|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
77-655 |
5.16e-175 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 531.28 E-value: 5.16e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 77 SLLQLFRFATTFdYILLLIGLITSVISGVSQPVLAIISGRMTNVLLVIDPLSKEFKTktmenVYIFLGLGIFVSINDFCQ 156
Cdd:COG1132 8 LLRRLLRYLRPY-RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLL-----LLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 157 YMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEW 236
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 237 RLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGG 316
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 317 FWSGFFGGIFFFWLMAFMGCGILYGGYLLKVGIIkSPGDV--FIIVVAMLLGAyfLGLISPHLMVLLNARVAAASIYKTI 394
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL-TVGDLvaFILYLLRLFGP--LRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 395 DRVPKIdPYSRHGKKIEKVVGKVTFENVHFRYPtrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQG 474
Cdd:COG1132 319 DEPPEI-PDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 475 SVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGV 554
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEA 634
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570 580
....*....|....*....|.
gi 1678196980 635 GNHEELVNLGGRYFDLVKAQA 655
Cdd:COG1132 556 GTHEELLARGGLYARLYRLQF 576
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
92-1317 |
2.93e-146 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 481.45 E-value: 2.93e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 92 LLLIGLITSVISGVSQP----VLAIISGRMtNVLLVIDPLskefktktmenVYIFLGLGIFVSINDFCQYMCFQRVCSRM 167
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPffvsVFGVIMKNM-NLGENVNDI-----------IFSLVLIGIFQFILSFISSFCMDVVTTKI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 168 MTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIP 247
Cdd:PTZ00265 129 LKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 248 VSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIFF 327
Cdd:PTZ00265 209 LIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMIN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 328 FWLMAFMGCGILYGGYLlkvgIIKSP-----------GDVFIIVVAMLLGAYFLGLISPHLMVLLNARVAAASIYKTIDR 396
Cdd:PTZ00265 289 GFILASYAFGFWYGTRI----IISDLsnqqpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 397 VPKIDPySRHGKKIeKVVGKVTFENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSV 476
Cdd:PTZ00265 365 KPLVEN-NDDGKKL-KDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 477 QI-DGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFG----------------NPDATRET--------------- 524
Cdd:PTZ00265 443 IInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQENknkrnscrakcagdl 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 525 --------------------------MIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLL 578
Cdd:PTZ00265 523 ndmsnttdsneliemrknyqtikdseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILI 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 579 LDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLSTIREADKIVFF---EKG------------------------ 629
Cdd:PTZ00265 603 LDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLsnrERGstvdvdiigedptkdnkennnknn 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 630 --------------------VIVEAGNHEELV-NLGGRYFDLV---------------------KAQAFKQ-----DPDE 662
Cdd:PTZ00265 683 kddnnnnnnnnnnkinnagsYIIEQGTHDALMkNKNGIYYTMInnqkvsskkssnndndkdsdmKSSAYKDsergyDPDE 762
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 663 IALEKEEEDQFDEFDKptvfNRKVSVRNSRSSGRSGSEEFRRgslanhsfDRFRKASHIPSaedeafALRV--KETMEKD 740
Cdd:PTZ00265 763 MNGNSKHENESASNKK----SCKMSDENASENNAGGKLPFLR--------NLFKRKPKAPN------NLRIvyREIFSYK 824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 741 GEITAGFLDIfknaqgnytymliglsaaLIRGLDLPTFALLFA-WVFEGFEFVPY-GGKMMHRLAMSVIAhcaagLGIWF 818
Cdd:PTZ00265 825 KDVTIIALSI------------------LVAGGLYPVFALLYAkYVSTLFDFANLeANSNKYSLYILVIA-----IAMFI 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 819 FQTLSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNPAHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVT 898
Cdd:PTZ00265 882 SETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 899 IGFINCWQVAILGTALIFLLgfiMAGLAFKISIVAAEHME--------------ND-----DAGKIAIEIIENVKTIQLL 959
Cdd:PTZ00265 962 MSFYFCPIVAAVLTGTYFIF---MRVFAIRARLTANKDVEkkeinqpgtvfaynSDdeifkDPSFLIQEAFYNMNTVIIY 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 960 TRTRRFLNSYENESKKRKRTELRKSVYEAVNYCISQNFMYYMSCFCFALAIRIINQGDQTVDKTFRCLMAMMLCCE--GI 1037
Cdd:PTZ00265 1039 GLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSyaGK 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1038 IMSAQFFPQfvGAKSAAGQMFNLINRQP-----QTGDLKSGTKPEIRGNILFENVKFSYPQRPHQPVMKQLQWTALRGQT 1112
Cdd:PTZ00265 1119 LMSLKGDSE--NAKLSFEKYYPLIIRKSnidvrDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKT 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1113 VALVGPSGSGKSTCIGMLERFYDV------------------------------------------------------TG 1138
Cdd:PTZ00265 1197 TAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNS 1276
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1139 GALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERG 1218
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1356
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1219 GQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEAL----DRAreGRTCITIAHRLSSIQNSDLIVYIDD- 1293
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNp 1434
|
1450 1460 1470
....*....|....*....|....*....|..
