
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPN------------LGKFDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIvkpqyv 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 109 ---------DYECLGERWDIRQRLADALAAEGLGHLRaDTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03236 97 dlipkavkgKVGELLKKKDERGKLDELVDQLELRHVL-DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
370-514 |
7.63e-10 |
|
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: 59.12 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAG-----QRAPLAGTCAVTVGAAY-LDQRLSLLDHGRGVLEQL---------------LEVNR 428
Cdd:cd03260 30 ALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYdLDVDVLELRRRVGMVFQKpnpfpgsiydnvaygLRLHG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 429 SRGESWLRTRLAQL----GLPAERLAQPCAT-LSGGERLKAALALVLyADRPAqLLLLDEPDNHLDLVARQALETMLRQY 503
Cdd:cd03260 110 IKLKEELDERVEEAlrkaALWDEVKDRLHALgLSGGQQQRLCLARAL-ANEPE-VLLLDEPTSALDPISTAKIEELIAEL 187
|
170
....*....|...
gi 2316862561 504 RG--ALLVVSHDP 514
Cdd:cd03260 188 KKeyTIVIVTHNM 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
356-513 |
7.67e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTC---AVTVGAAYLDQRLSLLDHG----RGVLE------Q 422
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldGKPVEGPGAERGVVFQNEGllpwRNVQDnvafglQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 LLEVNRSRGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETML-- 500
Cdd:PRK11248 97 LAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAAN--PQLLLLDEPFGALDAFTREQMQTLLlk 173
|
170
....*....|....*
gi 2316862561 501 --RQYRGALLVVSHD 513
Cdd:PRK11248 174 lwQETGKQVLLITHD 188
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-175 |
8.69e-10 |
|
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: 58.09 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGsllfsdldetfdtRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVrrqgrvryLAQQLEPADYP 82
Cdd:cd03247 12 EQEQQVLKNLSLELKQG-------------EKIALLGRSGSGKSTLLQLLTGDLKPQQGEI--------TLDGVPVSDLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 -TVADLAGVrpwlealarieagsldaadyeclgerwdIRQR--LADALAAEGLGhlradtpsERLSGGECMRVALLGAFL 159
Cdd:cd03247 71 kALSSLISV----------------------------LNQRpyLFDTTLRNNLG--------RRFSGGERQRLALARILL 114
|
170
....*....|....*.
gi 2316862561 160 DDADFLILDEPSNPLD 175
Cdd:cd03247 115 QDAPIVLLDEPTVGLD 130
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
369-524 |
9.12e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTvGAAYLDQRLSLLDHGRG----------VLEQLLEVNRSRG--ESWLR 436
Cdd:PRK13539 31 LVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD-GGDIDDPDVAEACHYLGhrnamkpaltVAENLEFWAAFLGgeELDIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 437 TRLAQLGL-PAERLaqPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQYR---GALLVVSH 512
Cdd:PRK13539 110 AALEAVGLaPLAHL--PFGYLSAGQKRRVALARLLVSNRP--IWILDEPTAALDAAAVALFAELIRAHLaqgGIVIAATH 185
|
170
....*....|..
gi 2316862561 513 DPwflrrLGLDG 524
Cdd:PRK13539 186 IP-----LGLPG 192
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-170 |
1.12e-09 |
|
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: 58.99 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptvaDLA 88
Cdd:cd03219 16 LDDVSFSVRPGEI-------------HGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE-----------------DIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPW----------------------LE--ALARIEAGSLDAADYECLGERWDIRQRLADALAAEGLGHlRADTPSERL 144
Cdd:cd03219 66 GLPPHeiarlgigrtfqiprlfpeltvLEnvMVAAQARTGSGLLLARARREEREARERAEELLERVGLAD-LADRPAGEL 144
|
170 180
....*....|....*....|....*.
gi 2316862561 145 SGGECMRVALLGAFLDDADFLILDEP 170
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEP 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
7-175 |
1.14e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.48 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlePADYPTva 85
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKgEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---------PIDYSR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 86 dlAGVRPWLEALARI----EAGSLDAADYE---------CLGERwDIRQRLADALAAEGLGHLRaDTPSERLSGGECMRV 152
Cdd:PRK13636 75 --KGLMKLRESVGMVfqdpDNQLFSASVYQdvsfgavnlKLPED-EVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRV 150
|
170 180
....*....|....*....|...
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLD 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-483 |
1.19e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 59.33 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAG----------------------QRA---------PLAGTCA-VTVG-----AAYLDQRLSLl 413
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGslppdsgsilidgkdvtklpeyKRAkyigrvfqdPMMGTAPsMTIEenlalAYRRGKRRGL- 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316862561 414 dhGRGvleqlleVNRSRGEsWLRTRLAQLGLPAE-RLAQPCATLSGGERlkAALALVLYADRPAQLLLLDE 483
Cdd:COG1101 116 --RRG-------LTKKRRE-LFRELLATLGLGLEnRLDTKVGLLSGGQR--QALSLLMATLTKPKLLLLDE 174
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-175 |
1.46e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 59.70 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPAD-------- 80
Cdd:COG3839 19 LKDIDLDIEDGEFL-------------VLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD---VTDLPPKDrniamvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 ----YP--TVAD-------LAGVrpwlealarieagslDAAdyeclgerwDIRQRLADALAAEGLGHLRADTPSErLSGG 147
Cdd:COG3839 83 syalYPhmTVYEniafplkLRKV---------------PKA---------EIDRRVREAAELLGLEDLLDRKPKQ-LSGG 137
|
170 180
....*....|....*....|....*....
gi 2316862561 148 ECMRVALLGAFLDDADFLILDEP-SNpLD 175
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPlSN-LD 165
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
356-513 |
1.50e-09 |
|
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: 58.50 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVG---------------AAYLDQR------LSLLD 414
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE--VRVAglvpwkrrkkflrriGVVFGQKtqlwwdLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 415 hGRGVLEQLLEVNRSRGESWLRtRLAQLGLPAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQ 494
Cdd:cd03267 115 -SFYLLAAIYDLPPARFKKRLD-ELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE--PEILFLDEPTIGLDVVAQE 190
|
170 180
....*....|....*....|...
gi 2316862561 495 ALETMLRQY---RGA-LLVVSHD 513
Cdd:cd03267 191 NIRNFLKEYnreRGTtVLLTSHY 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
368-517 |
1.80e-09 |
|
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: 57.98 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGtcAVTVGAA---------------YLDQRLSL----------LDHGRGVLEQ 422
Cdd:cd03245 32 KVAIIGRVGSGKSTLLKLLAGLYKPTSG--SVLLDGTdirqldpadlrrnigYVPQDVTLfygtlrdnitLGAPLADDER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 LLEVNRSRG-ESWLRTRLAQLGLP-AERLAQpcatLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETML 500
Cdd:cd03245 110 ILRAAELAGvTDFVNKHPNGLDLQiGERGRG----LSGGQRQAVALARALLNDPP--ILLLDEPTSAMDMNSEERLKERL 183
|
170
....*....|....*....
gi 2316862561 501 RQYRG--ALLVVSHDPWFL 517
Cdd:cd03245 184 RQLLGdkTLIIITHRPSLL 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-175 |
1.82e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.23 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLFsdlDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPADYP--- 82
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF---DLTIAAgERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERPvsm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 -----------TVAD-LA-GVRPWLealarieagSLDAADyeclgerwdiRQRLADALAAEGLGHLRADTPSErLSGGEC 149
Cdd:COG3840 76 lfqennlfphlTVAQnIGlGLRPGL---------KLTAEQ----------RAQVEQALERVGLAGLLDRLPGQ-LSGGQR 135
|
170 180
....*....|....*....|....*.
gi 2316862561 150 MRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALD 161
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
369-514 |
1.87e-09 |
|
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: 57.37 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTC-----AVTVGAAYLDQRLSLLDHGRG------VLEQLLEVNR-SRGESW-L 435
Cdd:TIGR01189 29 LQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtPLAEQRDEPHENILYLGHLPGlkpelsALENLHFWAAiHGGAQRtI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 436 RTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALETMLRQY---RGALLVVSH 512
Cdd:TIGR01189 109 EDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRP--LWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
..
gi 2316862561 513 DP 514
Cdd:TIGR01189 186 QD 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
370-512 |
2.80e-09 |
|
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: 57.23 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTCAVtvgaayLDQRLSLLDHGRGVLEQLLEV-----NRSrGESWLRTRLAQLGL 444
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILGLIKPDSGEITF------DGKSYQKNIEALRRIGALIEApgfypNLT-ARENLRLLARLLGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 445 PAERLAQ-------------PCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLRQYR---GALL 508
Cdd:cd03268 103 RKKRIDEvldvvglkdsakkKVKGFSLGMKQRLGIALAL-LGNP-DLLILDEPTNGLDPDGIKELRELILSLRdqgITVL 180
|
....
gi 2316862561 509 VVSH 512
Cdd:cd03268 181 ISSH 184
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
356-513 |
3.11e-09 |
|
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: 57.35 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCA-----VTV------GAAYLDQRLSLLDHgRGVLE--- 421
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkdITNlppekrDISYVPQNYALFPH-MTVYKnia 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 422 ---QLLEVNRSRGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALA--LVLyadRPaQLLLLDEPDNHLDLVARQAL 496
Cdd:cd03299 94 yglKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIAraLVV---NP-KILLLDEPFSALDVRTKEKL 168
|
170 180
....*....|....*....|.
gi 2316862561 497 ETMLRQYRGALLV----VSHD 513
Cdd:cd03299 169 REELKKIRKEFGVtvlhVTHD 189
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-175 |
3.31e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 35 TGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqlEPADYPTVADLAgVRPWLEAL-----ARIEAGSLD--- 106
Cdd:PRK13638 30 TGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG---------KPLDYSKRGLLA-LRQQVATVfqdpeQQIFYTDIDsdi 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 107 AADYECLG-ERWDIRQRLADALAAEGLGHLRaDTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13638 100 AFSLRNLGvPEAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
356-521 |
3.80e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQ-----RLSLLDHGRGVLEQL------- 423
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD--VIFNGQPMSKlssaaKAELRNQKLGFIYQFhhllpdf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 --LE----------VNRSRGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPAqLLLLDEPDNHLDLV 491
Cdd:PRK11629 103 taLEnvamplligkKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAIARAL-VNNPR-LVLADEPTGNLDAR 179
|
170 180 190
....*....|....*....|....*....|....
gi 2316862561 492 ARQALETML----RQYRGALLVVSHDPWFLRRLG 521
Cdd:PRK11629 180 NADSIFQLLgelnRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
363-517 |
4.73e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 363 LSGPRRLALVGPNGSGKSTLLRLLAGQRAP-LAGTCAV------TVG----------------AAYLDQRLSLLDHGRGV 419
Cdd:PLN03073 200 LAFGRHYGLVGRNGTGKTTFLRYMAMHAIDgIPKNCQIlhveqeVVGddttalqcvlntdierTQLLEEEAQLVAQQREL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 420 -------------------------LEQL---LE-VNRSRGESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVL 470
Cdd:PLN03073 280 efetetgkgkgankdgvdkdavsqrLEEIykrLElIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARAL 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316862561 471 YADrpAQLLLLDEPDNHLDLVARQALETMLRQYRGALLVVSHDPWFL 517
Cdd:PLN03073 360 FIE--PDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFL 404
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
356-513 |
4.78e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.39 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcavtvgAAYLDQRLSLLDHG------RGV---------- 419
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGN------VSWRGEPLAKLNRAqrkafrRDIqmvfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 420 --------------LEQLLEVNRSRGESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPD 485
Cdd:PRK10419 102 vnprktvreiirepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARAL-AVEP-KLLILDEAV 179
|
170 180 190
....*....|....*....|....*....|..
gi 2316862561 486 NHLDLVARQ---ALETMLRQYRG-ALLVVSHD 513
Cdd:PRK10419 180 SNLDLVLQAgviRLLKKLQQQFGtACLFITHD 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
370-510 |
4.80e-09 |
|
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: 59.64 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQRL-------------SLLDHGRGVLEQLLEVNRSRGESW-- 434
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGT--VLVGGKDIETNLdavrqslgmcpqhNILFHHLTVAEHILFYAQLKGRSWee 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 435 ----LRTRLAQLGLPAERlAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQYRGALLVV 510
Cdd:TIGR01257 1038 aqleMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGD--AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTII 1114
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-175 |
5.04e-09 |
|
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: 56.21 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 18 DGSLLFSDLDETFDTRHT-GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQLEPADYPTVADLAGVRPWLEA 96
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEAlQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 97 LARIE--AGSLDAADYECLgerwdirqrlaDALAAEGLGHLrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPL 174
Cdd:TIGR01189 91 LENLHfwAAIHGGAQRTIE-----------DALAAVGLTGF-EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
.
gi 2316862561 175 D 175
Cdd:TIGR01189 159 D 159
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
367-520 |
5.51e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.01 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 367 RRLALVGPNGSGKSTLLRLLAGQRAPlagtcavTVGAAYLDQRLS-LLDHGRGVLEQL--LEvNrsrgeswLRTRLAQLG 443
Cdd:COG1134 53 ESVGIIGRNGAGKSTLLKLIAGILEP-------TSGRVEVNGRVSaLLELGAGFHPELtgRE-N-------IYLNGRLLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 444 LP----AERLA-------------QPCATLSGGERLKAALALVLYADrpAQLLLLDEpdnhldlV-----------ARQA 495
Cdd:COG1134 118 LSrkeiDEKFDeivefaelgdfidQPVKTYSSGMRARLAFAVATAVD--PDILLVDE-------VlavgdaafqkkCLAR 188
|
170 180
....*....|....*....|....*
gi 2316862561 496 LETMLRQYRgALLVVSHDPWFLRRL 520
Cdd:COG1134 189 IRELRESGR-TVIFVSHSMGAVRRL 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-175 |
5.66e-09 |
|
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: 58.53 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGSLLFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrYLAQQLEPADYPTV 84
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPgERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG---VPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 85 ADLAGVRPWLEA---LARIEAGSLDAADYEclgerwdirqrLADALAAEGLGHLRADTPS----------ERLSGGECMR 151
Cdd:TIGR02868 411 VSVCAQDAHLFDttvRENLRLARPDATDEE-----------LWAALERVGLADWLRALPDgldtvlgeggARLSGGERQR 479
|
170 180
....*....|....*....|....
gi 2316862561 152 VALLGAFLDDADFLILDEPSNPLD 175
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLD 503
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
356-490 |
6.44e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.93 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVG--------AAYLDQR---------LSLLDHGRG 418
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT--VLVAgddvealsARAASRRvasvpqdtsLSFEFDVRQ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 419 VLEQLLEVNRSRGESW-------LRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDL 490
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWtetdraaVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATP--VLLLDEPTASLDI 172
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
356-513 |
6.88e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.79 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAG------QRAPLAGTCAVTVGA-----AYLDQRLSLLDH--------- 415
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsGHIRFHGTDVSRLHArdrkvGFVFQHYALFRHmtvfdniaf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 416 GRGVLE---------------QLLEvnrsrgeswlrtrLAQLGLPAERLAqpcATLSGGERLKAALALVLyADRPaQLLL 480
Cdd:PRK10851 98 GLTVLPrrerpnaaaikakvtQLLE-------------MVQLAHLADRYP---AQLSGGQKQRVALARAL-AVEP-QILL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316862561 481 LDEPDNHLDLVARQALETMLRQYRGAL----LVVSHD 513
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHD 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-171 |
7.24e-09 |
|
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: 56.29 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptvaDLA 88
Cdd:cd03224 16 LFGVSLTVPEGEI-------------VALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR-----------------DIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPWlealARIEAG------------------SLDAADYecLGERWDIRQRLADALA-----AEglghlRADTPSERLS 145
Cdd:cd03224 66 GLPPH----ERARAGigyvpegrrifpeltveeNLLLGAY--ARRRAKRKARLERVYElfprlKE-----RRKQLAGTLS 134
|
170 180
....*....|....*....|....*.
gi 2316862561 146 GGECMRVALLGAFLDDADFLILDEPS 171
Cdd:cd03224 135 GGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
369-513 |
7.77e-09 |
|
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: 56.54 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGA---------------AYLDQRLSLLDHGR-----GVLEQLLEVNR 428
Cdd:cd03295 30 LVLIGPSGSGKTTTMKMINRLIEPTSGE--IFIDGedireqdpvelrrkiGYVIQQIGLFPHMTveeniALVPKLLKWPK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 429 SRGESWLRTRLAQLGLPAERLAQ--PcATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQALE----TMLRQ 502
Cdd:cd03295 108 EKIRERADELLALVGLDPAEFADryP-HELSGGQQQRVGVARALAADPP--LLLMDEPFGALDPITRDQLQeefkRLQQE 184
|
170
....*....|.
gi 2316862561 503 YRGALLVVSHD 513
Cdd:cd03295 185 LGKTIVFVTHD 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-175 |
8.49e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.41 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylAQQLEPADYP 82
Cdd:COG4525 17 GQPQPALQDVSLTIESGEFVV-------------ALGASGCGKTTLLNLIAGFLAPSSGEITLDGV----PVTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADLAGVRPWLEALARIEAG----SLDAAdyeclgERwdiRQRLADALAAEGLGHLrADTPSERLSGGECMRVALLGAF 158
Cdd:COG4525 80 VVFQKDALLPWLNVLDNVAFGlrlrGVPKA------ER---RARAEELLALVGLADF-ARRRIWQLSGGMRQRVGIARAL 149
|
170
....*....|....*..