gi 1678196980 1294 ----GRVQESGTHKELMQLKG----KYFELIK 1317
Cdd:PTZ00265 1435 drtgSFVQAHGTHEELLSVQDgvykKYVKLAK 1466
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
760-1319 |
2.77e-139 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 437.29 E-value: 2.77e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 760 YMLIGLSAALIRGLDLPTFALLFAWVFEGFefvpYGGKMMHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIVSENLGVRFR 839
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDAL----LAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 840 VAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFINCWQVAILGTALIFLLG 919
Cdd:COG1132 98 RDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 920 FIMAGLAFKISIVAAEHME-NDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELRKSVYEAVNYCISQNFM 998
Cdd:COG1132 176 LVLRLFGRRLRKLFRRVQEaLAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 999 YYMSCFCFALAIRIINQGDQTVDKTFRCLMAMMLCCEGIIMSAQFFPQFVGAKSAAGQMFNLINRQPQTGDLKSGTK-PE 1077
Cdd:COG1132 256 NLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPlPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1078 IRGNILFENVKFSYPqrPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLR 1157
Cdd:COG1132 336 VRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1158 TQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVR 1237
Cdd:COG1132 414 RQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLK 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1238 DPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIK 1317
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
..
gi 1678196980 1318 KQ 1319
Cdd:COG1132 574 LQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
74-655 |
1.02e-136 |
|
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: 435.03 E-value: 1.02e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 74 QPVSLLQLFRFATTF--DYILLLIGLITSVISGVSQPVLA------IISGRMTNVLLVIdplskefktktmenVYIFLGL 145
Cdd:COG2274 140 KPFGLRWFLRLLRRYrrLLLQVLLASLLINLLALATPLFTqvvidrVLPNQDLSTLWVL--------------AIGLLLA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 146 GIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNmERIQDGV-GDKLGVLIRGISMV 224
Cdd:COG2274 206 LLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDV-ESIREFLtGSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 225 IASVVIsLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYE-- 302
Cdd:COG2274 285 IFLIVL-FFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWEnl 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 303 --KQLNSGKKHAIWGGFWSGFFGGifffwLMAFMGCGILY-GGYLLKVGIIkSPGDV--FIIVVAMLLGAyFLGLISpHL 377
Cdd:COG2274 364 laKYLNARFKLRRLSNLLSTLSGL-----LQQLATVALLWlGAYLVIDGQL-TLGQLiaFNILSGRFLAP-VAQLIG-LL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 378 MVLLNARVAAASIYKTIDRVPKIDPySRHGKKIEKVVGKVTFENVHFRYPTRkEAKVLNGLNLTVEPGTSVALVGHSGCG 457
Cdd:COG2274 436 QRFQDAKIALERLDDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 458 KSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDF 537
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDF 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 538 IKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTI 617
Cdd:COG2274 594 IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI 673
|
570 580 590
....*....|....*....|....*....|....*...