gi 2316862561 159 LDDADFLILDEPSNPLD 175
Cdd:COG4525 150 AADPRFLLMDEPFGALD 166
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-175 |
9.18e-09 |
|
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: 55.97 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptvaDLA 88
Cdd:cd03261 16 LKGVDLDVRRGEIL-------------AIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-----------------DIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPWLEALARIEAG----------SLDAAD--------YECLGERWdIRQRLADALAAEGLGHLRADTPSErLSGGECM 150
Cdd:cd03261 66 GLSEAELYRLRRRMGmlfqsgalfdSLTVFEnvafplreHTRLSEEE-IREIVLEKLEAVGLRGAEDLYPAE-LSGGMKK 143
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLD 168
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
307-514 |
9.75e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 307 ERLD--REVREAAREVEEASPLLLDSPDAELAAQRriVELK---GAVLphlrgpLREIDLLLSGPRRLALVGPNGSGKST 381
Cdd:COG4178 333 DRLAgfEEALEAADALPEAASRIETSEDGALALED--LTLRtpdGRPL------LEDLSLSLKPGERLLITGPSGSGKST 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 382 LLRLLAG---------QRAPLAGTcavtvgaAYLDQRLSLLDhgrGVL-EQLL--EVNRSRGESWLRTRLAQLGLP--AE 447
Cdd:COG4178 405 LLRAIAGlwpygsgriARPAGARV-------LFLPQRPYLPL---GTLrEALLypATAEAFSDAELREALEAVGLGhlAE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 448 RLAQPCA---TLSGGERLKAALALVLYAdRPaQLLLLDEPDNHLDLVARQALETMLRQ--YRGALLVVSHDP 514
Cdd:COG4178 475 RLDEEADwdqVLSLGEQQRLAFARLLLH-KP-DWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRS 544
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
37-175 |
1.06e-08 |
|
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: 55.93 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaQQLEPA-DYPTVADLAGVRPWLEALARIeAGSLDAADYEC-LG 114
Cdd:TIGR01184 16 LIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-----QITEPGpDRMVVFQNYSLLPWLTVRENI-ALAVDRVLPDLsKS 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316862561 115 ERwdiRQRLADALAAEGLGHlRADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:TIGR01184 90 ER---RAIVEEHIALVGLTE-AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
369-484 |
1.13e-08 |
|
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: 55.52 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAV---TVGAAYLDQR----LSLLDHGRG------VLEQLLEVNRSRGESWL 435
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrDITGLPPHERaragIGYVPEGRRifpeltVEENLLLGAYARRRAKR 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 436 RTRLAQ-LGL-P--AERLAQPCATLSGGER--LKAALALVLyadRPaQLLLLDEP 484
Cdd:cd03224 109 KARLERvYELfPrlKERRKQLAGTLSGGEQqmLAIARALMS---RP-KLLLLDEP 159
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
356-519 |
1.14e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTC-----AVTVGAAYLDQRLSLLDHGRGVLEQL------- 423
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqSIKKDLCTYQKQLCFVGHRSGINPYLtlrencl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 LEVNRSRGESWLrTRLAQLGLPAERLAQPCATLSGGERLKAALaLVLYADRpAQLLLLDEPDNHLDLVARQALETMLRQY 503
Cdd:PRK13540 97 YDIHFSPGAVGI-TELCRLFSLEHLIDYPCGLLSSGQKRQVAL-LRLWMSK-AKLWLLDEPLVALDELSLLTIITKIQEH 173
|
170
....*....|....*....
gi 2316862561 504 R---GALLVVSHDPWFLRR 519
Cdd:PRK13540 174 RakgGAVLLTSHQDLPLNK 192
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
370-521 |
1.17e-08 |
|
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: 55.31 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLR----LLAGQRAP----------LAGTCAVTvgaAYLDQRLSLLDHGRGVLEQLLEVNRS-----R 430
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPnskggahdpkLIREGEVR---AQVKLAFENANGKKYTITRSLAILENvifchQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 431 GES-WLrtrlaqlglpaerLAQPCATLSGGERLKAALALVL----YADRPAQLLLLDEPDNHLD-----LVARQALETML 500
Cdd:cd03240 103 GESnWP-------------LLDMRGRCSGGEKVLASLIIRLalaeTFGSNCGILALDEPTTNLDeenieESLAEIIEERK 169
|
170 180
....*....|....*....|.
gi 2316862561 501 RQYRGALLVVSHDPWFLRRLG 521
Cdd:cd03240 170 SQKNFQLIVITHDEELVDAAD 190
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-170 |
1.19e-08 |
|
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: 55.17 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQlepadyp 82
Cdd:cd03250 15 QETSFTLKDINLEVPKGEL-------------VAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 tvadlagvrPWlealarIEAGSLdaADYECLGERWDIrQRLADALAAeglGHLRADTPS----------ER---LSGGEC 149
Cdd:cd03250 75 ---------PW------IQNGTI--RENILFGKPFDE-ERYEKVIKA---CALEPDLEIlpdgdlteigEKginLSGGQK 133
|
170 180
....*....|....*....|.
gi 2316862561 150 MRVALLGAFLDDADFLILDEP 170
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDP 154
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-170 |
1.31e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.63 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG------RVRYLAQ-------- 74
Cdd:COG4586 38 VDDISFTIEPGEIV-------------GFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRigvvfgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 75 -QLEPadyptvaDLAgVRPWLEALARIEagSLDAADYEclgERWDirqRLADALaaeGLGHLrADTPSERLSGGECMRVA 153
Cdd:COG4586 105 sQLWW-------DLP-AIDSFRLLKAIY--RIPDAEYK---KRLD---ELVELL---DLGEL-LDTPVRQLSLGQRMRCE 164
|
170
....*....|....*..
gi 2316862561 154 LLGAFLDDADFLILDEP 170
Cdd:COG4586 165 LAAALLHRPKILFLDEP 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-175 |
1.38e-08 |
|
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: 55.19 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 18 DGSLLFSDLDETFDTRHT-GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQLEPADYPTVADLAGVRPWLEA 96
Cdd:cd03231 11 DGRALFSGLSFTLAAGEAlQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 97 LARIEAGSLDAADYECLgerwdirqrlaDALAAEGLGHLRaDTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03231 91 LENLRFWHADHSDEQVE-----------EALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
369-504 |
1.43e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 56.27 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVgaayLDQRLSLLDHG--------RG------VLEQLL------EVNR 428
Cdd:COG4152 30 FGLLGPNGAGKTTTIRIILGILAPDSGE--VLW----DGEPLDPEDRRrigylpeeRGlypkmkVGEQLVylarlkGLSK 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 429 SRGESWLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLRQYR 504
Cdd:COG4152 104 AEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAAL-LHDP-ELLILDEPFSGLDPVNVELLKDVIRELA 176
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
368-513 |
1.56e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 368 RLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVtVG-------AAYLD-------QR------LSLLDHGRgVLEQLLEVN 427
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-LGyvpfkrrKEFARrigvvfgQRsqlwwdLPAIDSFR-LLKAIYRIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 428 RSRgeswLRTRLAQ----LGLpAERLAQPCATLSGGERLKAALALVLYaDRPaQLLLLDEPDNHLDLVARQALETMLRQY 503
Cdd:COG4586 128 DAE----YKKRLDElvelLDL-GELLDTPVRQLSLGQRMRCELAAALL-HRP-KILFLDEPTIGLDVVSKEAIREFLKEY 200
|
170
....*....|....
gi 2316862561 504 ---RGA-LLVVSHD 513
Cdd:COG4586 201 nreRGTtILLTSHD 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-175 |
1.58e-08 |
|
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: 55.19 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 35 TGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrVRYLAqqLEPADYPT--VADLAGVRPWLE-----ALARIEAGSLDA 107
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTA--APPADRPVsmLFQENNLFAHLTveqnvGLGLSPGLKLTA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316862561 108 ADyeclgerwdiRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03298 104 ED----------RQAIEVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-175 |
1.72e-08 |
|
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: 55.07 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGS--------VRRQGRVR----YL 72
Cdd:cd03265 12 DFEAVRGVSFRVRRG--------EIF-----GLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVRrrigIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 73 AQqlepadYPTVADLAGVRPWLEALARIeagsldaadYECLGERWdiRQRLADALAAEGLGHLRaDTPSERLSGGECMRV 152
Cdd:cd03265 79 FQ------DLSVDDELTGWENLYIHARL---------YGVPGAER--RERIDELLDFVGLLEAA-DRLVKTYSGGMRRRL 140
|
170 180
....*....|....*....|...
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLD 163
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
370-512 |
1.92e-08 |
|
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: 53.59 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPlagtcavtvgaayldqrlslldhgrgvleqllevnrSRGESWLRTRLAQLGLPAERL 449
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKP------------------------------------DSGEILVDGKEVSFASPRDAR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 450 AQPCAT---LSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQYRG---ALLVVSH 512
Cdd:cd03216 74 RAGIAMvyqLSVGERQMVEIARALARN--ARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
350-519 |
1.95e-08 |
|
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: 55.27 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 350 PHLRGPLREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV------TVGAAYLDQ--------------- 408
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinKLKGKALRQlrrqigmifqqfnli 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 409 -RLSLLD---HGRgvleqLLEVNRSRGESWLRTR---------LAQLGLpAERLAQPCATLSGGERLKAALALVLYADrp 475
Cdd:cd03256 91 eRLSVLEnvlSGR-----LGRRSTWRSLFGLFPKeekqralaaLERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQ-- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316862561 476 AQLLLLDEPDNHLD-LVARQALETMLR--QYRGALLVVS-HDPWFLRR 519
Cdd:cd03256 163 PKLILADEPVASLDpASSRQVMDLLKRinREEGITVIVSlHQVDLARE 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-213 |
2.02e-08 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 55.05 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-VRYLAQqlepadyptvADL 87
Cdd:COG1136 24 LRGVSLSIEAGEFVA-------------IVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdISSLSE----------REL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 88 AGVR--------------PWLEALARIE-AGSLDAADyeclgeRWDIRQRLADALAAEGLGHLRADTPSErLSGGECMRV 152
Cdd:COG1136 81 ARLRrrhigfvfqffnllPELTALENVAlPLLLAGVS------RKERRERARELLERVGLGDRLDHRPSQ-LSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLDgPARALL-----RARLAAWDGGLLLVSHDRELLEGMQRIVELS 213
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLD-SKTGEEvlellRELNRELGTTIVMVTHDPELAARADRVIRLR 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
370-513 |
2.24e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.56 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTC-------------AVTVGAAYLDQRL---------SLLDHGR----GVLEQL 423
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsskAFARKVAYLPQQLpaaegmtvrELVAIGRypwhGALGRF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 LEVNRSRGESwlrtRLAQLGLP--AERLAQpcaTLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDlVARQ----ALE 497
Cdd:PRK10575 121 GAADREKVEE----AISLVGLKplAHRLVD---SLSGGERQRAWIAMLVAQD--SRCLLLDEPTSALD-IAHQvdvlALV 190
|
170
....*....|....*..
gi 2316862561 498 TMLRQYRG-ALLVVSHD 513
Cdd:PRK10575 191 HRLSQERGlTVIAVLHD 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
370-484 |
2.44e-08 |
|
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: 54.86 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGT-----CAVT---------VGAAYLDQ------RLSLLDHGRGVLEqLLEVNRS 429
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIVGLVKPDSGKilldgQDITklpmhkrarLGIGYLPQeasifrKLTVEENILAVLE-IRGLSKK 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 430 RGESWLRTRLAQLGLpaERLA-QPCATLSGGERLKAALALVLYADrpAQLLLLDEP 484
Cdd:cd03218 109 EREEKLEELLEEFHI--THLRkSKASSLSGGERRRVEIARALATN--PKFLLLDEP 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-175 |
2.44e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLA--------------Q 74
Cdd:COG1129 20 LDGVSLELRPGEV-------------HALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprdaqaagiaiihQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 75 QLEPADYPTVAD-LagvrpWLEALARiEAGSLDAAdyeclgerwDIRQRLADALAAEGLgHLRADTPSERLSGGECMRVA 153
Cdd:COG1129 87 ELNLVPNLSVAEnI-----FLGREPR-RGGLIDWR---------AMRRRARELLARLGL-DIDPDTPVGDLSVAQQQLVE 150
|
170 180
....*....|....*....|..
gi 2316862561 154 LLGAFLDDADFLILDEPSNPLD 175
Cdd:COG1129 151 IARALSRDARVLILDEPTASLT 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-175 |
2.81e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.41 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylaqqLEPAdyp 82
Cdd:PRK13635 17 DAATYALKDVSFSVYEGEWV-------------AIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV------LSEE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADlagVRpwlealARIE----------AGSLDAAD----YECLG-ERWDIRQRLADALAAEGLGHLRADTPSeRLSGG 147
Cdd:PRK13635 75 TVWD---VR------RQVGmvfqnpdnqfVGATVQDDvafgLENIGvPREEMVERVDQALRQVGMEDFLNREPH-RLSGG 144
|
170 180
....*....|....*....|....*...
gi 2316862561 148 ECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-175 |
2.96e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.08 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-VRYLAQQL-------- 76
Cdd:PRK13639 15 TEALKGINFKAEKGEMV-------------ALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYDKKSLlevrktvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 ----EPADY---PTVADLAGVRPWLEALARIEagsldaadyeclgerwdIRQRLADALAAEGLGHLrADTPSERLSGGEC 149
Cdd:PRK13639 82 ivfqNPDDQlfaPTVEEDVAFGPLNLGLSKEE-----------------VEKRVKEALKAVGMEGF-ENKPPHHLSGGQK 143
|
170 180
....*....|....*....|....*.
gi 2316862561 150 MRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
356-526 |
2.97e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVtvgaayLDQRLSLLDH-GRGVL--EQLLEVNRS--- 429
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL------VGQPLHQMDEeARAKLraKHVGFVFQSfml 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 ----------------RGESWLRTR------LAQLGLpAERLAQPCATLSGGERLKAALALVlYADRPAqLLLLDEPDNH 487
Cdd:PRK10584 100 iptlnalenvelpallRGESSRQSRngakalLEQLGL-GKRLDHLPAQLSGGEQQRVALARA-FNGRPD-VLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2316862561 488 LDlvaRQA-------LETMLRQYRGALLVVSHDPWFL----RRLGL-DGVL 526
Cdd:PRK10584 177 LD---RQTgdkiadlLFSLNREHGTTLILVTHDLQLAarcdRRLRLvNGQL 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
370-513 |
3.21e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.70 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTCAV------TVGAAYLDQRLSLLD---------------------HGRGVL-- 420
Cdd:COG4604 31 ALIGPNGAGKSTLLSMISRLLPPDSGEVLVdgldvaTTPSRELAKRLAILRqenhinsrltvrelvafgrfpYSKGRLta 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 421 EQLLEVNRSrgeswlrtrLAQLGLpaERLAQ-PCATLSGGERLKAALALVLyadrpAQ---LLLLDEPDNHLDLvaRQAL 496
Cdd:COG4604 111 EDREIIDEA---------IAYLDL--EDLADrYLDELSGGQRQRAFIAMVL-----AQdtdYVLLDEPLNNLDM--KHSV 172
|
170 180
....*....|....*....|....
gi 2316862561 497 ETMlRQYRGA-------LLVVSHD 513
Cdd:COG4604 173 QMM-KLLRRLadelgktVVIVLHD 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
315-518 |
3.27e-08 |
|
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: 56.35 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 315 EAAREVEEASPLLldspdaelaaqrRIVELKGAVLPHLRGPLREID---LLLSGPRRLALVGPNGSGKSTLLRLLAGQRA 391
Cdd:TIGR03269 268 EKECEVEVGEPII------------KVRNVSKRYISVDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 392 PLAGTCAVTVGAAYLD--------------------QRLSLLDHgRGVLEQL-----LEVNRSRGESWLRTRLAQLGLPA 446
Cdd:TIGR03269 336 PTSGEVNVRVGDEWVDmtkpgpdgrgrakryigilhQEYDLYPH-RTVLDNLteaigLELPDELARMKAVITLKMVGFDE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 447 ER----LAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALETMLRQYRGAL----LVVSHDPWFLR 518
Cdd:TIGR03269 415 EKaeeiLDKYPDELSEGERHRVALAQVLI--KEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqtfIIVSHDMDFVL 492
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
366-522 |
4.39e-08 |
|
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: 52.38 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 366 PRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQRLSLLDHGRGVLEQLlevnrsrgeswlrtrlaqlglp 445
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 446 aerlaqpcaTLSGGERLKAALALVLYadRPAQLLLLDEPDNHLD---------LVARQALETMLRQYRGALLVVSHDPWF 516
Cdd:smart00382 60 ---------SGSGELRLRLALALARK--LKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEKD 128
|
....*.
gi 2316862561 517 LRRLGL 522
Cdd:smart00382 129 LGPALL 134
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-175 |
5.20e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.23 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR------VRYLAQQLep 78
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLV-------------GLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsARAASRRV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 79 ADYPTVADLA---GVRPWLEALARIEAGSLDAADYeclgerwDIRQRLADALAAEGLGHLrADTPSERLSGGECMRVALL 155
Cdd:PRK09536 80 ASVPQDTSLSfefDVRQVVEMGRTPHRSRFDTWTE-------TDRAAVERAMERTGVAQF-ADRPVTSLSGGERQRVLLA 151
|
170 180
....*....|....*....|
gi 2316862561 156 GAFLDDADFLILDEPSNPLD 175
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLD 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-175 |
5.85e-08 |
|
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: 53.74 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 2 TNTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------------- 67
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIF-------------GIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 68 --RVRYLAQQLEPADYPTVAD-------LAGVrpwlealarieagsldaadyeclgERWDIRQRLADALAAEGLGHLRAD 138
Cdd:cd03258 81 rrRIGMIFQHFNLLSSRTVFEnvalpleIAGV------------------------PKAEIEERVLELLELVGLEDKADA 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316862561 139 TPSErLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03258 137 YPAQ-LSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
37-175 |
6.77e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKS-LLARLlAGhLQPSSGSVRRQG------------RVR-YLAQQLEPA-DYPTVADLAGVRPwleALARIE 101
Cdd:PRK03695 27 LVGPNGAGKStLLARM-AG-LLPGSGSIQFAGqpleawsaaelaRHRaYLSQQQTPPfAMPVFQYLTLHQP---DKTRTE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 102 AgSLDAADYECLgerwdiRQRLADALAaeglghlradTPSERLSGGECMRVALLGAFLD-------DADFLILDEPSNPL 174
Cdd:PRK03695 102 A-VASALNEVAE------ALGLDDKLG----------RSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
.
gi 2316862561 175 D 175
Cdd:PRK03695 165 D 165
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
38-175 |
7.73e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.53 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 38 VGRNGVGKSLLARLLAGHLQPSSGSVrrqgrvrylaqqlepadyptvadLAGVRPWLEALARIEAGSLDA--------AD 109
Cdd:PRK11247 44 VGRSGCGKSTLLRLLAGLETPSAGEL-----------------------LAGTAPLAEAREDTRLMFQDArllpwkkvID 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 110 YECLGERWDIRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK11247 101 NVGLGLKGQWRDAALQALAAVGLADRANEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-175 |
8.06e-08 |
|
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: 52.05 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPADyptvADLA 88
Cdd:cd03216 16 LDGVSLSVRRGE-------------VHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE---VSFASPRD----ARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPwlealarieagsldaadyeclgerwdIRQrladalaaeglghlradtpserLSGGECMRVALLGAFLDDADFLILD 168
Cdd:cd03216 76 GIAM--------------------------VYQ----------------------LSVGERQMVEIARALARNARLLILD 107
|
....*..
gi 2316862561 169 EPSNPLD 175
Cdd:cd03216 108 EPTAALT 114
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-170 |
8.49e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGsllfsdldetfdtRHTGLVGRNGVGKSLLARLLAGHLQPSSGSV------------RRQ--GRVR 70
Cdd:NF033858 13 KTVALDDVSLDIPAG-------------CMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdmadarhRRAvcPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 71 YLAQQLEPADYPTVAdlagVRPWLEALARIEAgsLDAAdyeclgERwdiRQRLADALAAEGLGHLrADTPSERLSGGECM 150
Cdd:NF033858 80 YMPQGLGKNLYPTLS----VFENLDFFGRLFG--QDAA------ER---RRRIDELLRATGLAPF-ADRPAGKLSGGMKQ 143
|
170 180
....*....|....*....|
gi 2316862561 151 RVALLGAFLDDADFLILDEP 170
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEP 163
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
370-512 |
8.75e-08 |
|
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: 52.53 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLagtcaVTVGAAYLDqrlslldhGRGVLEqlLEVN-RSRgeswlrtrlaqLGL---- 444
Cdd:cd03217 30 ALMGPNGSGKSTLAKTIMGHPKYE-----VTEGEILFK--------GEDITD--LPPEeRAR-----------LGIflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 445 --PAE----RLAQPC----ATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLRQYRG---ALLVVS 511
Cdd:cd03217 84 qyPPEipgvKNADFLryvnEGFSGGEKKRNEILQLL-LLEP-DLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIIT 161
|
.
gi 2316862561 512 H 512
Cdd:cd03217 162 H 162
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
370-513 |
8.99e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPlagtcavTVGAAYLD------------------QRLSLLDHgrGVLEQ-----LLEV 426
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQP-------TAGQIMLDgvdlshvppyqrpinmmfQSYALFPH--MTVEQniafgLKQD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 427 NRSRGEswLRTRLAQ-LGLP--AERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLD--LVARQALET--M 499
Cdd:PRK11607 120 KLPKAE--IASRVNEmLGLVhmQEFAKRKPHQLSGGQRQRVALARSL-AKRP-KLLLLDEPMGALDkkLRDRMQLEVvdI 195
|
170
....*....|....
gi 2316862561 500 LRQYRGALLVVSHD 513
Cdd:PRK11607 196 LERVGVTCVMVTHD 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-170 |
9.40e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 54.00 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVR------------RQGRVRYLAQQl 76
Cdd:COG1118 18 LDDVSLEIASGELV-------------ALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlppRERRVGFVFQH- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 ePADYP--TVAD--LAG--VRPWLEAlarieagsldaadyeclgerwDIRQRLADALAAEGLGHLrADT-PSErLSGGEC 149
Cdd:COG1118 84 -YALFPhmTVAEniAFGlrVRPPSKA---------------------EIRARVEELLELVQLEGL-ADRyPSQ-LSGGQR 139
|
170 180
....*....|....*....|.
gi 2316862561 150 MRVALLGAFLDDADFLILDEP 170
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEP 160
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-175 |
1.07e-07 |
|
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: 53.07 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLFSDLDETFDTRHT-GLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------------RVRYL 72
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFlVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 73 AQQLEPADYPTVADLAGVRPWLEALARieagsldaadyeclgERwdIRQRLADALAAEGL--GHLRADTPSErLSGGECM 150
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPK---------------EK--IRERADELLALVGLdpAEFADRYPHE-LSGGQQQ 142
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALD 167
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
369-513 |
1.17e-07 |
|
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: 53.20 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAV----TVGAAYLD---QRLSLL----DH---GRGVLEQL---LEvNR--S 429
Cdd:TIGR04520 31 VAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdgldTLDEENLWeirKKVGMVfqnpDNqfvGATVEDDVafgLE-NLgvP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 RGESWLRTR--LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQA-LETM--LRQYR 504
Cdd:TIGR04520 110 REEMRKRVDeaLKLVGMEDFRDREP-HLLSGGQKQRVAIAGVL-AMRP-DIIILDEATSMLDPKGRKEvLETIrkLNKEE 186
|
170
....*....|.
gi 2316862561 505 GaLLVVS--HD 513
Cdd:TIGR04520 187 G-ITVISitHD 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-175 |
1.29e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 17 PDGSLLFSDLD-ETFDTRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRrQGRVRYLAQQLEPADYPTVADLAGVRPWLE 95
Cdd:PRK13643 16 PFASRALFDIDlEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 96 ALARIEAGSLDAAdyecLG-ERWDIRQRLADALAAEGL------GHLRADTPSErLSGGECMRVALLGAFLDDADFLILD 168
Cdd:PRK13643 95 SQLFEETVLKDVA----FGpQNFGIPKEKAEKIAAEKLemvglaDEFWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLD 169
|
....*..
gi 2316862561 169 EPSNPLD 175
Cdd:PRK13643 170 EPTAGLD 176
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-175 |
1.36e-07 |
|
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: 52.67 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptvaDLA 88
Cdd:COG1127 21 LDGVSLDVPRG--------EI-----LAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ-----------------DIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPwlEALARIEA------------GSLDAAD--------YECLGERwDIRQRLADALAAEGLGHLRADTPSErLSGGE 148
Cdd:COG1127 71 GLSE--KELYELRRrigmlfqggalfDSLTVFEnvafplreHTDLSEA-EIRELVLEKLELVGLPGAADKMPSE-LSGGM 146
|
170 180
....*....|....*....|....*..
gi 2316862561 149 CMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLD 173
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-513 |
1.41e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAP------------------------------LAGTCAVTVGAAYLDQrlsLLDHGRG 418
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPnlgkfddppdwdeildefrgselqnyftklLEGDVKVIVKPQYVDL---IPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 419 VLEQLLEVNRSRGEswLRTRLAQLGLpAERLAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLvaRQALeT 498
Cdd:cd03236 106 KVGELLKKKDERGK--LDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALA--RDADFYFFDEPSSYLDI--KQRL-N 177
|
170 180
....*....|....*....|.
gi 2316862561 499 MLRQYRG------ALLVVSHD 513
Cdd:cd03236 178 AARLIRElaeddnYVLVVEHD 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
369-514 |
1.42e-07 |
|
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: 51.78 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGA------------AYLDQRLSLLDHgRGVLEQLLEVNRSRGeswlr 436
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGrpldkrsfrkiiGYVPQDDILHPT-LTVRETLMFAAKLRG----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 437 trlaqlglpaerlaqpcatLSGGERLKAALALVLYAdRPaQLLLLDEPDNHLDLVARQALETMLRQYR--GALLVVS-HD 513
Cdd:cd03213 112 -------------------LSGGERKRVSIALELVS-NP-SLLFLDEPTSGLDSSSALQVMSLLRRLAdtGRTIICSiHQ 170
|
.
gi 2316862561 514 P 514
Cdd:cd03213 171 P 171
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-514 |
1.46e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.74 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLL------------AGQRAPLAGTCAVTVGAAYLDQR-------------L 410
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiydskikVDGKVLYFGKDIFQIDAIKLRKEvgmvfqqpnpfphL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 411 SLLDH------GRGVLEQLlEVNRSRGESwlrtrLAQLGLPAE---RLAQPCATLSGGE--RLKAALALVLyadRPaQLL 479
Cdd:PRK14246 106 SIYDNiayplkSHGIKEKR-EIKKIVEEC-----LRKVGLWKEvydRLNSPASQLSGGQqqRLTIARALAL---KP-KVL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316862561 480 LLDEPDNHLDLVARQALETMLRQYRG--ALLVVSHDP 514
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNP 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
370-512 |
1.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYL-----DQRLSLLDHGRGVL-----EQLLE-------------- 425
Cdd:PRK13634 37 AIIGHTGSGKSTLLQHLNGLLQPTSGT--VTIGERVItagkkNKKLKPLRKKVGIVfqfpeHQLFEetvekdicfgpmnf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 -VNRSRGESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETM---LR 501
Cdd:PRK13634 115 gVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVL-AMEP-EVLVLDEPTAGLDPKGRKEMMEMfykLH 192
|
170
....*....|..
gi 2316862561 502 QYRGALLV-VSH 512
Cdd:PRK13634 193 KEKGLTTVlVTH 204
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
370-512 |
1.74e-07 |
|
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: 51.70 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTL---------------LR-------LLAG-QRAPLAGTCAVTVGAAYLDQRLSLLDHGRgvLEQLLEv 426
Cdd:cd03278 26 AIVGPNGSGKSNIidairwvlgeqsaksLRgekmsdvIFAGsETRKPANFAEVTLTFDNSDGRYSIISQGD--VSEIIE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 427 nrSRGEswlrtRLAQLGLpaerlaqpcatLSGGERLKAALALV--LYADRPAQLLLLDEPDNHLDL--VARQAleTMLRQ 502
Cdd:cd03278 103 --APGK-----KVQRLSL-----------LSGGEKALTALALLfaIFRVRPSPFCVLDEVDAALDDanVERFA--RLLKE 162
|
170
....*....|..
gi 2316862561 503 YRGA--LLVVSH 512
Cdd:cd03278 163 FSKEtqFIVITH 174
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-212 |
1.77e-07 |
|
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: 51.06 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqlepadyp 82
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESL-------------AIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 tvadlAGVRPWLEALARIEAGSLdAADYEclgerwdirqrladalaaeglghLRADTPSER-LSGGECMRVALLGAFLDD 161
Cdd:cd03246 64 -----ADISQWDPNELGDHVGYL-PQDDE-----------------------LFSGSIAENiLSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 162 ADFLILDEPSNPLDGPARALLRARLAAWDGG---LLLVSHDRELLEGMQRIVEL 212
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETLASADRILVL 168
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-175 |
1.82e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 54.02 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGSLLFSDLDetFDTR---HTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyp 82
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDIS--LTIPpgeTVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV-------------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 tvaDLAGVRpwLEALAR-------------------IEAGSLDAADYEclgerwdIRQRLADALAAE-------GLghlr 136
Cdd:COG1132 403 ---DIRDLT--LESLRRqigvvpqdtflfsgtirenIRYGRPDATDEE-------VEEAAKAAQAHEfiealpdGY---- 466
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316862561 137 aDTP-SER---LSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG1132 467 -DTVvGERgvnLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-175 |
1.95e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 53.18 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-----------VRYLAQqle 77
Cdd:COG3842 21 LDDVSLSIEPGEFVA-------------LLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 78 paDYP-----TVAD-----LagvrpwlealariEAGSLDAADyeclgerwdIRQRLADALAAEGLGHLRADTPSErLSGG 147
Cdd:COG3842 85 --DYAlfphlTVAEnvafgL-------------RMRGVPKAE---------IRARVAELLELVGLEGLADRYPHQ-LSGG 139
|
170 180
....*....|....*....|....*....
gi 2316862561 148 ECMRVALLGAFLDDADFLILDEP-SNpLD 175
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPlSA-LD 167
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-175 |
1.97e-07 |
|
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: 52.34 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-----------VRYLAQQLE 77
Cdd:cd03296 18 LDDVSLDIPSGEL-------------VALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 78 PADYPTVADlaGVRPWLEALARIEAGSLDaadyeclgerwDIRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGA 157
Cdd:cd03296 85 LFRHMTVFD--NVAFGLRVKPRSERPPEA-----------EIRAKVHELLKLVQLDWLADRYPAQ-LSGGQRQRVALARA 150
|
170
....*....|....*...
gi 2316862561 158 FLDDADFLILDEPSNPLD 175
Cdd:cd03296 151 LAVEPKVLLLDEPFGALD 168
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
369-513 |
1.98e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQRlSLLDHGR--GVLEQ-----------------LLEvNR- 428
Cdd:PRK13635 36 VAIVGHNGSGKSTLAKLLNGLLLPEAGT--ITVGGMVLSEE-TVWDVRRqvGMVFQnpdnqfvgatvqddvafGLE-NIg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 429 -SRGESWLRTR--LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLRQYR- 504
Cdd:PRK13635 112 vPREEMVERVDqaLRQVGMEDFLNREP-HRLSGGQKQRVAIAGVL-ALQP-DIIILDEATSMLDPRGRREVLETVRQLKe 188
|
170
....*....|..
gi 2316862561 505 -GALLVVS--HD 513
Cdd:PRK13635 189 qKGITVLSitHD 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-171 |
2.31e-07 |
|
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: 51.91 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptvaDLA 88
Cdd:COG0410 19 LHGVSLEVEEGEI-------------VALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE-----------------DIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPWlealARIEAG------------------SLDAADYeCLGERWDIRQRLADALA-----AEglghlRADTPSERLS 145
Cdd:COG0410 69 GLPPH----RIARLGigyvpegrrifpsltveeNLLLGAY-ARRDRAEVRADLERVYElfprlKE-----RRRQRAGTLS 138
|
170 180
....*....|....*....|....*.
gi 2316862561 146 GGECMRVALLGAFLDDADFLILDEPS 171
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
369-484 |
2.78e-07 |
|
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: 51.52 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCA--------------VTVGAAYLDQrlslldhGRGVLEQL-----LEV--- 426
Cdd:COG0410 32 VALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglpphriARLGIGYVPE-------GRRIFPSLtveenLLLgay 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 427 --NRSRGESWLRTRLAQLgLP--AERLAQPCATLSGGER--LKAALALVLyadRPaQLLLLDEP 484
Cdd:COG0410 105 arRDRAEVRADLERVYEL-FPrlKERRRQRAGTLSGGEQqmLAIGRALMS---RP-KLLLLDEP 163
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-175 |
2.80e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.11 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 4 TSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaQQLEPADYPT 83
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRI-------------AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG------EPITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 84 VADLAGV----------RPWLE---ALARIEAGsLDAADyeclgerwdIRQRLADALAAEGLGHLRADTPsERLSGGECM 150
Cdd:PRK13652 76 VRKFVGLvfqnpddqifSPTVEqdiAFGPINLG-LDEET---------VAHRVSSALHMLGLEELRDRVP-HHLSGGEKK 144
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13652 145 RVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
356-513 |
3.28e-07 |
|
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: 51.10 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV------TVGAAYLD-----QRLSLLDHGRgVLEQL- 423
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdvtDLPPKDRDiamvfQNYALYPHMT-VYDNIa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 --LEVNRSRGESWLR--TRLAQLGLPAERLAQPCATLSGGERLKAAL--ALVlyadRPAQLLLLDEP----DNHLDLVAR 493
Cdd:cd03301 95 fgLKLRKVPKDEIDErvREVAELLQIEHLLDRKPKQLSGGQRQRVALgrAIV----REPKVFLMDEPlsnlDAKLRVQMR 170
|
170 180
....*....|....*....|
gi 2316862561 494 QALETMLRQYRGALLVVSHD 513
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHD 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
356-514 |
3.45e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.19 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAP------LAGTCAVTVGA-----------AYLDQRLSLLDHGRG 418
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPtsgtyrVAGQDVATLDAdalaqlrrehfGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 419 vlEQLLEV-----NRSRGESWLRTR--LAQLGLpAERLAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLV 491
Cdd:PRK10535 104 --AQNVEVpavyaGLERKQRLLRAQelLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALM--NGGQVILADEPTGALDSH 178
|
170 180
....*....|....*....|....*.
gi 2316862561 492 ARQALETMLRQYRG---ALLVVSHDP 514
Cdd:PRK10535 179 SGEEVMAILHQLRDrghTVIIVTHDP 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
371-501 |
3.82e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQRLSLLDHGRGVLEQL--LEVNRSRGESWL--------RTRLA 440
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGK--ITVLGVPVPARARLARARIGVVPQFdnLDLEFTVRENLLvfgryfgmSTREI 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 441 QLGLPA-------ERLAQ-PCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLR 501
Cdd:PRK13536 150 EAVIPSllefarlESKADaRVSDLSGGMKRRLTLARALIND--PQLLILDEPTTGLDPHARHLIWERLR 216
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
354-514 |
4.09e-07 |
|
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: 50.73 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 354 GPLRE---IDLLLSGPRRLALV-GPNGSGKSTLLRL----LAGQRAPLAGTCAVTVGAAYLDQRLSL-LDHGRGvlEQLL 424
Cdd:cd03279 12 GPFREeqvIDFTGLDNNGLFLIcGPTGAGKSTILDAityaLYGKTPRYGRQENLRSVFAPGEDTAEVsFTFQLG--GKKY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 425 EVNRSRG---ESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVL--------YADRPAQLLLLDEPDNHLDLVAR 493
Cdd:cd03279 90 RVERSRGldyDQFTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLALalsevlqnRGGARLEALFIDEGFGTLDPEAL 169
|
170 180
....*....|....*....|....
gi 2316862561 494 QALETMLRQYRG---ALLVVSHDP 514
Cdd:cd03279 170 EAVATALELIRTenrMVGVISHVE 193
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
356-514 |
4.25e-07 |
|
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: 49.84 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAG---------QRAPLAGTcavtvgaAYLDQRLSLldhGRGVLEQllev 426
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwpwgsgriGMPEGEDL-------LFLPQRPYL---PLGTLRE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 427 nrsrgeswlrtrlaQLGLPAERlaqpcaTLSGGERLKAALALVLYAdRPaQLLLLDEPDNHLDLVARQALETMLRQYRGA 506
Cdd:cd03223 83 --------------QLIYPWDD------VLSGGEQQRLAFARLLLH-KP-KFVFLDEATSALDEESEDRLYQLLKELGIT 140
|
....*...