gi 1678196980 618 READKIVFFEKGVIVEAGNHEELVNLGGRYFDLVKAQA 655
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
417-654 |
6.78e-134 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 409.62 E-value: 6.78e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDLVKAQ 654
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1082-1319 |
6.40e-127 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 391.13 E-value: 6.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1242 LLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
90-651 |
4.86e-119 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 387.54 E-value: 4.86e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 90 YILLLIGLITSVISGVSQPvlaIISGRmtnvllVIDPLSKEFKTKTMENVYIFLGLGIFVS-INDFCQYMCFQRVCSRMM 168
Cdd:TIGR00958 163 LISAFVFLTLSSLGEMFIP---FYTGR------VIDTLGGDKGPPALASAIFFMCLLSIASsVSAGLRGGSFNYTMARIN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 169 TVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPV 248
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 249 STICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNS----GKKHAIWGGFWSGFfgg 324
Cdd:TIGR00958 314 VFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEEtlqlNKRKALAYAGYLWT--- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 325 ifffwlMAFMGCGIL-----YGGYLLKVGIIKSPGDVFIIVVAMLLGAYFLGLIS--PHLMvllNARVAAASIYKTIDRV 397
Cdd:TIGR00958 391 ------TSVLGMLIQvlvlyYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYvySGMM---QAVGASEKVFEYLDRK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 398 PKIDPYSRHgkKIEKVVGKVTFENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQ 477
Cdd:TIGR00958 462 PNIPLTGTL--APLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 478 IDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLS 557
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 558 GGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSAlnNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNH 637
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
570
....*....|....
gi 1678196980 638 EELVNLGGRYFDLV 651
Cdd:TIGR00958 698 KQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
91-658 |
2.67e-111 |
|
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: 362.11 E-value: 2.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIGLITSVISGVSQPVLAIIsgrmtnvllvIDPLSKEFKTKTMENVYIFLGLGI--FVSINDFCQY---MCFQRVCS 165
Cdd:TIGR02203 14 AGLVLAGVAMILVAATESTLAAL----------LKPLLDDGFGGRDRSVLWWVPLVVigLAVLRGICSFvstYLLSWVSN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 166 RMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGL 245
Cdd:TIGR02203 84 KVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 246 IPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGI 325
Cdd:TIGR02203 164 LPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 326 FFFWLMAFMGCGILYGGYLLKVGIIkSPGDVFIIVVAMLLgayflgLISPhLMVLLNAR-------VAAASIYKTIDRVP 398
Cdd:TIGR02203 244 TQLIASLALAVVLFIALFQAQAGSL-TAGDFTAFITAMIA------LIRP-LKSLTNVNapmqrglAAAESLFTLLDSPP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 399 KIDPYSRHgkkIEKVVGKVTFENVHFRYPTRkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQI 478
Cdd:TIGR02203 316 EKDTGTRA---IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 479 DGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNP-DATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLS 557
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 558 GGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNH 637
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTH 551
|
570 580
....*....|....*....|.
gi 1678196980 638 EELVNLGGRYFDLVKAQaFKQ 658
Cdd:TIGR02203 552 NELLARNGLYAQLHNMQ-FRE 571
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
811-1319 |
1.13e-110 |
|
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: 364.93 E-value: 1.13e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 811 AAGLGIWFFQTLSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNpaHAPGSLITRL-AADPpcVKAVVDGRMMQVVYA 889
Cdd:COG2274 204 LALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRFrDVES--IREFLTGSLLTALLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 890 TA-AVIACVTIGFINcWQVAILGTALIFLLGFIMAGLAFKISIVAAEHMEndDAGKIA---IEIIENVKTIQLLTRTRRF 965
Cdd:COG2274 280 LLfVLIFLIVLFFYS-PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESE--ASAKRQsllVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 966 LNSYENESKKRKRTELRKSVYEAVNYCISQNFMYYMSCFCFALAIRIINQGDQTvdktfrclMAMMLCCEGIIMS----- 1040
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLT--------LGQLIAFNILSGRflapv 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1041 ---AQFFPQFVGAKSAAGQMFNLINRQP-QTGDLKSGTKPEIRGNILFENVKFSYPQRPhQPVMKQLQWTALRGQTVALV 1116
Cdd:COG2274 429 aqlIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGDS-PPVLDNISLTIKPGERVAIV 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1117 GPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALEL 1196
Cdd:COG2274 508 GRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1197 ANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIA 1276
Cdd:COG2274 588 AGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1678196980 1277 HRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:COG2274 668 HRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
417-650 |
8.93e-110 |
|
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: 344.98 E-value: 8.93e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAkVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDL 650
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
415-662 |
2.39e-107 |
|
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: 352.20 E-value: 2.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRY-PTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRN 493
Cdd:COG5265 356 GEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRD 573
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 574 PKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDLVKA 653
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWAR 592
|
....*....