gi 2316862561 507 LLVVSHDP 514
Cdd:cd03223 141 VISVGHRP 148
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-175 |
4.31e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqlEPADYPTVADLA 88
Cdd:PRK13539 18 FSGLSFTLAAGEALV-------------LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---------GDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 -------GVRPWLEALARIE--AGSLDAADYeclgerwdirqRLADALAAEGLGHLrADTPSERLSGGECMRVALLGAFL 159
Cdd:PRK13539 76 hylghrnAMKPALTVAENLEfwAAFLGGEEL-----------DIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLV 143
|
170
....*....|....*.
gi 2316862561 160 DDADFLILDEPSNPLD 175
Cdd:PRK13539 144 SNRPIWILDEPTAALD 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-175 |
4.31e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 8 TLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQ------------ 75
Cdd:TIGR00957 653 TLNGITFSIPEGALV-------------AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQawiqndslreni 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 76 -----LEPADYPTVADLAGVRPWLEALARieagsldaadyeclGERWDIRQRLADalaaeglghlradtpserLSGGECM 150
Cdd:TIGR00957 720 lfgkaLNEKYYQQVLEACALLPDLEILPS--------------GDRTEIGEKGVN------------------LSGGQKQ 767
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
356-513 |
4.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV---TVGAAYLDQRLSLLDHGRGVL-----EQLLEVN 427
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVddiTITHKTKDKYIRPVRKRIGMVfqfpeSQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 428 RSRG---------------ESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVA 492
Cdd:PRK13646 103 VEREiifgpknfkmnldevKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMN--PDIIVLDEPTAGLDPQS 180
|
170 180
....*....|....*....|....*
gi 2316862561 493 RQALETMLRQYR----GALLVVSHD 513
Cdd:PRK13646 181 KRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
370-512 |
4.97e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.22 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAplagtCAVTVGAAYLDQRlSLLD---HGR----------------GV-LEQLL--EVN 427
Cdd:COG0396 30 AIMGPNGSGKSTLAKVLMGHPK-----YEVTSGSILLDGE-DILElspDERaragiflafqypveipGVsVSNFLrtALN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 428 RSRGE--------SWLRTRLAQLGLPAERLAQPC-ATLSGGERLKA--ALALVLyadRPAqLLLLDEPDNHLDLVARQAL 496
Cdd:COG0396 104 ARRGEelsareflKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNeiLQMLLL---EPK-LAILDETDSGLDIDALRIV 179
|
170
....*....|....*....
gi 2316862561 497 ETMLRQYRG---ALLVVSH 512
Cdd:COG0396 180 AEGVNKLRSpdrGILIITH 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-175 |
5.15e-07 |
|
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: 52.41 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 8 TLDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSG---------------SVRRQgrVRYL 72
Cdd:TIGR02203 347 ALDSISLVIEPGET-------------VALVGRSGSGKSTLVNLIPRFYEPDSGqilldghdladytlaSLRRQ--VALV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 73 AQQLEPADyPTVADlagvrpwlealaRIEAGSLDAADYEclgerwDIRQRLADALAAEGLGHLRA--DTP----SERLSG 146
Cdd:TIGR02203 412 SQDVVLFN-DTIAN------------NIAYGRTEQADRA------EIERALAAAYAQDFVDKLPLglDTPigenGVLLSG 472
|
170 180
....*....|....*....|....*....
gi 2316862561 147 GECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
350-512 |
5.61e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 51.27 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 350 PHLRGPLREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV---TVGAAYLDQRLSLLDHGRGVLEQLLE- 425
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdiVVSSTSKQKEIKPVRKKVGVVFQFPEs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 -------------------VNRSRGESWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDN 486
Cdd:PRK13643 96 qlfeetvlkdvafgpqnfgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL-AMEP-EVLVLDEPTA 173
|
170 180
....*....|....*....|....*....
gi 2316862561 487 HLDLVARQALETM---LRQYRGALLVVSH 512
Cdd:PRK13643 174 GLDPKARIEMMQLfesIHQSGQTVVLVTH 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-175 |
5.68e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.24 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqLEPADYP 82
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFL-------------VILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--------LDTSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADL---AGV---RPWLEALARIEAGSLdAADYECLG-ERWDIRQRLADALAAEGLGHLRADTPsERLSGGECMRVALL 155
Cdd:PRK13633 79 NLWDIrnkAGMvfqNPDNQIVATIVEEDV-AFGPENLGiPPEEIRERVDESLKKVGMYEYRRHAP-HLLSGGQKQRVAIA 156
|
170 180
....*....|....*....|
gi 2316862561 156 GAFLDDADFLILDEPSNPLD 175
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLD 176
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
373-513 |
8.64e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.10 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 373 GPNGSGKSTLLRLLAGQRAP------LAGTCAVTVG-------AAYLDQRLSLLdhGRGVLEQLLEVNRSRG----ESWL 435
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISPtsgtllFEGEDISTLKpeiyrqqVSYCAQTPTLF--GDTVYDNLIFPWQIRNqqpdPAIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 436 RTRLAQLGLPAERLAQPCATLSGGERLKAALALVLyaDRPAQLLLLDEPDNHLDLVARQALETMLRQY----RGALLVVS 511
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVLLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVT 195
|
..
gi 2316862561 512 HD 513
Cdd:PRK10247 196 HD 197
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
7-175 |
9.08e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.52 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGsllfsdldetfdtRHTGLVGRNGVGKSLLARLLAGHLQPSSgsvrrqGRVRYLAQQLEPADYPTVAD 86
Cdd:PRK13648 23 FTLKDVSFNIPKG-------------QWTSIVGHNGSGKSTIAKLMIGIEKVKS------GEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 87 LAGV---RPWLEALARI----EAGSLD--AADYECLGERwdIRQRLADALAAEglghlRADTPSERLSGGECMRVALLGA 157
Cdd:PRK13648 84 HIGIvfqNPDNQFVGSIvkydVAFGLEnhAVPYDEMHRR--VSEALKQVDMLE-----RADYEPNALSGGQKQRVAIAGV 156
|
170
....*....|....*...
gi 2316862561 158 FLDDADFLILDEPSNPLD 175
Cdd:PRK13648 157 LALNPSVIILDEATSMLD 174
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-169 |
1.01e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLFSDLDETFdtrHTG----LVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------RVRYLA 73
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTI---KRGellfLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpvtaeqPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 74 -------------QQLEPADYPtvADLAGVRPWLEALarieagsldaadyeclgerwdirqRLADALAAEglGHLRADTp 140
Cdd:PRK10522 398 lfsavftdfhlfdQLLGPEGKP--ANPALVEKWLERL------------------------KMAHKLELE--DGRISNL- 448
|
170 180
....*....|....*....|....*....
gi 2316862561 141 seRLSGGECMRVALLGAFLDDADFLILDE 169
Cdd:PRK10522 449 --KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-204 |
1.15e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.09 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVR--YLAQQLEpadyptv 84
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIV-------------GVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKlaYVDQSRD------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 85 aDLAGVRPWLEALArieagslDAADYECLGERwDIRQRladalAAEGLGHLRADTPSER---LSGGECMRVALLGAFLDD 161
Cdd:TIGR03719 396 -ALDPNKTVWEEIS-------GGLDIIKLGKR-EIPSR-----AYVGRFNFKGSDQQKKvgqLSGGERNRVHLAKTLKSG 461
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316862561 162 ADFLILDEPSNPLDGPARALLRARLAAWDGGLLLVSHDRELLE 204
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLD 504
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-511 |
1.18e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.01 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLR----LLAGQRAP-----LAGTCAVTVGAAYLDQRLSLLDHGRgVLEQLLEV 426
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAgshieLLGRTVQREGRLARDIRKSRANTGY-IFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 427 NR----------SRGE--------SWLRTRLAQLGLPA-ERLA------QPCATLSGGERLKAALALVLYadRPAQLLLL 481
Cdd:PRK09984 99 NRlsvlenvligALGStpfwrtcfSWFTREQKQRALQAlTRVGmvhfahQRVSTLSGGQQQRVAIARALM--QQAKVILA 176
|
170 180 190
....*....|....*....|....*....|...
gi 2316862561 482 DEPDNHLD-LVARQALETM--LRQYRGALLVVS 511
Cdd:PRK09984 177 DEPIASLDpESARIVMDTLrdINQNDGITVVVT 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-170 |
1.34e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAqqlEPAD-------- 80
Cdd:COG3845 21 NDDVSLTVRPGEIH-------------ALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR---SPRDaialgigm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 -------YP--TVAD--LAGVRPWLEALARIEAgsldaadyeclgerwdIRQRLADALAAEGLgHLRADTPSERLSGGEC 149
Cdd:COG3845 85 vhqhfmlVPnlTVAEniVLGLEPTKGGRLDRKA----------------ARARIRELSERYGL-DVDPDAKVEDLSVGEQ 147
|
170 180
....*....|....*....|.
gi 2316862561 150 MRVALLGAFLDDADFLILDEP 170
Cdd:COG3845 148 QRVEILKALYRGARILILDEP 168
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
369-514 |
1.39e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 50.46 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVG-------------AAYLDQRLSLLDHG------------RGVLEQl 423
Cdd:COG3839 32 LVLLGPSGCGKSTLLRMIAGLEDPTSGE--ILIGgrdvtdlppkdrnIAMVFQSYALYPHMtvyeniafplklRKVPKA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 lEVNRsRGESWLRT-RLAQLglpAERLAqpcATLSGGERLKAAL--ALVlyadRPAQLLLLDEPDNHLDLVARQALETML 500
Cdd:COG3839 109 -EIDR-RVREAAELlGLEDL---LDRKP---KQLSGGQRQRVALgrALV----REPKVFLLDEPLSNLDAKLRVEMRAEI 176
|
170
....*....|....*...
gi 2316862561 501 RQY---RGALLV-VSHDP 514
Cdd:COG3839 177 KRLhrrLGTTTIyVTHDQ 194
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-176 |
1.54e-06 |
|
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: 50.90 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVR------------RQGR-V 69
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVL-------------GVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwdreELGRhI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 70 RYLAQQLE--PAdypTVAD----LAGVRPwlealARIEAgsldAAdyeclgerwdirqRLADAlaaeglgH---LRA--- 137
Cdd:COG4618 409 GYLPQDVElfDG---TIAEniarFGDADP-----EKVVA----AA-------------KLAGV-------HemiLRLpdg 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316862561 138 -DTP----SERLSGGECMRVALLGAFLDDADFLILDEP-SNpLDG 176
Cdd:COG4618 457 yDTRigegGARLSGGQRQRIGLARALYGDPRLVVLDEPnSN-LDD 500
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-175 |
1.58e-06 |
|
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: 49.18 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPAD---- 80
Cdd:cd03301 12 NVTALDDLNLDIADGEFVV-------------LLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD---VTDLPPKDrdia 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 --------YP--TVAD-------LAGVRpwlealarieagsldaadyeclgeRWDIRQRLADALAAEGLGHLRADTPSeR 143
Cdd:cd03301 76 mvfqnyalYPhmTVYDniafglkLRKVP------------------------KDEIDERVREVAELLQIEHLLDRKPK-Q 130
|
170 180 190
....*....|....*....|....*....|..
gi 2316862561 144 LSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
369-513 |
1.60e-06 |
|
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: 49.54 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGaaylDQRLSLLD-HGRGV--------LEQLLEV--N-------RSR 430
Cdd:cd03300 29 FTLLGPSGCGKTTLLRLIAGFETPTSGE--ILLD----GKDITNLPpHKRPVntvfqnyaLFPHLTVfeNiafglrlKKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 431 GESWLRTR----LAQLGLPAERLAQPcATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLRQYRGA 506
Cdd:cd03300 103 PKAEIKERvaeaLDLVQLEGYANRKP-SQLSGGQQQRVAIARAL-VNEP-KVLLLDEPLGALDLKLRKDMQLELKRLQKE 179
|
170
....*....|.
gi 2316862561 507 L----LVVSHD 513
Cdd:cd03300 180 LgitfVFVTHD 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-175 |
1.61e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.73 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQLE-------- 77
Cdd:PRK13647 18 TKALKGLSLSIPEGS-------------KTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvglv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 78 ---PADY---PTVADLAGVRPWLEALARIEagsldaadyeclgerwdIRQRLADALAAEGLGHLRaDTPSERLSGGECMR 151
Cdd:PRK13647 85 fqdPDDQvfsSTVWDDVAFGPVNMGLDKDE-----------------VERRVEEALKAVRMWDFR-DKPPYHLSYGQKKR 146
|
170 180
....*....|....*....|....
gi 2316862561 152 VALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLD 170
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
456-514 |
1.79e-06 |
|
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: 51.13 E-value: 1.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 456 LSGGERLKAALALV--LYADRPAQLLLLDEPDNHLDLVARQALETMLRQYR--GALLVVSHDP 514
Cdd:pfam02463 1078 LSGGEKTLVALALIfaIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSknAQFIVISLRE 1140
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-212 |
1.83e-06 |
|
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: 49.01 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 2 TNTSTLTLDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPADY 81
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEV-------------TALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 82 PTVADLAGVRPWLEA--LARIEAGSLDAADYECLGErwdirqrLADALAAEGLGHLRADTPSE-------RLSGGECMRV 152
Cdd:cd03248 87 HSKVSLVGQEPVLFArsLQDNIAYGLQSCSFECVKE-------AAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAW--DGGLLLVSHDRELLEGMQRIVEL 212
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVERADQILVL 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
370-519 |
1.93e-06 |
|
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: 48.09 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRllagqraplagTCAVTVGAAYLDQRLSLLDHGRGV-LEQLlevnrsrgeswlrTRLAQLGLPAER 448
Cdd:cd03238 25 VVTGVSGSGKSTLVN-----------EGLYASGKARLISFLPKFSRNKLIfIDQL-------------QFLIDVGLGYLT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316862561 449 LAQPCATLSGGERLKAALALVLYADRPAQLLLLDEPDNHLDlvaRQALETMLRQYRG------ALLVVSHDPWFLRR 519
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLH---QQDINQLLEVIKGlidlgnTVILIEHNLDVLSS 154
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-175 |
1.94e-06 |
|
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: 49.10 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSV---------------RRQ-GRVRYL 72
Cdd:cd03256 17 LKDVSLSINPGEF-------------VALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalRQLrRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 73 AQQLEPADYPTVAD-----LAGVRPWLEALArieaGSLDAADyeclgerwdiRQRLADALAAEGLGHL---RADTpserL 144
Cdd:cd03256 84 FQQFNLIERLSVLEnvlsgRLGRRSTWRSLF----GLFPKEE----------KQRALAALERVGLLDKayqRADQ----L 145
|
170 180 190
....*....|....*....|....*....|.
gi 2316862561 145 SGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-175 |
2.03e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 2 TNTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaQQLEPADY 81
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWL-------------SIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG------DLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 82 PTVADLAGV---RPWLEAL-ARIEAgslDAA-DYECLG-ERWDIRQRLADALAAEGLGHLRADTPSeRLSGGECMRVALL 155
Cdd:PRK13650 77 WDIRHKIGMvfqNPDNQFVgATVED---DVAfGLENKGiPHEEMKERVNEALELVGMQDFKEREPA-RLSGGQKQRVAIA 152
|
170 180
....*....|....*....|
gi 2316862561 156 GAFLDDADFLILDEPSNPLD 175
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLD 172
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
354-501 |
2.05e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.61 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 354 GPLREIDLLLSGPRRL-ALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQRLSLLDHGRGVLeqLLEVNRSRGE 432
Cdd:COG3950 12 RGFEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLIL--YYGTSRLLLD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 433 SWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLYADRPAQLLLLDEPDNHLDLVaRQALETMLR 501
Cdd:COG3950 90 GPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAV-REALNKLLP 157
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-175 |
2.08e-06 |
|
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: 49.15 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaQQLEPADYP 82
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGK-------------KVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG------QDIREVTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADLAGVRPWLEAL------ARIEAGSLDAADYEC-----LGERWDIRQRLADA----LAAEGLghlradtpseRLSGG 147
Cdd:cd03253 72 SLRRAIGVVPQDTVLfndtigYNIRYGRPDATDEEVieaakAAQIHDKIMRFPDGydtiVGERGL----------KLSGG 141
|
170 180
....*....|....*....|....*...
gi 2316862561 148 ECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-175 |
2.58e-06 |
|
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: 48.77 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 5 STLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVrylAQQLEPADYP-- 82
Cdd:cd03300 12 GFVALDGVSLDIKEGEFF-------------TLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD---ITNLPPHKRPvn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADLAGVRPWLEALARIEAG----SLDAADyeclgerwdIRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAF 158
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGlrlkKLPKAE---------IKERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARAL 145
|
170
....*....|....*..