gi 1678196980 654 QAFKQDPDE 662
Cdd:COG5265 593 QQEEEEAEE 601
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
417-654 |
4.68e-105 |
|
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: 332.27 E-value: 4.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDLVKAQ 654
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
772-1316 |
1.42e-100 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 337.08 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 772 GLDLPTFALLFAWVF---EGFEFVPY----------GGKMMHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIVSENLGVRF 838
Cdd:TIGR00958 157 GRDWPWLISAFVFLTlssLGEMFIPFytgrvidtlgGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 839 RVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFINCWQVAILGTALIFLL 918
Cdd:TIGR00958 237 REDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 919 GFIMAGLAFKISIVAAEHMEN-DDAGKIAIEIIENVKTIqlltrtRRFLNsyENESKKRKRTELR--KSVY--EAVNYCI 993
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEAvAKANQVAEEALSGMRTV------RSFAA--EEGEASRFKEALEetLQLNkrKALAYAG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 994 sqnFMYYMSCFCFALAIRIINQGDQTV---DKTFRCLMAMMLCCEGIIMSAQ----FFPQFVGAKSAAGQMFNLINRQPQ 1066
Cdd:TIGR00958 387 ---YLWTTSVLGMLIQVLVLYYGGQLVltgKVSSGNLVSFLLYQEQLGEAVRvlsyVYSGMMQAVGASEKVFEYLDRKPN 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1067 ---TGDLKSgtkPEIRGNILFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRM 1143
Cdd:TIGR00958 464 iplTGTLAP---LNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1144 DGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSG 1223
Cdd:TIGR00958 541 DGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1224 GQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEalDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHK 1303
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
570
....*....|...
gi 1678196980 1304 ELMQLKGKYFELI 1316
Cdd:TIGR00958 699 QLMEDQGCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1082-1315 |
1.64e-98 |
|
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: 314.17 E-value: 1.64e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1242 LLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFEL 1315
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
822-1319 |
2.77e-98 |
|
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: 326.29 E-value: 2.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 822 LSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGF 901
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 902 INCWQVAILGTALIFLLGFIMAGLAFKISIVAAEHME-NDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTE 980
Cdd:TIGR02203 151 YYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNsMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 981 LRKSVYEAVNYCISQnfmyymscFCFALAIRII-------NQGDQTVDKTFRCLMAMMLCCEGII-----MSAQFFPQFV 1048
Cdd:TIGR02203 231 MKMTSAGSISSPITQ--------LIASLALAVVlfialfqAQAGSLTAGDFTAFITAMIALIRPLksltnVNAPMQRGLA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1049 GAKSaagqMFNLINrQPQTGDLKSGTKPEIRGNILFENVKFSYPQRpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIG 1128
Cdd:TIGR02203 303 AAES----LFTLLD-SPPEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVN 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1129 MLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLG-LKDVPLEKINQALELANANRFLGNLP 1207
Cdd:TIGR02203 377 LIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLP 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1208 DGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDL 1287
Cdd:TIGR02203 457 LGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADR 536
|
490 500 510
....*....|....*....|....*....|..