gi 2316862561 159 LDDADFLILDEPSNPLD 175
Cdd:cd03300 146 VNEPKVLLLDEPLGALD 162
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-175 |
2.58e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 50.23 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 12 VSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLqPSSGSVRRQGRVRylaQQLEPADyptvadlagvr 91
Cdd:PRK11174 369 LNFTLPAGQ-------------RIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIEL---RELDPES----------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 92 pWLEALA------RIEAGSL---------DAADYEclgerwdIRQRLADALAAEGLGHLRA--DTP----SERLSGGECM 150
Cdd:PRK11174 421 -WRKHLSwvgqnpQLPHGTLrdnvllgnpDASDEQ-------LQQALENAWVSEFLPLLPQglDTPigdqAAGLSVGQAQ 492
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLD 517
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
339-529 |
2.65e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 339 RRIVELKGAVLPHLRGPLREIDLLLSGPRRLALVGPNGSGKS----TLLRLLAGQRAPLAGTCA---VTVGAAYLDQRL- 410
Cdd:PRK10418 2 PQQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLldgKPVAPCALRGRKi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 411 ---------------SLLDHGRgvlEQLLEVNRSRGESWLRTRLAQLGLP-AERLAQPCA-TLSGGERLKAALALVLYAD 473
Cdd:PRK10418 82 atimqnprsafnplhTMHTHAR---ETCLALGKPADDATLTAALEAVGLEnAARVLKLYPfEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 474 RPaqLLLLDEPDNHLDLVArQA-----LETMLRQYRGALLVVSHDPWFLRRLGLD-GVLAAG 529
Cdd:PRK10418 159 AP--FIIADEPTTDLDVVA-QArildlLESIVQKRALGMLLVTHDMGVVARLADDvAVMSHG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
37-175 |
2.65e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.70 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLARLLAGHLQPSSGSVR-----------RQGRVRYLAQQLEPADYPTVADlaGVRPWLEALARIEAGSL 105
Cdd:PRK10851 33 LLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlhaRDRKVGFVFQHYALFRHMTVFD--NIAFGLTVLPRRERPNA 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 106 DAadyeclgerwdIRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK10851 111 AA-----------IKAKVTQLLEMVQLAHLADRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
356-514 |
2.73e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQ-RAPLAGTCAVTVGAAYLD---------QRLSLLdhgRGVLEQLLE 425
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDlTGGGAPRGARVTGDVTLNgeplaaidaPRLARL---RAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 VN-----------------RSRGESWLRTR------LAQLGLPAeRLAQPCATLSGGERLKAALALVLY-------ADRP 475
Cdd:PRK13547 94 PAfafsareivllgryphaRRAGALTHRDGeiawqaLALAGATA-LVGRDVTTLSGGELARVQFARVLAqlwpphdAAQP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316862561 476 AQLLLLDEPDNHLDLVARQAL----ETMLRQYRGALLVVSHDP 514
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLldtvRRLARDWNLGVLAIVHDP 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
369-513 |
3.07e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAV---TVGAAYLDQRLSLLDHGRGVLEQLLEVN------------------ 427
Cdd:PRK13641 36 VALVGHTGSGKSTLMQHFNALLKPSSGTITIagyHITPETGNKNLKKLRKKVSLVFQFPEAQlfentvlkdvefgpknfg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 428 ------RSRGESWLRtrlaQLGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLVARQALETMLR 501
Cdd:PRK13641 116 fsedeaKEKALKWLK----KVGLSEDLISKSPFELSGGQMRRVAIAGVM-AYEP-EILCLDEPAAGLDPEGRKEMMQLFK 189
|
170
....*....|....*
gi 2316862561 502 QYRGA---LLVVSHD 513
Cdd:PRK13641 190 DYQKAghtVILVTHN 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
371-484 |
3.26e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.49 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAG----------------------QRAPLagtcavtvGAAYLDQ------RLSLLDHGRGVLEq 422
Cdd:COG1137 34 LLGPNGAGKTTTFYMIVGlvkpdsgrifldgedithlpmhKRARL--------GIGYLPQeasifrKLTVEDNILAVLE- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 423 LLEVNRSRGESWLRTRLAQLGLpaERLA-QPCATLSGGERLKAALALVLyADRPaQLLLLDEP 484
Cdd:COG1137 105 LRKLSKKEREERLEELLEEFGI--THLRkSKAYSLSGGERRRVEIARAL-ATNP-KFILLDEP 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
371-501 |
3.47e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.03 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRAPLAGT---CAVTV--GAAYLDQRLSL------LDHGRGVLEQLLEVNRSRGES--WLRT 437
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSislCGEPVpsRARHARQRVGVvpqfdnLDPDFTVRENLLVFGRYFGLSaaAARA 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316862561 438 RLAQLgLPAERLAQ----PCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLR 501
Cdd:PRK13537 118 LVPPL-LEFAKLENkadaKVGELSGGMKRRLTLARALVND--PDVLVLDEPTTGLDPQARHLMWERLR 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
369-513 |
3.86e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQRLSLLDHGRGVL---------------------------E 421
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLlrtewgfvhqhprdglrmqvsaggnigE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 422 QLLEVN-------RSRGESWLRtrlaQLGLPAERLAQPCATLSGG--ERLKAALALVlyaDRPaQLLLLDEPDNHLDlVA 492
Cdd:PRK11701 115 RLMAVGarhygdiRATAGDWLE----RVEIDAARIDDLPTTFSGGmqQRLQIARNLV---THP-RLVFMDEPTGGLD-VS 185
|
170 180
....*....|....*....|....*.
gi 2316862561 493 RQA-----LETMLRQYRGALLVVSHD 513
Cdd:PRK11701 186 VQArlldlLRGLVRELGLAVVIVTHD 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
360-512 |
3.90e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.72 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 360 DLLLSGPRR--LALVGPNGSGKSTLLRLLAGQRAPlagtcavTVGAAYLDQR-LSLLDH--------------------- 415
Cdd:PRK10790 359 NINLSVPSRgfVALVGHTGSGKSTLASLLMGYYPL-------TEGEIRLDGRpLSSLSHsvlrqgvamvqqdpvvladtf 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 416 ------GR--------GVLE--QLLEVNRSRGESwLRTRLAQLGlpaerlaqpcATLSGGERLKAALALVLYAdrPAQLL 479
Cdd:PRK10790 432 lanvtlGRdiseeqvwQALEtvQLAELARSLPDG-LYTPLGEQG----------NNLSVGQKQLLALARVLVQ--TPQIL 498
|
170 180 190
....*....|....*....|....*....|....*
gi 2316862561 480 LLDEPDNHLDLVARQALETMLRQYR--GALLVVSH 512
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVRehTTLVVIAH 533
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-175 |
4.08e-06 |
|
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: 47.18 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadypTVADLA 88
Cdd:cd03229 16 LNDVSLNIEAGEI-------------VALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE--------------DLTDLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPwlealarieagsldaadyeclgerwDIRQRLADALAAEGL-GHL-RADTPSERLSGGECMRVALLGAFLDDADFLI 166
Cdd:cd03229 69 DELP-------------------------PLRRRIGMVFQDFALfPHLtVLENIALGLSGGQQQRVALARALAMDPDVLL 123
|
....*....
gi 2316862561 167 LDEPSNPLD 175
Cdd:cd03229 124 LDEPTSALD 132
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-175 |
4.17e-06 |
|
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: 48.16 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSG-SVRRQGRVRY---------------- 71
Cdd:COG1119 19 LDDISWTVKPGE-------------HWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGgedvwelrkriglvsp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 72 -LAQQLEPADypTVADL------AGVRPWLEalarieagsLDAADyeclgerwdiRQRLADALAAEGLGHLrADTPSERL 144
Cdd:COG1119 86 aLQLRFPRDE--TVLDVvlsgffDSIGLYRE---------PTDEQ----------RERARELLELLGLAHL-ADRPFGTL 143
|
170 180 190
....*....|....*....|....*....|.
gi 2316862561 145 SGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
369-513 |
4.37e-06 |
|
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: 47.18 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAGTcavtvgaayldqrlslldhgrgvleqllevnrsrgESWLRTRLAqlglpaer 448
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDN-----------------------------------DEWDGITPV-------- 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 449 LAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLD----LVARQALETMLRQYRGALLVVSHD 513
Cdd:cd03222 65 YKPQYIDLSGGELQRVAIAAALL--RNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHD 131
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-175 |
4.75e-06 |
|
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: 49.42 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSV----------------RRQGRV-RY 71
Cdd:TIGR03269 300 VDNVSLEVKEG--------EIF-----GIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDGRGRAkRY 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 72 LA--QQlEPADYPTvadlagvRPWLEALAriEAGSLDAADYecLGerwdiRQRLADALAAEGLGHLRADT-----PSErL 144
Cdd:TIGR03269 367 IGilHQ-EYDLYPH-------RTVLDNLT--EAIGLELPDE--LA-----RMKAVITLKMVGFDEEKAEEildkyPDE-L 428
|
170 180 190
....*....|....*....|....*....|.
gi 2316862561 145 SGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-175 |
5.04e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVR--RQGRVRYLA---QQLepady 81
Cdd:PRK13540 15 PLLQQISFHLPAGGLLH-------------LKGSNGAGKTTLLKLIAGLLNPEKGEILfeRQSIKKDLCtyqKQL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 82 PTVADLAGVRPWLealarieagsldAADYECLgerWDIRQRLADALAAE-----GLGHLrADTPSERLSGGECMRVALLG 156
Cdd:PRK13540 77 CFVGHRSGINPYL------------TLRENCL---YDIHFSPGAVGITElcrlfSLEHL-IDYPCGLLSSGQKRQVALLR 140
|
170
....*....|....*....
gi 2316862561 157 AFLDDADFLILDEPSNPLD 175
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALD 159
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-212 |
7.38e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.50 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaQQLEPADYP 82
Cdd:PRK11629 19 SVQTDVLHNVSFSIGEGEMM-------------AIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG------QPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 TVADLAGVR-----------PWLEALARIEAGSLDAADyeclgERWDIRQRLADALAAEGLGHLRADTPSErLSGGECMR 151
Cdd:PRK11629 80 AKAELRNQKlgfiyqfhhllPDFTALENVAMPLLIGKK-----KPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 152 VALLGAFLDDADFLILDEPSNPLDGPAR----ALLRARLAAWDGGLLLVSHDRELLEGMQRIVEL 212
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNAdsifQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-175 |
8.04e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaQQLEPADYPTVADL- 87
Cdd:PRK11308 31 LDGVSFTLERGKTL-------------AVVGESGCGKSTLARLLTMIETPTGGELYYQG------QDLLKADPEAQKLLr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 88 -----------AGVRP------WLEALARIEAgSLDAAdyeclgERwdiRQRLADALAAEGLGHLRADTPSERLSGGECM 150
Cdd:PRK11308 92 qkiqivfqnpyGSLNPrkkvgqILEEPLLINT-SLSAA------ER---REKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALD 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
356-494 |
8.80e-06 |
|
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: 48.75 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPlagtcavTVGAAYLDQRLSLLDHGRGVLEQLLEVNRSRGESWL 435
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP-------SEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYD 514
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 436 RTRLAQ----------LGLPAER----LAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQ 494
Cdd:TIGR01271 515 EYRYTSvikacqleedIALFPEKdktvLGEGGITLSGGQRARISLARAVYKD--ADLYLLDSPFTHLDVVTEK 585
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
356-513 |
9.22e-06 |
|
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: 46.98 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV--------------TVGaaYLDQRLSlLDHGRGVLE 421
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprevrrRIG--IVFQDLS-VDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 422 QLLEVNRSRGESW--LRTRLAQ------LGLPAERLAqpcATLSGG--ERLKAALALVlyaDRPaQLLLLDEPDNHLDLV 491
Cdd:cd03265 93 NLYIHARLYGVPGaeRRERIDElldfvgLLEAADRLV---KTYSGGmrRRLEIARSLV---HRP-EVLFLDEPTIGLDPQ 165
|
170 180
....*....|....*....|....*.
gi 2316862561 492 ARQAL----ETMLRQYRGALLVVSHD 513
Cdd:cd03265 166 TRAHVweyiEKLKEEFGMTILLTTHY 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
356-512 |
1.01e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.24 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVG--------------------------------- 402
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR--ILIDgvdirdltleslrrqigvvpqdtflfsgtiren 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 403 ------------------AAYLDQRLSLLDHGrgvleqllevnrsrgeswLRTRLAQLGlpaerlaqpcATLSGGERLKA 464
Cdd:COG1132 434 irygrpdatdeeveeaakAAQAHEFIEALPDG------------------YDTVVGERG----------VNLSGGQRQRI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 465 ALALVLYADrpAQLLLLDEPDNHLDLVA----RQALETMLRQYrgALLVVSH 512
Cdd:COG1132 486 AIARALLKD--PPILILDEATSALDTETealiQEALERLMKGR--TTIVIAH 533
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-175 |
1.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.43 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 18 DGSLLFSDLDETFDTRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVryLAQQLEPADYPTVADLAG-VRPWLEA 96
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTL--ITSTSKNKDIKQIRKKVGlVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 97 LARIEAGSLDAAdyecLG-ERWDIRQRLADALAAEGLG------HLRADTPSErLSGGECMRVALLGAFLDDADFLILDE 169
Cdd:PRK13649 97 QLFEETVLKDVA----FGpQNFGVSQEEAEALAREKLAlvgiseSLFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDE 171
|
....*.
gi 2316862561 170 PSNPLD 175
Cdd:PRK13649 172 PTAGLD 177
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-170 |
1.09e-05 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 46.88 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG----------RVR----YLAQ 74
Cdd:TIGR04406 17 VNDVSLSVKSGEIV-------------GLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGqdithlpmheRARlgigYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 75 QlepadyPTVADLAGVRPWLEALARIEaGSLDAADyeclgerwdiRQRLADALAAE-GLGHLRaDTPSERLSGGECMRVA 153
Cdd:TIGR04406 84 E------ASIFRKLTVEENIMAVLEIR-KDLDRAE----------REERLEALLEEfQISHLR-DNKAMSLSGGERRRVE 145
|
170
....*....|....*..
gi 2316862561 154 LLGAFLDDADFLILDEP 170
Cdd:TIGR04406 146 IARALATNPKFILLDEP 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
370-512 |
1.09e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTC--------------AVTVGAAYLDQRLSL--------------LDHGRGVle 421
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSIlidgqemrfasttaALAAGVAIIYQELHLvpemtvaenlylgqLPHKGGI-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 422 qlleVNRSRGESWLRTRLAQLGL---PAERLaqpcATLSGGER--LKAALALVlyadRPAQLLLLDEPDNHLDLVARQAL 496
Cdd:PRK11288 112 ----VNRRLLNYEAREQLEHLGVdidPDTPL----KYLSIGQRqmVEIAKALA----RNARVIAFDEPTSSLSAREIEQL 179
|
170
....*....|....*....
gi 2316862561 497 ETMLRQYRG---ALLVVSH 512
Cdd:PRK11288 180 FRVIRELRAegrVILYVSH 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
370-512 |
1.24e-05 |
|
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: 46.70 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLL------AGQRAPLAGTCAVTVGAAYLDQRLSLLDHGRGVLEQLLEVNRSRG---ESWLRTRLA 440
Cdd:cd03248 44 ALVGPSGSGKSTVVALLenfyqpQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGlqsCSFECVKEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 441 QLGLPA------------ERLAQPCATLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALETMLRQY--RGA 506
Cdd:cd03248 124 AQKAHAhsfiselasgydTEVGEKGSQLSGGQKQRVAIARALI--RNPQVLILDEATSALDAESEQQVQQALYDWpeRRT 201
|
....*.
gi 2316862561 507 LLVVSH 512
Cdd:cd03248 202 VLVIAH 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-170 |
1.27e-05 |
|
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: 46.77 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG----------RVR----YLAQ 74
Cdd:cd03218 16 VNGVSLSVKQGEIV-------------GLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkRARlgigYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 75 qlEPADYP--TVADlagvrpwlealarieagSLDAAdYECLGERWDIRQRLADALAAE-GLGHLRaDTPSERLSGGECMR 151
Cdd:cd03218 83 --EASIFRklTVEE-----------------NILAV-LEIRGLSKKEREEKLEELLEEfHITHLR-KSKASSLSGGERRR 141
|
170
....*....|....*....
gi 2316862561 152 VALLGAFLDDADFLILDEP 170
Cdd:cd03218 142 VEIARALATNPKFLLLDEP 160
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
370-525 |
1.55e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 46.49 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAplagtCAVTVGAAYL----------DQR-----------------LSLLDHGRGVLEQ 422
Cdd:TIGR01978 30 AIMGPNGSGKSTLSKTIAGHPS-----YEVTSGTILFkgqdllelepDERaraglflafqypeeipgVSNLEFLRSALNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 lleVNRSRGES---------WLRTRLAQLGLPAERLAQPCAT-LSGGERLKAALaLVLYADRPaQLLLLDEPDNHLDLVA 492
Cdd:TIGR01978 105 ---RRSARGEEpldlldfekLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEI-LQMALLEP-KLAILDEIDSGLDIDA 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316862561 493 RQALETMLRQYRG---ALLVVSHDPWFLRRLGLDGV 525
Cdd:TIGR01978 180 LKIVAEGINRLREpdrSFLIITHYQRLLNYIKPDYV 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-177 |
1.81e-05 |
|
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: 47.03 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 35 TGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVryLAQQLEPADYPT-------VADLAGVRPWLEALARIEAGsLDA 107
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT--LFDSRKGIFLPPekrrigyVFQEARLFPHLSVRGNLRYG-MKR 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 108 ADYECLGERWDirqRLADALaaeGLGHLrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLDGP 177
Cdd:TIGR02142 103 ARPSERRISFE---RVIELL---GIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
359-512 |
2.07e-05 |
|
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: 47.70 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 359 IDLLLSGPRR---LALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQRLSLLDHGRGVLEQLLEVNR---SRGE 432
Cdd:TIGR01257 1955 VDRLCVGVRPgecFGLLGVNGAGKTTTFKMLTGDTTVTSGD--ATVAGKSILTNISDVHQNMGYCPQFDAIDDlltGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 433 SWLRTRL----------------AQLGLP--AERLAqpcATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDLVARQ 494
Cdd:TIGR01257 2033 LYLYARLrgvpaeeiekvanwsiQSLGLSlyADRLA---GTYSGGNKRKLSTAIALIGCPP--LVLLDEPTTGMDPQARR 2107
|
170 180
....*....|....*....|..