gi 1678196980 1288 IVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:TIGR02203 537 IVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
171-645 |
2.05e-97 |
|
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: 323.63 E-value: 2.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 171 MRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRgisMVIASVVISLI---YEWRLALMMLG--- 244
Cdd:COG4988 93 LRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFL---AALVPLLILVAvfpLDWLSGLILLVtap 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 245 LIPVSticMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEK---------------QLNSGk 309
Cdd:COG4988 170 LIPLF---MILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEasedfrkrtmkvlrvAFLSS- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 310 khaiwggfwsgffggiFFFWLMAFMG--CGILYGGY-LLKVGIIKSPGdVFIIVVAM-------LLGAYFlglispHlmV 379
Cdd:COG4988 246 ----------------AVLEFFASLSiaLVAVYIGFrLLGGSLTLFAA-LFVLLLAPefflplrDLGSFY------H--A 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 380 LLNARVAAASIYKTIDRvPKIDPYSRHGKKIEKVVGKVTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKS 459
Cdd:COG4988 301 RANGIAAAEKIFALLDA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKS 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 460 TSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIK 539
Cdd:COG4988 378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 540 KMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIRE 619
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
|
490 500
....*....|....*....|....*.
gi 1678196980 620 ADKIVFFEKGVIVEAGNHEELVNLGG 645
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
415-645 |
5.18e-97 |
|
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: 309.93 E-value: 5.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYptRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV 494
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDP 574
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGG 645
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
140-654 |
5.46e-96 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 320.43 E-value: 5.46e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 140 YIFLGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIR 219
Cdd:PRK11176 69 LVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 220 GISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLS-RFLEKSTGEElEKVGEAGAIAEECLMGVRTIQAFNGQEEMV 298
Cdd:PRK11176 149 EGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSkRFRNISKNMQ-NTMGQVTTSAEQMLKGHKEVLIFGGQEVET 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 299 AKYEKQLNS----GKKHAIWGGFWSGFFGGIFFFWLMAfmgcgILYGGYLLKVGIIKSPGDVFIIVVAMLlgayflGLIS 374
Cdd:PRK11176 228 KRFDKVSNRmrqqGMKMVSASSISDPIIQLIASLALAF-----VLYAASFPSVMDTLTAGTITVVFSSMI------ALMR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 375 PhLMVLLNA-----RVAAASiyKTIDRVPKIDPYSRHGK-KIEKVVGKVTFENVHFRYPTrKEAKVLNGLNLTVEPGTSV 448
Cdd:PRK11176 297 P-LKSLTNVnaqfqRGMAAC--QTLFAILDLEQEKDEGKrVIERAKGDIEFRNVTFTYPG-KEVPALRNINFKIPAGKTV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 449 ALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDA-TRETMIR 527
Cdd:PRK11176 373 ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 528 VCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTT 607
Cdd:PRK11176 453 AARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1678196980 608 IMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDLVKAQ 654
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
391-661 |
1.80e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 316.13 E-value: 1.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 391 YKTIDRVPKI-DPysRHGKKIEKVVGKVTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLY 469
Cdd:PRK13657 310 FEVEDAVPDVrDP--PGAIDLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 470 EPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQI 549
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 550 GDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKG 629
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
250 260 270
....*....|....*....|....*....|..
gi 1678196980 630 VIVEAGNHEELVNLGGRYFDLVKAQAFKQDPD 661
Cdd:PRK13657 546 RVVESGSFDELVARGGRFAALLRAQGMLQEDE 577
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
827-1319 |
1.17e-93 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 313.56 E-value: 1.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 827 FAIVSeNLGVRF----RVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFI 902
Cdd:TIGR02204 79 FYLVT-WLGERVvadiRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 903 NCWQVAILGTALIFLLGFIMAGLAFKISIVAAEHMEN-DDAGKIAIEIIENVKTIQlltrtrrflnSYENESKKRKRTEL 981
Cdd:TIGR02204 156 TSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRiADAGSYAGETLGAIRTVQ----------AFGHEDAERSRFGG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 982 R-KSVYEAVNYCISQN-----FMYYMScFCFALAIRIINQGDQTVDK-TFRCLMAMMLCCEGIIMSAQFFPQFVG----A 1050
Cdd:TIGR02204 226 AvEKAYEAARQRIRTRalltaIVIVLV-FGAIVGVLWVGAHDVIAGKmSAGTLGQFVFYAVMVAGSIGTLSEVWGelqrA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1051 KSAAGQMFNLINRQPqtgDLKSGTKPE-----IRGNILFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKST 1125
Cdd:TIGR02204 305 AGAAERLIELLQAEP---DIKAPAHPKtlpvpLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKST 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1126 CIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGN 1205
Cdd:TIGR02204 382 LFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISA 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1206 LPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNS 1285
Cdd:TIGR02204 462 LPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKA 541
|
490 500 510
....*....|....*....|....*....|....
gi 1678196980 1286 DLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:TIGR02204 542 DRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1082-1319 |
2.60e-93 |
|
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: 299.92 E-value: 2.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPqrPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1242 LLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
166-652 |
2.86e-93 |
|
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: 312.47 E-value: 2.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 166 RMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDgvgdklgVLIRGISMVIASVVISLI-------YEWRL 238
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDN-------LYLRVLLPLLVALLVILAavaflafFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 239 ALMMLGLIPVSTICMTLLSRFLEKSTGEELEKV-GEAGAIAEECLMGVRTIQAFNGQEEMVAKY---EKQLNSGKKHAiw 314
Cdd:COG4987 158 ALVLALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLdaaEARLAAAQRRL-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 315 ggFWSGFFGGIFFFWLMAFMGCGILY-GGYLLKVGIIkspGDVFIIVVAML-LGAY--FLGLisPHLMVLLN-ARVAAAS 389
Cdd:COG4987 236 --ARLSALAQALLQLAAGLAVVAVLWlAAPLVAAGAL---SGPLLALLVLAaLALFeaLAPL--PAAAQHLGrVRAAARR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 390 IYKTIDRVPKIdPYSRHGKKIEKVVGkVTFENVHFRYPTRKEAkVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLY 469
Cdd:COG4987 309 LNELLDAPPAV-TEPAEPAPAPGGPS-LELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 470 EPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQI 549
Cdd:COG4987 386 DPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 550 GDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKG 629
Cdd:COG4987 466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDG 545
|
490 500
....*....|....*....|...
gi 1678196980 630 VIVEAGNHEELVNLGGRYFDLVK 652
Cdd:COG4987 546 RIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1056-1319 |
3.05e-93 |
|
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: 313.30 E-value: 3.05e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1056 QMFNLINRQPQTGDlKSGTKPEI--RGNILFENVKFSYpqRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERF 1133
Cdd:COG5265 331 RMFDLLDQPPEVAD-APDAPPLVvgGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1134 YDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTE 1213
Cdd:COG5265 408 YDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTR 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1214 VGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDD 1293
Cdd:COG5265 488 VGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEA 567
|
250 260
....*....|....*....|....*.
gi 1678196980 1294 GRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:COG5265 568 GRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1050-1310 |
1.27e-92 |
|
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: 310.15 E-value: 1.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1050 AKSAAGQMFNLINRQPQTGDLKSGTKPEIRGN-ILFENVKFSYPQRphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIG 1128
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPsIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1129 MLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPD 1208
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPD 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1209 GIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLI 1288
Cdd:COG4988 462 GLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRI 541
|
250 260
....*....|....*....|..