gi 2316862561 495 AL----ETMLRQYRgALLVVSH 512
Cdd:TIGR01257 2108 MLwntiVSIIREGR-AVVLTSH 2128
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
356-519 |
2.11e-05 |
|
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: 45.54 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQrlslldhgrgvleqllevnrsrgESWL 435
Cdd:cd03250 21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQ-----------------------EPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 436 RTRLAQ----LGLP--AERLAQ---PCA---------------------TLSGGERLKAALALVLYADrpAQLLLLDEP- 484
Cdd:cd03250 78 QNGTIRenilFGKPfdEERYEKvikACAlepdleilpdgdlteigekgiNLSGGQKQRISLARAVYSD--ADIYLLDDPl 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316862561 485 ---DNHldlVAR----QALETMLRQYRGALLvVSHDPWFLRR 519
Cdd:cd03250 156 savDAH---VGRhifeNCILGLLLNNKTRIL-VTHQLQLLPH 193
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
9-204 |
2.65e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 45.71 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrHTgLVGRNGVGKSLLARLLAGH--LQPSSGSVRRQG----------RVR---YLA 73
Cdd:TIGR01978 16 LKGVNLTVKKGEI------------HA-IMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKGqdllelepdeRARaglFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 74 QQLePADYPTVADLAGVRPWLEALARIEA-GSLDAADYECLgerwdirqrLADALAAEGL-GHLRADTPSERLSGGECMR 151
Cdd:TIGR01978 83 FQY-PEEIPGVSNLEFLRSALNARRSARGeEPLDLLDFEKL---------LKEKLALLDMdEEFLNRSVNEGFSGGEKKR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 152 VALLGAFLDDADFLILDEPSNPLDGPARALLRARLAAW---DGGLLLVSHDRELLE 204
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLN 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-175 |
2.73e-05 |
|
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: 45.79 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLFSDLDetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-----------RVRYLAQq 75
Cdd:cd03299 6 LSKDWKEFKLKNVSLEVERGD------YFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 76 lepaDYptvadlaGVRPWLEALARIEAGSLDAadyecLGERWDIRQRLADALAAEGLGHLRADTPsERLSGGECMRVALL 155
Cdd:cd03299 79 ----NY-------ALFPHMTVYKNIAYGLKKR-----KVDKKEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIA 141
|
170 180
....*....|....*....|
gi 2316862561 156 GAFLDDADFLILDEPSNPLD 175
Cdd:cd03299 142 RALVVNPKILLLDEPFSALD 161
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-175 |
2.78e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 46.36 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqlepADYPTVADLA 88
Cdd:PRK13536 57 VNGLSFTVASG--------ECF-----GLLGPNGAGKSTIARMILGMTSPDAGKITVLG-----------VPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 ----GVRPWLEALarieagSLDAADYECL---GERWDIRQRLADALAAEGLGHLR----ADTPSERLSGGECMRVALLGA 157
Cdd:PRK13536 113 rariGVVPQFDNL------DLEFTVRENLlvfGRYFGMSTREIEAVIPSLLEFARleskADARVSDLSGGMKRRLTLARA 186
|
170
....*....|....*...
gi 2316862561 158 FLDDADFLILDEPSNPLD 175
Cdd:PRK13536 187 LINDPQLLILDEPTTGLD 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
370-521 |
2.84e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTC--------------AVTVGAAYLDQRLSLLDH---------GRGVLEQLLEV 426
Cdd:PRK09700 35 ALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhklAAQLGIGIIYQELSVIDEltvlenlyiGRHLTKKVCGV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 427 N-------RSRGESWLRtrlaQLGLPAErLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETM 499
Cdd:PRK09700 115 NiidwremRVRAAMMLL----RVGLKVD-LDEKVANLSISHKQMLEIAKTLMLD--AKVIIMDEPTSSLTNKEVDYLFLI 187
|
170 180
....*....|....*....|....*
gi 2316862561 500 LRQYRG---ALLVVSHDPWFLRRLG 521
Cdd:PRK09700 188 MNQLRKegtAIVYISHKLAEIRRIC 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
356-512 |
2.87e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.74 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGT-------------CAVTVGAAYLDQRLSLLDhgrGVL-E 421
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEillngqpiadyseAALRQAISVVSQRVHLFS---ATLrD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 422 QLLEVNRSRGESWLRTRLAQLGLpaERLAQPCA-----------TLSGGERLKAALALVLYADRPaqLLLLDEPDNHLDL 490
Cdd:PRK11160 433 NLLLAAPNASDEALIEVLQQVGL--EKLLEDDKglnawlgeggrQLSGGEQRRLGIARALLHDAP--LLLLDEPTEGLDA 508
|
170 180
....*....|....*....|....
gi 2316862561 491 VARQALETMLRQY-RG-ALLVVSH 512
Cdd:PRK11160 509 ETERQILELLAEHaQNkTVLMITH 532
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
465-526 |
3.19e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.46 E-value: 3.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 465 ALALVLYADRPAQLLLLDEPDNHLDLVARQALETMLRQY--RGALLVVSHDPWFLRRLGLDGVL 526
Cdd:COG4637 268 ALLAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREAseRTQVIVTTHSPALLDALEPEEVL 331
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
39-175 |
3.41e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 39 GRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQLEPADYptVADLAGVRPWLEALARIEagsldaadYECLGERWD 118
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY--LGHLPGLKADLSTLENLH--------FLCGLHGRR 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316862561 119 IRQRLADALAAEGL-GHlrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13543 114 AKQMPGSALAIVGLaGY--EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
370-502 |
3.91e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTC------AVTVGAAYLDQRLS---------LL-----DHGRGVLEQLLEVNRS 429
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGERqsqfshITRLSFEQLQKLVSdewqrnntdMLspgedDTGRTTAEIIQDEVKD 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 430 RGeswLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLRQ 502
Cdd:PRK10938 113 PA---RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSE--PDLLILDEPFDGLDVASRQQLAELLAS 180
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
356-490 |
4.29e-05 |
|
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: 45.62 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTvgaayldQRLSLLDHGRGVLEQLLEVNRSRGESWL 435
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-------GRISFSSQFSWIMPGTIKENIIFGVSYD 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 436 RTRL------AQL-----GLPAER---LAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDL 490
Cdd:cd03291 126 EYRYksvvkaCQLeeditKFPEKDntvLGEGGITLSGGQRARISLARAVYKD--ADLYLLDSPFGYLDV 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
37-520 |
4.40e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLArLLAGHLQPSSGSVRRQGRVRYLAQQLEPADYPTVADLAGVR-------PW--LEALARIEAG---- 103
Cdd:PRK15134 40 LVGESGSGKSVTA-LSILRLLPSPPVVYPSGDIRFHGESLLHASEQTLRGVRGNKiamifqePMvsLNPLHTLEKQlyev 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 104 -SL------DAADYECLG--ERWDIRQrladalAAEGLghlrADTPSErLSGGECMRVALLGAFLDDADFLILDEPSNPL 174
Cdd:PRK15134 119 lSLhrgmrrEAARGEILNclDRVGIRQ------AAKRL----TDYPHQ-LSGGERQRVMIAMALLTRPELLIADEPTTAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 175 D----GPARALLRARLAAWDGGLLLVSHDrellegmQRIVelstlglrsygggysfyaqsreeareaaerrldqRRLERK 250
Cdd:PRK15134 188 DvsvqAQILQLLRELQQELNMGLLFITHN-------LSIV----------------------------------RKLADR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 251 RQTLamreqqqrqerrqasgrREGKTA--NQAKILLGgfrersevsagklRNAHQAERERLDREVREAAREVEEASPLLL 328
Cdd:PRK15134 227 VAVM-----------------QNGRCVeqNRAATLFS-------------APTHPYTQKLLNSEPSGDPVPLPEPASPLL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 329 DSPDAELAAQRRIVELKGAVLPHLrgPLREIDLLLSGPRRLALVGPNGSGKST----LLRLLAGQRA------------- 391
Cdd:PRK15134 277 DVEQLQVAFPIRKGILKRTVDHNV--VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEiwfdgqplhnlnr 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 392 ----PLAGTCAVTVGAAY--LDQRLSLLDhgrgVLEQLLEV-----NRSRGESWLRTRLAQLGL-PAERLAQPcATLSGG 459
Cdd:PRK15134 355 rqllPVRHRIQVVFQDPNssLNPRLNVLQ----IIEEGLRVhqptlSAAQREQQVIAVMEEVGLdPETRHRYP-AEFSGG 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 460 ERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQALETMLR----QYRGALLVVSHDPWFLRRL 520
Cdd:PRK15134 430 QRQRIAIARALILK--PSLIILDEPTSSLDKTVQAQILALLKslqqKHQLAYLFISHDLHVVRAL 492
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
37-212 |
4.75e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.77 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLARLLAGHLQPSSGsvrrqgRVRYLAQQLEPADYPTVADLAG-----------VRPWLEALARIEAGSL 105
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSG------EVSLVGQPLHQMDEEARAKLRAkhvgfvfqsfmLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 106 DAADYEClgerwDIRQRLADALAAEGLGHlRADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLDGPARALLR-- 183
Cdd:PRK10584 115 LRGESSR-----QSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAdl 188
|
170 180 190
....*....|....*....|....*....|.
gi 2316862561 184 --ARLAAWDGGLLLVSHDRELLEGMQRIVEL 212
Cdd:PRK10584 189 lfSLNREHGTTLILVTHDLQLAARCDRRLRL 219
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
370-502 |
4.78e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 44.22 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLrllagqraplagtCAVTVG----AAYLDQRLSLLDHGRGVLEQlleVNRSRGESWLRTRLaQLgLP 445
Cdd:cd03239 26 AIVGPNGSGKSNIV-------------DAICFVlggkAAKLRRGSLLFLAGGGVKAG---INSASVEITFDKSY-FL-VL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 446 AERLAQpcaTLSGGERLKAALALVLYADR--PAQLLLLDEPDNHLDLVARQALETMLRQ 502
Cdd:cd03239 88 QGKVEQ---ILSGGEKSLSALALIFALQEikPSPFYVLDEIDAALDPTNRRRVSDMIKE 143
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
356-489 |
5.36e-05 |
|
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: 44.88 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV------TVGAAYLD----------QRLSLLDhGRGV 419
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdgtdltLLSGKELRkarrrigmifQHFNLLS-SRTV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 420 LE------QLLEVNRSRGESWLRTRLAQLGLPAERLAQPcATLSGGERLKAALALVLYADrPAqLLLLDEPDNHLD 489
Cdd:cd03258 100 FEnvalplEIAGVPKAEIEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANN-PK-VLLCDEATSALD 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
356-484 |
5.70e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTVGAAYLDQRLSLLDHGRGVL----EQLLEVNRSRG 431
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT--LEIGGNPCARLTPAKAHQLGIYlvpqEPLLFPNLSVK 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 432 ESWLrTRLAQLGLPAERLAQPCATLSGGERLKAALALVLYAD-----------RPAQLLLLDEP 484
Cdd:PRK15439 105 ENIL-FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADrqiveilrglmRDSRILILDEP 167
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-175 |
5.92e-05 |
|
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: 44.48 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAG-----HLQPSSGSVRRQGRVRYLAQQL------- 76
Cdd:cd03260 16 LKDISLDIPKGEI-------------TALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDvlelrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 ------EPADYP-TVADLAGVRPWLEALARIEAgsLDAADYECLgerwdirqRLAdALAAEGLGHLRADtpseRLSGGEC 149
Cdd:cd03260 83 vgmvfqKPNPFPgSIYDNVAYGLRLHGIKLKEE--LDERVEEAL--------RKA-ALWDEVKDRLHAL----GLSGGQQ 147
|
170 180
....*....|....*....|....*.
gi 2316862561 150 MRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALD 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-175 |
7.31e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 44.65 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSV------------------RRQGRV- 69
Cdd:PRK13637 23 LDNVNIEIEDGEFV-------------GLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvklsdirKKVGLVf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 70 RYLAQQLepadyptvadlagvrpWLEALAR-IEAGSLDaadyecLG-ERWDIRQRLADALAAEGLGH--LRADTPSErLS 145
Cdd:PRK13637 90 QYPEYQL----------------FEETIEKdIAFGPIN------LGlSEEEIENRVKRAMNIVGLDYedYKDKSPFE-LS 146
|
170 180 190
....*....|....*....|....*....|
gi 2316862561 146 GGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
120-175 |
7.42e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 44.01 E-value: 7.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 120 RQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG4136 111 RARVEQALEEAGLAGFADRDPAT-LSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-175 |
7.56e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 44.80 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqlEPAdyPTVA 85
Cdd:PRK13537 20 KLVVDGLSFHVQRG--------ECF-----GLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---------EPV--PSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 86 DLA----GVRPWLEALA---RIEAGSLDAADYECLGERwDIRQRLADALAAEGLGHlRADTPSERLSGGECMRVALLGAF 158
Cdd:PRK13537 76 RHArqrvGVVPQFDNLDpdfTVRENLLVFGRYFGLSAA-AARALVPPLLEFAKLEN-KADAKVGELSGGMKRRLTLARAL 153
|
170
....*....|....*..
gi 2316862561 159 LDDADFLILDEPSNPLD 175
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLD 170
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-175 |
7.70e-05 |
|
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: 44.35 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGS--VRRQGRVRYLAQqlepADYPTVAD 86
Cdd:COG4778 27 LDGVSFSVAAGECV-------------ALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDLAQ----ASPREILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 87 L-----AGVRPWLEALARIEAgsLDAAdYECLGERWDIRQRlADALAAEGLGHLRADtpsERL--------SGGECMRVA 153
Cdd:COG4778 90 LrrrtiGYVSQFLRVIPRVSA--LDVV-AEPLLERGVDREE-ARARARELLARLNLP---ERLwdlppatfSGGEQQRVN 162
|
170 180
....*....|....*....|..
gi 2316862561 154 LLGAFLDDADFLILDEPSNPLD 175
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLD 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-175 |
7.78e-05 |
|
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: 43.30 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSLLFSDLDetFDTRHTG---LVGRNGVGKSLLARLLAGhLQPSsgsvrRQGRVrylaqqlepaDYPT 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLS--FEIKPGDrllITGPSGTGKSSLFRALAG-LWPW-----GSGRI----------GMPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 84 VADLAGV--RPWLealariEAGSLdaadyeclgerwdiRQRLADALaaeglghlradtpSERLSGGECMRVALLGAFLDD 161
Cdd:cd03223 63 GEDLLFLpqRPYL------PLGTL--------------REQLIYPW-------------DDVLSGGEQQRLAFARLLLHK 109
|
170
....*....|....
gi 2316862561 162 ADFLILDEPSNPLD 175
Cdd:cd03223 110 PKFVFLDEATSALD 123
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
370-489 |
8.07e-05 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (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: 213241 [Multi-domain] Cd Length: 212 Bit Score: 43.82 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTL---LRLLAGQRA------------------PLAGTCAVTVGAAYLDQRLSL------LDHGR----- 417
Cdd:cd03274 29 AIVGPNGSGKSNVidsMLFVFGFRAskmrqkklsdlihnsaghPNLDSCSVEVHFQEIIDKPLLkskgidLDHNRflilq 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 418 GVLEQLLEVNRsrgESWlrtrlaqlglpaerlaQPCATLSGGERLKAALALV--LYADRPAQLLLLDEPDNHLD 489
Cdd:cd03274 109 GEVEQIAQMPK---KSW----------------KNISNLSGGEKTLSSLALVfaLHHYKPTPLYVMDEIDAALD 163
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
371-532 |
8.41e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 44.61 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRAPLAGtcavtvgaAYLDQRLSLLDHGRGVL---EQLLEVNRSRGESWLRT--------RL 439
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKG--------AVLWQGKPLDYSKRGLLalrQQVATVFQDPEQQIFYTdidsdiafSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 440 AQLGLPAERLA-----------------QPCATLSGGERLKAAL--ALVLyadrPAQLLLLDEPDNHLDLVARQALETML 500
Cdd:PRK13638 104 RNLGVPEAEITrrvdealtlvdaqhfrhQPIQCLSHGQKKRVAIagALVL----QARYLLLDEPTAGLDPAGRTQMIAII 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316862561 501 RQYRGA---LLVVSHD----------PWFLRRlglDGVLAAGAEG 532
Cdd:PRK13638 180 RRIVAQgnhVIISSHDidliyeisdaVYVLRQ---GQILTHGAPG 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
360-513 |
9.08e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 44.37 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 360 DLLLSGPRR--LALVGPNGSGKSTLLRLLAGQRAPLAGTC--------AVTVGAAY-LDQRLSLLDHGRGVLEQL----- 423
Cdd:PRK11831 25 NISLTVPRGkiTAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipAMSRSRLYtVRKRMSMLFQSGALFTDMnvfdn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 424 ----LEVNRSRGESWLRT----RLAQLGLPAERLAQPcATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVARQA 495
Cdd:PRK11831 105 vaypLREHTQLPAPLLHStvmmKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALE--PDLIMFDEPFVGQDPITMGV 181
|
170 180
....*....|....*....|..
gi 2316862561 496 LETMLRQYRGAL----LVVSHD 513
Cdd:PRK11831 182 LVKLISELNSALgvtcVVVSHD 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-175 |
9.47e-05 |
|
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: 44.01 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQL-PDGSLLFSDLD-ETFDTRHTGLVGRNGVGKSLLARLLAGHLQPSSGSV---------------RRQgrV 69
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISlRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpawlRRQ--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 70 RYLAQQLEPADYPTVADLAGVRPWLEALARIEAGSL-DAADYEClgerwDIRQRLADALAAEGLGhlradtpserLSGGE 148
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLaGAHDFIS-----ELPEGYDTIVGEQGAG----------LSGGQ 143
|
170 180
....*....|....*....|....*..
gi 2316862561 149 CMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALD 170
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-175 |
1.08e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 43.92 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylAQQLEPADYPTVADLA 88
Cdd:PRK11248 17 LEDINLTLESGELLV-------------VLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK----PVEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 89 GVRPWLEALARIEAGsLDAADYEcLGERWDIRQRLADALAAEGLGHLRAdtpsERLSGGECMRVALLGAFLDDADFLILD 168
Cdd:PRK11248 80 GLLPWRNVQDNVAFG-LQLAGVE-KMQRLEIAHQMLKKVGLEGAEKRYI----WQLSGGQRQRVGIARALAANPQLLLLD 153
|
....*..
gi 2316862561 169 EPSNPLD 175
Cdd:PRK11248 154 EPFGALD 160
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-169 |
1.16e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQlepadyp 82
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVI-------------GLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAIS------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 83 tvadlAGVRPWLEALARIEAGSLdaadyeCLG-ERWDIRQRLADALAAEGLGHLrADTPSERLSGGecMRvALLGAFLD- 160
Cdd:PRK13546 94 -----AGLSGQLTGIENIEFKML------CMGfKRKEIKAMTPKIIEFSELGEF-IYQPVKKYSSG--MR-AKLGFSINi 158
|
170
....*....|.