gi 1678196980 1289 VYIDDGRVQESGTHKELMQLKG 1310
Cdd:COG4988 542 LVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1080-1310 |
4.67e-91 |
|
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: 293.36 E-value: 4.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYpqRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQ 1159
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDP 1239
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1240 KILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKG 1310
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
417-654 |
1.85e-87 |
|
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: 283.99 E-value: 1.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDLVKAQ 654
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
837-1315 |
9.15e-86 |
|
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: 291.28 E-value: 9.15e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 837 RFRVAAFRNLLYQDAAYFdnPAHAPGSLITRLAADppcVKAVVDG--RMMQ--VVYATAAVIACVTIGFINcWQVAILGT 912
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVAD---VDALDNLylRVLLplLVALLVILAAVAFLAFFS-PALALVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 913 ALIFLLGFIMAGLAFKISIVAAEHMENDDAG--KIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELRKSVYEAVN 990
Cdd:COG4987 163 LGLLLAGLLLPLLAARLGRRAGRRLAAARAAlrARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 991 YCISQNFMYYMSCFCFALAIRIINQGDQTVDktfrcLMAMMLCC-----EGIIMSAQFFPQFVGAKSAAGQMFNLINRQP 1065
Cdd:COG4987 243 QALLQLAAGLAVVAVLWLAAPLVAAGALSGP-----LLALLVLAalalfEALAPLPAAAQHLGRVRAAARRLNELLDAPP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1066 QTGDLKSGTKPEIRGNILFENVKFSYPQRPhQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDG 1145
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1146 QDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQ 1225
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1226 KQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|
gi 1678196980 1306 MQLKGKYFEL 1315
Cdd:COG4987 557 LAQNGRYRQL 566
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
93-390 |
2.32e-84 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 277.82 E-value: 2.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQPVLAIISGRMTNVL---LVIDPLSKEFKTKTMENVYIFLGLGIFVSINDFCQYMCFQRVCSRMMT 169
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 170 VMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVS 249
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 250 TICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIFFFW 329
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 330 LMAFMGCGILYGGYLLKVGIIkSPGDVFIIVVAMLLGAYFLGLISPHLMVLLNARVAAASI 390
Cdd:cd18577 241 IFAMYALAFWYGSRLVRDGEI-SPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1078-1296 |
1.54e-83 |
|
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: 272.42 E-value: 1.54e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1078 IRGNILFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGqdiKNISLY--- 1154
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQYehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1155 HLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARA 1234
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1235 LVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRV 1296
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
185-654 |
5.87e-82 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 284.33 E-value: 5.87e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 185 GWFDKNLSGTITTRLNDnMERIQDGV-GDKLGVLIRgismvIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRF---- 259
Cdd:TIGR01846 228 GYFESRRVGDTVARVRE-LEQIRNFLtGSALTVVLD-----LLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFvgpi 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 260 LEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLnSGKKHAiwggfwsgffggifffwlmafmgcgil 339
Cdd:TIGR01846 302 LRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQL-AAYVAA--------------------------- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 340 yGGYLLKVGIIKSPGDVFI--IVVAMLL--GAYFL--GLISPHLMVLLN---ARVAA-----ASIYK-------TIDRVP 398
Cdd:TIGR01846 354 -SFRVTNLGNIAGQAIELIqkLTFAILLwfGAHLVigGALSPGQLVAFNmlaGRVTQpvlrlAQLWQdfqqtgiALERLG 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 399 KI-----DPYSRHGKKIEKVVGKVTFENVHFRYpTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQ 473
Cdd:TIGR01846 433 DIlnsptEPRSAGLAALPELRGAITFENIRFRY-APDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQH 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 474 GSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGG 553
Cdd:TIGR01846 512 GQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKG 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 554 VQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVE 633
Cdd:TIGR01846 592 ANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
490 500
....*....|....*....|.