gi 2316862561 161 --DADFLILDE 169
Cdd:PRK13546 159 tvNPDILVIDE 169
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
456-514 |
1.23e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.30 E-value: 1.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 456 LSGGE-RLKAALALVLYADRPAQLLLLDEPDNHLDLVARQALETMLR---QYRGALLVVSHDP 514
Cdd:pfam13304 237 LSDGTkRLLALLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKelsRNGAQLILTTHSP 299
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
316-512 |
1.32e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.84 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 316 AAREVEEasplLLDSPDAELAAQRRIVELKGA---------VLPH----LRGPLreiDLLLSGPRRLALVGPNGSGKSTL 382
Cdd:PRK11174 320 AAESLVT----FLETPLAHPQQGEKELASNDPvtieaedleILSPdgktLAGPL---NFTLPAGQRIALVGPSGAGKTSL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 383 LRLLAGqraplagtcavtvgaaYLDQRLSLLDHGrgvleqlLEVNRSRGESWlRTRLAQLG----LPAE------RLAQP 452
Cdd:PRK11174 393 LNALLG----------------FLPYQGSLKING-------IELRELDPESW-RKHLSWVGqnpqLPHGtlrdnvLLGNP 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 453 CAT----------------------------------LSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALET 498
Cdd:PRK11174 449 DASdeqlqqalenawvseflpllpqgldtpigdqaagLSVGQAQRLALARALL--QPCQLLLLDEPTASLDAHSEQLVMQ 526
|
250
....*....|....*.
gi 2316862561 499 MLRQY--RGALLVVSH 512
Cdd:PRK11174 527 ALNAAsrRQTTLMVTH 542
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
354-512 |
1.52e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.30 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 354 GPLreiDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTVGAAYLDQR---LSLLDHGRGV------LEQLL 424
Cdd:PRK13543 28 GPL---DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsrfMAYLGHLPGLkadlstLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 425 EVNRSRGESWLRT---RLAQLGLP--AERLAQpcaTLSGGERLKAALALVLYAdrPAQLLLLDEPDNHLDLVARQALETM 499
Cdd:PRK13543 105 FLCGLHGRRAKQMpgsALAIVGLAgyEDTLVR---QLSAGQKKRLALARLWLS--PAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*.
gi 2316862561 500 LRQY---RGALLVVSH 512
Cdd:PRK13543 180 ISAHlrgGGAALVTTH 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-68 |
1.55e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.32 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316862561 3 NTSTLTLDGVSFQLPDGSLLFSDLDETFDTRH-TGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR 68
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR 403
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-174 |
1.55e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrHtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGrvrylaqqlEPADYPTVAD-- 86
Cdd:PRK11288 20 LDDISFDCRAGQV------------H-ALMGENGAGKSTLLKILSGNYQPDAGSILIDG---------QEMRFASTTAal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 87 LAGVRPWLEALARIEagSLDAADYECLGE---------RWDIRQRLADALAAEGLgHLRADTPSERLSGGECMRVALLGA 157
Cdd:PRK11288 78 AAGVAIIYQELHLVP--EMTVAENLYLGQlphkggivnRRLLNYEAREQLEHLGV-DIDPDTPLKYLSIGQRQMVEIAKA 154
|
170
....*....|....*..
gi 2316862561 158 FLDDADFLILDEPSNPL 174
Cdd:PRK11288 155 LARNARVIAFDEPTSSL 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
370-484 |
1.65e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.24 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTV-GAAY-----LD----------QRLSLLDHgRGVLEQLL---EVNRSR 430
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGE--ILLdGEPVrfrspRDaqaagiaiihQELNLVPN-LSVAENIFlgrEPRRGG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 431 GESWLRTR------LAQLGLPaERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEP 484
Cdd:COG1129 111 LIDWRAMRrrarelLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRD--ARVLILDEP 167
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-175 |
1.68e-04 |
|
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: 44.29 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGhLQPSSGSVRRQGR--VRYLAQQLEPA------- 79
Cdd:COG4172 302 VDGVSLTLRRG--------ETL-----GLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdlDGLSRRALRPLrrrmqvv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 80 --DyP--------TVADLAGvrpwlEALaRIEAGSLDAAdyeclgERwdiRQRLADALAAEGL-GHLRADTPSErLSGGE 148
Cdd:COG4172 368 fqD-PfgslsprmTVGQIIA-----EGL-RVHGPGLSAA------ER---RARVAEALEEVGLdPAARHRYPHE-FSGGQ 430
|
170 180
....*....|....*....|....*..
gi 2316862561 149 CMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
37-204 |
1.69e-04 |
|
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: 42.90 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLARLLAGH--LQPSSGSVRRQG----------RVR---YLAQQlEPADYPTVadlagvrpwlealarie 101
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGeditdlppeeRARlgiFLAFQ-YPPEIPGV----------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 102 agsldaadyeclgerwdirqRLADALAAEGLGhlradtpserLSGGECMRVALLGAFLDDADFLILDEPSNPLDGPARAL 181
Cdd:cd03217 93 --------------------KNADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180
....*....|....*....|....*.
gi 2316862561 182 LRARLAAW---DGGLLLVSHDRELLE 204
Cdd:cd03217 143 VAEVINKLreeGKSVLIITHYQRLLD 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-175 |
1.94e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 6 TLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQQlepadyptva 85
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLL-------------AVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQT---------- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 86 dlagvrPWlealarIEAGSLdaADYECLGERWDiRQRLADALAAEGLGHLRADTPSE----------RLSGGECMRVALL 155
Cdd:TIGR01271 496 ------SW------IMPGTI--KDNIIFGLSYD-EYRYTSVIKACQLEEDIALFPEKdktvlgeggiTLSGGQRARISLA 560
|
170 180
....*....|....*....|
gi 2316862561 156 GAFLDDADFLILDEPSNPLD 175
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLD 580
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-170 |
1.97e-04 |
|
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: 43.50 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETFdtrhtGLVGRNGVGKSLLARLLAGHLQP---SSGSVRRQGRvrylaqqlepadyptva 85
Cdd:COG0444 21 VDGVSFDVRRG--------ETL-----GLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGE----------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 86 DLAGVRPwlEALARIEA-----------GSLD-----------AADYECLGERWDIRQRLADALAAEGLghlraDTPSER 143
Cdd:COG0444 71 DLLKLSE--KELRKIRGreiqmifqdpmTSLNpvmtvgdqiaePLRIHGGLSKAEARERAIELLERVGL-----PDPERR 143
|
170 180 190
....*....|....*....|....*....|....
gi 2316862561 144 -------LSGGECMRVALLGAFLDDADFLILDEP 170
Cdd:COG0444 144 ldrypheLSGGMRQRVMIARALALEPKLLIADEP 177
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
9-175 |
2.01e-04 |
|
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: 43.31 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLAQ--QLEPAdypTVAD 86
Cdd:cd03291 53 LKNINLKIEKGEML-------------AITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQfsWIMPG---TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 87 --LAGVrpwlealarieagSLDAADYECLGERWDIRQRLA------DALAAEGlghlradtpSERLSGGECMRVALLGAF 158
Cdd:cd03291 117 niIFGV-------------SYDEYRYKSVVKACQLEEDITkfpekdNTVLGEG---------GITLSGGQRARISLARAV 174
|
170
....*....|....*..
gi 2316862561 159 LDDADFLILDEPSNPLD 175
Cdd:cd03291 175 YKDADLYLLDSPFGYLD 191
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
370-513 |
2.17e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLR----LLAGQRA-----------PLAGTCAVTV-----GAAYLDQR-----LSLLDHG----RGVL 420
Cdd:COG0419 27 LIVGPNGAGKSTILEairyALYGKARsrsklrsdlinVGSEEASVELefehgGKRYRIERrqgefAEFLEAKpserKEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 421 EQLLEVNRSRG--------ESWLRTRLAQL----GLPAERLAQ-----PCATLSGGERLKAALALVLYadrpaqlLLLDe 483
Cdd:COG0419 107 KRLLGLEIYEElkerlkelEEALESALEELaelqKLKQEILAQlsgldPIETLSGGERLRLALADLLS-------LILD- 178
|
170 180 190
....*....|....*....|....*....|
gi 2316862561 484 pDNHLDLVARQALETMLRQyrgaLLVVSHD 513
Cdd:COG0419 179 -FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
356-512 |
2.35e-04 |
|
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: 42.99 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGtcAVTV-GAAYLDQRLSLLDHGRGVLEQ------------ 422
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSG--RILIdGHDVRDYTLASLRRQIGLVSQdvflfndtvaen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 ----LLEVNRSRGESWLRTRLAQ---LGLPA---ERLAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVA 492
Cdd:cd03251 96 iaygRPGATREEVEEAARAANAHefiMELPEgydTVIGERGVKLSGGQRQRIAIARALLKD--PPILILDEATSALDTES 173
|
170 180
....*....|....*....|....
gi 2316862561 493 ----RQALETmLRQYRGAlLVVSH 512
Cdd:cd03251 174 erlvQAALER-LMKNRTT-FVIAH 195
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-175 |
2.56e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.08 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 25 DLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVryLAQQLEPADYPTVADLAG-VRPWLEALARIEA 102
Cdd:PRK13634 25 DVNVSIPSgSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--ITAGKKNKKLKPLRKKVGiVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 103 GSLDAadyeCLG------ERWDIRQRLADALAAEGLGH-LRADTPSErLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13634 103 VEKDI----CFGpmnfgvSEEDAKQKAREMIELVGLPEeLLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
7-170 |
2.64e-04 |
|
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: 43.17 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDgVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRV--------------R-- 70
Cdd:COG4148 14 FTLD-VDFTLPGRGV-------------TALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrRri 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 71 -YLAQqlEPADYP--TVAD--LAGVRPWLEALARIeagsldaadyeclgerwdirqRLADALAAEGLGHLRADTPsERLS 145
Cdd:COG4148 80 gYVFQ--EARLFPhlSVRGnlLYGRKRAPRAERRI---------------------SFDEVVELLGIGHLLDRRP-ATLS 135
|
170 180
....*....|....*....|....*
gi 2316862561 146 GGECMRVALLGAFLDDADFLILDEP 170
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
31-175 |
2.71e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.05 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 31 DTRHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG-------------RVRYLAQQLEPADYPTVADLA--GVRPwle 95
Cdd:PRK10253 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQNATTPGDITVQELVarGRYP--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 96 alarieagsldaadYECLGERW--DIRQRLADALAAEGLGHLrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNP 173
Cdd:PRK10253 109 --------------HQPLFTRWrkEDEEAVTKAMQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
..
gi 2316862561 174 LD 175
Cdd:PRK10253 174 LD 175
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-63 |
2.83e-04 |
|
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: 41.59 E-value: 2.83e-04
10 20 30
....*....|....*....|....*....|.
gi 2316862561 33 RHTGLVGRNGVGKSLLARLLAGHLQPSSGSV 63
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
39-212 |
2.94e-04 |
|
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: 42.63 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 39 GRNGVGKSLLArllaghlqpsSGSVRRQGRVRYL-------AQQLEPADYPTVADLAGVRPwleALA----------RIE 101
Cdd:cd03270 28 GVSGSGKSSLA----------FDTIYAEGQRRYVeslsayaRQFLGQMDKPDVDSIEGLSP---AIAidqkttsrnpRST 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 102 AGSL-DAADYEC-LGERWDIRQRLaDALAAEGLGHLRADTPSERLSGGECMRVAL---LGAFLDDADFlILDEPS---NP 173
Cdd:cd03270 95 VGTVtEIYDYLRlLFARVGIRERL-GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLatqIGSGLTGVLY-VLDEPSiglHP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316862561 174 LDGPARALLRARLAAWDGGLLLVSHDRELLEGMQRIVEL 212
Cdd:cd03270 173 RDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
356-386 |
3.08e-04 |
|
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: 42.60 E-value: 3.08e-04
10 20 30
....*....|....*....|....*....|.
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLL 386
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLL 47
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-175 |
4.10e-04 |
|
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: 42.22 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-VRYLAQQ-------LEPAD 80
Cdd:cd03251 18 LRDISLDIPAG--------ET-----VALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdVRDYTLAslrrqigLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 ----YPTVADlagvrpwlealaRIEAGSLDAADYEclgerwdIRQRLADALAAEGLGHLRA--DTP-SER---LSGGECM 150
Cdd:cd03251 85 vflfNDTVAE------------NIAYGRPGATREE-------VEEAARAANAHEFIMELPEgyDTViGERgvkLSGGQRQ 145
|
170 180
....*....|....*....|....*
gi 2316862561 151 RVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALD 170
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
392-514 |
4.12e-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: 43.46 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 392 PLAGTCAVTVGAAY-LDQRLSLLDHGRGVLEQLLEVNRSRgeswlRTRLAQLGLPAERLAQPCATLSGGERLKAALALVL 470
Cdd:TIGR00630 429 SIADVSELSIREAHeFFNQLTLTPEEKKIAEEVLKEIRER-----LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQI 503
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 471 YADRPAQLLLLDEP-------DNHldlvarQALETM--LRQYRGALLVVSHDP 514
Cdd:TIGR00630 504 GSGLTGVLYVLDEPsiglhqrDNR------RLINTLkrLRDLGNTLIVVEHDE 550
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
142-213 |
4.30e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 142 ERLSGGECM------RVALLGAFLDDADFLILDEPSNPLDGPARALL-----RARLAAWDGGLLLVSHDRELLEGMQRIV 210
Cdd:cd03240 114 GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESlaeiiEERKSQKNFQLIVITHDEELVDAADHIY 193
|
...
gi 2316862561 211 ELS 213
Cdd:cd03240 194 RVE 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
37-175 |
4.69e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.31 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLARLLAG----------HLQPSSGSVRRQGRVR-----------YLAQQLEPADYPTVadlagvrpwle 95
Cdd:PRK09984 35 LLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNLVNRLSV----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 96 aLARIEAGSLDAADYECLGERWDIR---QRLADALAAEGLGHLrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSN 172
Cdd:PRK09984 104 -LENVLIGALGSTPFWRTCFSWFTReqkQRALQALTRVGMVHF-AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
...
gi 2316862561 173 PLD 175
Cdd:PRK09984 182 SLD 184
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
356-513 |
4.98e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.03 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV---------------TVGAAYL---DQRLSLL---D 414
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmgrevnaenekwvrsKVGLVFQdpdDQVFSSTvwdD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 415 HGRGVLEQLL---EVNRSRGESwlrtrLAQLGLPAERlAQPCATLSGGERLKAALALVLyADRPaQLLLLDEPDNHLDLV 491
Cdd:PRK13647 101 VAFGPVNMGLdkdEVERRVEEA-----LKAVRMWDFR-DKPPYHLSYGQKKRVAIAGVL-AMDP-DVIVLDEPMAYLDPR 172
|
170 180
....*....|....*....|....*
gi 2316862561 492 ARQALETMLRQYRGA---LLVVSHD 513
Cdd:PRK13647 173 GQETLMEILDRLHNQgktVIVATHD 197
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-514 |
5.12e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLR-----LLAGQRAPLAGTCAVTVGAAYLDQ---------------------R 409
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDvdpievrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 410 LSLLDH-GRGVleQLLEVNRSRGE-----SWLRTRLAQLGLPAERLAQPCATLSGGERLKAALALVLyADRPaQLLLLDE 483
Cdd:PRK14267 100 LTIYDNvAIGV--KLNGLVKSKKEldervEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL-AMKP-KILLMDE 175
|
170 180 190
....*....|....*....|....*....|...
gi 2316862561 484 PDNHLDLVARQALETMLRQYRG--ALLVVSHDP 514
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKeyTIVLVTHSP 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-176 |
5.43e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.78 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSLLFsdldetfdtrhtgLVGRNGVGKSLLARLLAGHLQPSSGSV---------RRQGRVRYLAQQ---- 75
Cdd:PRK10908 18 LQGVTFHMRPGEMAF-------------LTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrLKNREVPFLRRQigmi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 76 -------LEPADYPTVAdlagvRPWLEALARIEagsldaadyeclgerwDIRQRLADALAAEGLGHLRADTPSErLSGGE 148
Cdd:PRK10908 85 fqdhhllMDRTVYDNVA-----IPLIIAGASGD----------------DIRRRVSAALDKVGLLDKAKNFPIQ-LSGGE 142
|
170 180
....*....|....*....|....*...
gi 2316862561 149 CMRVALLGAFLDDADFLILDEPSNPLDG 176
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
371-512 |
5.95e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRaPLAGTCAVTV----------------------GAAYLDQRLS----------LLDhGRG 418
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITGDH-PQGYSNDLTLfgrrrgsgetiwdikkhigyvsSSLHLDYRVStsvrnvilsgFFD-SIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 419 VLEQLLEVNRSRGESWLrtrlAQLGLPAERLAQPCATLS-GGERLK-AALALVLYadrPAqLLLLDEPDNHLDLVARQA- 495
Cdd:PRK10938 369 IYQAVSDRQQKLAQQWL----DILGIDKRTADAPFHSLSwGQQRLAlIVRALVKH---PT-LLILDEPLQGLDPLNRQLv 440
|
170 180
....*....|....*....|
gi 2316862561 496 ---LETMLRQYRGALLVVSH 512
Cdd:PRK10938 441 rrfVDVLISEGETQLLFVSH 460
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
371-521 |
6.26e-04 |
|
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: 41.86 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRAPLAGTCAV------TVGAAYLD-----------QRLSLLDHgRGVLEQL---LEV-NRS 429
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIdgqdiaAMSRKELRelrrkkismvfQSFALLPH-RTVLENVafgLEVqGVP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 RGESWLRTR--LAQLGLPAERLAQPcATLSGGERLKAALALVLYADRPaqLLLLDEPDNHLD-LVARQALETMLR---QY 503
Cdd:cd03294 134 RAEREERAAeaLELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPD--ILLMDEAFSALDpLIRREMQDELLRlqaEL 210
|
170
....*....|....*...
gi 2316862561 504 RGALLVVSHDPWFLRRLG 521
Cdd:cd03294 211 QKTIVFITHDLDEALRLG 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
356-501 |
6.61e-04 |
|
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: 41.44 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVTvGAAYLDQRLSLLDHGRGVLEQ------------- 422
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-GIDIRDISRKSLRSMIGVVLQdtflfsgtimeni 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 423 LLEVNRSRGESWLR-TRLAQLGLPAERLAQPCAT--------LSGGERLKAALALVLYADrpAQLLLLDEPDNHLDLVAR 493
Cdd:cd03254 98 RLGRPNATDEEVIEaAKEAGAHDFIMKLPNGYDTvlgenggnLSQGERQLLAIARAMLRD--PKILILDEATSNIDTETE 175
|
....*...
gi 2316862561 494 QALETMLR 501
Cdd:cd03254 176 KLIQEALE 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
356-401 |
6.81e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 6.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTcaVTV 401
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGR--VEV 60
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
144-175 |
7.53e-04 |
|
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: 40.63 E-value: 7.53e-04
10 20 30
....*....|....*....|....*....|..
gi 2316862561 144 LSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-175 |
7.90e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 42.12 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 7 LTLDGVSFQLPDGSL-LFSDLDETFDT-RHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepadyptv 84
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAgEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ---------------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 85 aDLAGvrpWLEALAR-----------IEAGSL---------DAADyeclgerwdirQRLADALAAEGLGHLRADTPS--- 141
Cdd:PRK11160 403 -PIAD---YSEAALRqaisvvsqrvhLFSATLrdnlllaapNASD-----------EALIEVLQQVGLEKLLEDDKGlna 467
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316862561 142 ------ERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK11160 468 wlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
37-175 |
8.49e-04 |
|
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: 41.48 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 37 LVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR-VRYLA----QQLEPADYPTVADLAGVRPWLEALARIEAGsLDAADyE 111
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdIAAMSrkelRELRRKKISMVFQSFALLPHRTVLENVAFG-LEVQG-V 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 112 CLGERwdiRQRLADALAAEGLGHLRADTPSErLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03294 133 PRAER---EERAAEALELVGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-175 |
1.14e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.83 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGsllfsdldETfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGR----------------VRYL 72
Cdd:PRK10419 28 LNNVSLSLKSG--------ET-----VALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafrrdIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 73 AQQLEPADYPTVADLAGVRPWLEALArieagSLDAADYEclgerwdirQRLADALAAEGLGHLRADTPSERLSGGECMRV 152
Cdd:PRK10419 95 FQDSISAVNPRKTVREIIREPLRHLL-----SLDKAERL---------ARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180
....*....|....*....|...
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-64 |
1.17e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316862561 7 LTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVR 64
Cdd:PRK11819 338 LLIDDLSFSLPPGGIV-------------GIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-175 |
1.26e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 40.84 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 9 LDGVSFQLPDGSllfsdldetFDTrhtgLVGRNGVGKSLLARLLAGHLQPSSGSVRRQG----------RVRYLAQ--Ql 76
Cdd:COG1101 22 LDGLNLTIEEGD---------FVT----VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykRAKYIGRvfQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 77 EPadyptvadLAGVRPWLE-------ALARIEAGSLdaadyeclgeRWDI----RQRLADALAAEGLGhL--RADTPSER 143
Cdd:COG1101 88 DP--------MMGTAPSMTieenlalAYRRGKRRGL----------RRGLtkkrRELFRELLATLGLG-LenRLDTKVGL 148
|
170 180 190
....*....|....*....|....*....|..
gi 2316862561 144 LSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
356-489 |
1.30e-03 |
|
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: 40.55 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV------TVGAAYLDQRLSLldhgrgVLEQLLEVNRS 429
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdghdlaLADPAWLRRQVGV------VLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 430 RGESwlrTRLAQLGLPAER------------------------LAQPCATLSGGERLKAALALVLYADrpAQLLLLDEPD 485
Cdd:cd03252 92 IRDN---IALADPGMSMERvieaaklagahdfiselpegydtiVGEQGAGLSGGQRQRIAIARALIHN--PRILIFDEAT 166
|
....
gi 2316862561 486 NHLD 489
Cdd:cd03252 167 SALD 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
359-513 |
1.47e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 359 IDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAV---TVGAAYLDQRLSLLD------HgrgVLEQLL----- 424
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgkPVTAEQPEDYRKLFSavftdfH---LFDQLLgpegk 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 425 EVNRSRGESWLRTRLAQ--LGLPAERLAQPcaTLSGGERLKAALALVLYADRPaqLLLLDE----PDNHLDLVARQALET 498
Cdd:PRK10522 419 PANPALVEKWLERLKMAhkLELEDGRISNL--KLSKGQKKRLALLLALAEERD--ILLLDEwaadQDPHFRREFYQVLLP 494
|
170
....*....|....*
gi 2316862561 499 MLRQYRGALLVVSHD 513
Cdd:PRK10522 495 LLQEMGKTIFAISHD 509
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
356-504 |
1.57e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 40.25 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQraPLAGTCAVTVG---------AAYLDQRLSLLDHGRGVLEQL-LE 425
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD--PRATSGRIVFDgkditdwqtAKIMREAVAIVPEGRRVFSRMtVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 VNRSRG-----ESWLRTRLAQLG--LP--AERLAQPCATLSGGERLKAALALVLYAdRPaQLLLLDEPDNHLDLVARQAL 496
Cdd:PRK11614 99 ENLAMGgffaeRDQFQERIKWVYelFPrlHERRIQRAGTMSGGEQQMLAIGRALMS-QP-RLLLLDEPSLGLAPIIIQQI 176
|
....*...
gi 2316862561 497 ETMLRQYR 504
Cdd:PRK11614 177 FDTIEQLR 184
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
456-512 |
1.67e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (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: 213240 [Multi-domain] Cd Length: 251 Bit Score: 40.36 E-value: 1.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 456 LSGGERLKAALALVL----YadRPAQLLLLDEPDNHLDLVARQALETMLRQ-YRGA-LLVVSH 512
Cdd:cd03273 167 LSGGQRSLVALSLILalllF--KPAPMYILDEVDAALDLSHTQNIGRMIKThFKGSqFIVVSL 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
353-513 |
1.89e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 40.26 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 353 RGPLREIDLLLSGPRRLALVGPNGSGKSTLLRLLAGQRAPLAGTCAVT--------------VGAAYLDQ------RLSL 412
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllplhararRGIGYLPQeasifrRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 413 LDHGRGVLEQLLEVNRSRGESWLRTRLAQLGLPAER--LAQpcaTLSGGERLKAALALVLYADrpAQLLLLDEPDNHLDL 490
Cdd:PRK10895 96 YDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRdsMGQ---SLSGGERRRVEIARALAAN--PKFILLDEPFAGVDP 170
|
170 180
....*....|....*....|....*.
gi 2316862561 491 VARQALETM---LRQYRGALLVVSHD 513
Cdd:PRK10895 171 ISVIDIKRIiehLRDSGLGVLITDHN 196
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
144-175 |
1.93e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.45 E-value: 1.93e-03
10 20 30
....*....|....*....|....*....|..
gi 2316862561 144 LSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-78 |
2.30e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.91 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVR---RQGRVRYLAQQLEP 78
Cdd:PRK11701 22 CRDVSFDLYPGEVL-------------GIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRDLYALSEA 81
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-175 |
2.54e-03 |
|
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: 39.52 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 8 TLDGVSFQLPDGSllfsdldetfdtrHTGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRvrylaqqlepaDYPTVaDL 87
Cdd:cd03254 18 VLKDINFSIKPGE-------------TVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI-----------DIRDI-SR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 88 AGVR---------PWLEA---LARIEAGSLDAADYEClgerwdirQRLADALAAEGLGHLRAD----TPSER---LSGGE 148
Cdd:cd03254 73 KSLRsmigvvlqdTFLFSgtiMENIRLGRPNATDEEV--------IEAAKEAGAHDFIMKLPNgydtVLGENggnLSQGE 144
|
170 180
....*....|....*....|....*..
gi 2316862561 149 CMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNID 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-520 |
2.60e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 369 LALVGPNGSGKS----TLLRLLAGQRAPLAGTCAVTVGAAYLDQRLSLLDHGRG-------------------VLEQLLE 425
Cdd:PRK15134 38 LALVGESGSGKSvtalSILRLLPSPPVVYPSGDIRFHGESLLHASEQTLRGVRGnkiamifqepmvslnplhtLEKQLYE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 426 V---------NRSRGEswLRTRLAQLGL--PAERLAQPCATLSGGERLKAALALVLYAdRPaQLLLLDEPDNHLDLVARQ 494
Cdd:PRK15134 118 VlslhrgmrrEAARGE--ILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVMIAMALLT-RP-ELLIADEPTTALDVSVQA 193
|
170 180 190
....*....|....*....|....*....|
gi 2316862561 495 ALETMLRQYRG----ALLVVSHDPWFLRRL 520
Cdd:PRK15134 194 QILQLLRELQQelnmGLLFITHNLSIVRKL 223
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
435-514 |
2.64e-03 |
|
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: 39.55 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 435 LRTRLAQL---GLPAERLAQPCATLSGGERLKAALALVLYADRPAQLLLLDEP-------DNHldlvarQALETM--LRQ 502
Cdd:cd03270 114 IRERLGFLvdvGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPsiglhprDND------RLIETLkrLRD 187
|
90
....*....|..
gi 2316862561 503 YRGALLVVSHDP 514
Cdd:cd03270 188 LGNTVLVVEHDE 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-175 |
2.85e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.73 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 2 TNTSTLTLDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPS-SGSVRRQGRVRYLAQQlepad 80
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLV-------------AIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQV----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 81 yptvadlagvrPWLEAlARIEAGSLDAADYEclGERWdirQRLADALAAEG-----LGHLRADTpSER---LSGGECMRV 152
Cdd:PLN03232 688 -----------SWIFN-ATVRENILFGSDFE--SERY---WRAIDVTALQHdldllPGRDLTEI-GERgvnISGGQKQRV 749
|
170 180
....*....|....*....|...
gi 2316862561 153 ALLGAFLDDADFLILDEPSNPLD 175
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALD 772
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-64 |
2.94e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 40.06 E-value: 2.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 9 LDGVSFQLPDGSLlfsdldetfdtrhTGLVGRNGVGKSLLARLLAGHLQPSSGSVR 64
Cdd:COG1135 21 LDDVSLTIEKGEI-------------FGIIGYSGAGKSTLIRCINLLERPTSGSVL 63
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-175 |
3.45e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 38 VGRNGVGKSLLARLLAGHLQPSSG----SVRRQGRVRYLAQQ--------------LEPADYPTVADLAGVrpwlealar 99
Cdd:PRK10938 35 VGANGSGKSALARALAGELPLLSGerqsQFSHITRLSFEQLQklvsdewqrnntdmLSPGEDDTGRTTAEI--------- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316862561 100 IEAGSLDAAdyEClgerwdirQRLADALaaeGLGHLrADTPSERLSGGECMRVALLGAFLDDADFLILDEPSNPLD 175
Cdd:PRK10938 106 IQDEVKDPA--RC--------EQLAQQF---GITAL-LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
356-386 |
3.52e-03 |
|
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: 40.19 E-value: 3.52e-03
10 20 30
....*....|....*....|....*....|.
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLLRLL 386
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
456-513 |
3.56e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 456 LSGGER----LKAALALVLYADRPAQLLLLDEPDNHLDLVARQAL-ETMLRQYR--GALLVVSHD 513
Cdd:PRK03918 789 LSGGERialgLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvDIMERYLRkiPQVIIVSHD 853
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
435-513 |
3.57e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 435 LRTRLA---QLGLPAERLAQPCATLSGGERLKAALALVLYADRPAQLLLLDEP-------DNH--LDLVARqaletmLRQ 502
Cdd:PRK00635 453 LKSRLSiliDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPsiglhpqDTHklINVIKK------LRD 526
|
90
....*....|.
gi 2316862561 503 YRGALLVVSHD 513
Cdd:PRK00635 527 QGNTVLLVEHD 537
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
370-512 |
3.98e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.25 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLR-------LLAGQRaplagtcavTVGAAYLD----------------------QR-----LSLLD- 414
Cdd:COG1117 41 ALIGPSGCGKSTLLRclnrmndLIPGAR---------VEGEILLDgediydpdvdvvelrrrvgmvfQKpnpfpKSIYDn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 415 -------HG---RGVLEQLLEvnRSrgeswLRtrlaQLGLPAE---RLAQPCATLSGGE--RLKAALALvlyADRPaQLL 479
Cdd:COG1117 112 vayglrlHGiksKSELDEIVE--ES-----LR----KAALWDEvkdRLKKSALGLSGGQqqRLCIARAL---AVEP-EVL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 2316862561 480 LLDEPDNHLDLVARQALETMLRQYRG--ALLVVSH 512
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILELKKdyTIVIVTH 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
314-501 |
4.32e-03 |
|
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: 39.93 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 314 REAAREVEEASPllldspdAELAAQRRIVELKGAVL---PHLRGPLREIDLLLSGPRRLALVGPNGSGKST----LLRLL 386
Cdd:TIGR00957 1264 KEAPWQIQETAP-------PSGWPPRGRVEFRNYCLryrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRIN 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 387 AGQRAPLA--GTCAVTVGAAYLDQRLSLLDHGRGVLEQLLEVN------RSRGESWLRTRLAQL-----GLPAeRLAQPC 453
Cdd:TIGR00957 1337 ESAEGEIIidGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNldpfsqYSDEEVWWALELAHLktfvsALPD-KLDHEC 1415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 454 A----TLSGGERLKAALALVLYadRPAQLLLLDEPDNHLDLVARQALETMLR 501
Cdd:TIGR00957 1416 AeggeNLSVGQRQLVCLARALL--RKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-73 |
4.67e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 4.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316862561 9 LDGVSFQLPDGSLLfsdldetfdtrhtGLVGRNGVGKSLLARLLAGHLQPSSGSVRRQGRVRYLA 73
Cdd:PRK13545 40 LNNISFEVPEGEIV-------------GIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA 91
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
449-512 |
4.99e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 4.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316862561 449 LAQPCATLSGGERLKAALALVL----YADRPAQLLLLDEPDNHLDLVARQAL----ETMLRQYRG--ALLVVSH 512
Cdd:PRK01156 795 MVEGIDSLSGGEKTAVAFALRVavaqFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSDipQVIMISH 868
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
370-499 |
5.77e-03 |
|
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: 37.99 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 370 ALVGPNGSGKSTLLRLLAGQRaplagTCAVTVGAAYLDQRLSLLDHGR--GVLEQL------LEVNRS-RGESWLRtrla 440
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAGRK-----TAGVITGEILINGRPLDKNFQRstGYVEQQdvhspnLTVREAlRFSALLR---- 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316862561 441 qlGLPAErlaqpcatlsggERLKAALALVLYAdRPaQLLLLDEPDNHLDlvARQALETM 499
Cdd:cd03232 108 --GLSVE------------QRKRLTIGVELAA-KP-SILFLDEPTSGLD--SQAAYNIV 148
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
369-395 |
5.77e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 38.62 E-value: 5.77e-03
10 20
....*....|....*....|....*..
gi 2316862561 369 LALVGPNGSGKSTLLRLLAGQRAPLAG 395
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSG 68
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
456-502 |
6.15e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (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: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 6.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2316862561 456 LSGGERLKAALALVLYADR--PAQLLLLDEPDNHLDLVARQALETMLRQ 502
Cdd:cd03272 159 LSGGQKSLVALALIFAIQKcdPAPFYLFDEIDAALDAQYRTAVANMIKE 207
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
356-484 |
6.30e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 356 LREIDLLLSGPRRLALVGPNGSGKSTLL---------RLLAGQRAPlAGTCAVTVGAAYLDqRLSLLD------------ 414
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQ-PGNHDRIEGLEHID-KVIVIDqspigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 415 ------------------HGRGVLEQLLEVnRSRGES------------------------WLRTrLAQLGLPAERLAQP 452
Cdd:cd03271 89 atytgvfdeirelfcevcKGKRYNRETLEV-RYKGKSiadvldmtveealeffenipkiarKLQT-LCDVGLGYIKLGQP 166
|
170 180 190
....*....|....*....|....*....|....
gi 2316862561 453 CATLSGGE--RLKAALALvLYADRPAQLLLLDEP 484
Cdd:cd03271 167 ATTLSGGEaqRIKLAKEL-SKRSTGKTLYILDEP 199
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-63 |
6.48e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 38.82 E-value: 6.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316862561 2 TNTSTLTLDGVSFQLPDGsllfsdldetfdtRHTGLVGRNGVGKSLLARLLAGHLQPSSGSV 63
Cdd:PRK13632 18 PNSENNALKNVSFEINEG-------------EYVAILGHNGSGKSTISKILTGLLKPQSGEI 66
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
33-175 |
7.29e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.65 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 33 RHTGLVGRNGVGKSLLARLLAGHLQPS--SGSVRRQGRVRYLAQQLEPADYPTVADLAGVRPWlealARIEAGSLDAADY 110
Cdd:PRK13547 28 RVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQ----AAQPAFAFSAREI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316862561 111 ECLGERWDIRQRLADA-----LAAEGLGHLRADTPSER----LSGGECMRVALLGAF---------LDDADFLILDEPSN 172
Cdd:PRK13547 104 VLLGRYPHARRAGALThrdgeIAWQALALAGATALVGRdvttLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTA 183
|
...
gi 2316862561 173 PLD 175
Cdd:PRK13547 184 ALD 186
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
370-391 |
7.30e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.47 E-value: 7.30e-03
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
371-396 |
7.99e-03 |
|
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: 39.01 E-value: 7.99e-03
10 20
....*....|....*....|....*.
gi 2316862561 371 LVGPNGSGKSTLLRLLAGQRAPLAGT 396
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGE 388
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
343-387 |
8.46e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 37.61 E-value: 8.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316862561 343 ELKGAVLPHLRGPLRE-----IDLLLSGPRRLALVGPNGSGKSTLLRLLA 387
Cdd:cd03243 1 EIKGGRHPVLLALTKGetfvpNDINLGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| |