gi 1678196980 634 AGNHEELVNLGGRYFDLVKAQ 654
Cdd:TIGR01846 672 SGRHEELLALQGLYARLWQQQ 692
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1042-1323 |
1.03e-81 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 280.31 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1042 QFFPQFVGAKSAAGQMFNLINRQPQTGDLKSGTKPE-IRGNILFENVKFSYPQRPhqPVMKQLQWTALRGQTVALVGPSG 1120
Cdd:PRK13657 294 AFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGrVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1121 SGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANAN 1200
Cdd:PRK13657 372 AGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAH 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1201 RFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLS 1280
Cdd:PRK13657 452 DFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLS 531
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1678196980 1281 SIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQDLAI 1323
Cdd:PRK13657 532 TVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQ 574
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
823-1319 |
2.24e-80 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 276.51 E-value: 2.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 823 STVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFI 902
Cdd:PRK11176 85 SSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 903 NCWQVAILgtalIFLLGFImagLAFKISIVAaehmenddagKIAIEIIENVKTI--QLLTRTRRFLN------SYENESK 974
Cdd:PRK11176 163 YSWQLSLI----LIVIAPI---VSIAIRVVS----------KRFRNISKNMQNTmgQVTTSAEQMLKghkevlIFGGQEV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 975 KRKRtelrksvYEAVNYCISQNFMYYMSC-----------FCFALA-----------IRIINQGDQTVdkTFRCLMAMML 1032
Cdd:PRK11176 226 ETKR-------FDKVSNRMRQQGMKMVSAssisdpiiqliASLALAfvlyaasfpsvMDTLTAGTITV--VFSSMIALMR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1033 CCEGII-MSAQFfpqfvGAKSAAGQ-MFNLINRQPQTGDLKSGTKPeIRGNILFENVKFSYPQRPHqPVMKQLQWTALRG 1110
Cdd:PRK11176 297 PLKSLTnVNAQF-----QRGMAACQtLFAILDLEQEKDEGKRVIER-AKGDIEFRNVTFTYPGKEV-PALRNINFKIPAG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1111 QTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDV-PLEK 1189
Cdd:PRK11176 370 KTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1190 INQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREG 1269
Cdd:PRK11176 450 IEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1270 RTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:PRK11176 530 RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
417-629 |
4.42e-80 |
|
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: 260.39 E-value: 4.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTIHNNLlfgnpdatretmirvckmanahdfikkmpkgydtqigdggvqLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKG 629
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
415-631 |
1.84e-76 |
|
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: 252.39 E-value: 1.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV 494
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDP 574
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVI 631
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
92-652 |
6.99e-73 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 258.34 E-value: 6.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 92 LLLIGLiTSVISGVSQPVLA------IISGRMTNVLLvidPLskefktktmenvyiFLGLGIFVSINDFC---QYMCFQR 162
Cdd:TIGR03796 159 LLLAGL-LLVLPGLVIPAFSqifvdeILVQGRQDWLR---PL--------------LLGMGLTALLQGVLtwlQLYYLRR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 163 VCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNmERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMM 242
Cdd:TIGR03796 221 LEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 243 LGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAK----YEKQLNS----GKKHAIW 314
Cdd:TIGR03796 300 IAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRwagyQAKLLNAqqelGVLTQIL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 315 GGFWSGffggifffwLMAFMGCGILYGGYLLkvgIIKSPGDVFIIVVAMLLGAYFLGLIspHLMVLLNAR---------- 384
Cdd:TIGR03796 380 GVLPTL---------LTSLNSALILVVGGLR---VMEGQLTIGMLVAFQSLMSSFLEPV--NNLVGFGGTlqelegdlnr 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 385 ---VAAASIYKTIDRVPKIDPYSRHGKKIEkvvGKVTFENVHFRYpTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTS 461
Cdd:TIGR03796 446 lddVLRNPVDPLLEEPEGSAATSEPPRRLS---GYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTI 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 462 VGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKM 541
Cdd:TIGR03796 522 AKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSR 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 542 PKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALnnASKGRTTIMIAHRLSTIREAD 621
Cdd:TIGR03796 602 PGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCD 679
|
570 580 590
....*....|....*....|....*....|.
gi 1678196980 622 KIVFFEKGVIVEAGNHEELVNLGGRYFDLVK 652
Cdd:TIGR03796 680 EIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1082-1295 |
1.70e-72 |
|
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: 238.82 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHqPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVGTIRENVclglkdvplekinqalelananrflgnlpdgidtevgerggqLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1242 LLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGR 1295
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1082-1319 |
1.06e-70 |
|
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: 236.61 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYpqRPHQP-VMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQM 1160
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPK 1240
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1241 ILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
1037-1319 |
1.13e-70 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 251.59 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1037 IIMSAQFFPQFVGAKSAAGQMFNLINRQPQTGDLKSGTKPEIRGNILFENVKFSYpqRPHQP-VMKQLQWTALRGQTVAL 1115
Cdd:TIGR01846 411 VLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGI 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1116 VGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALE 1195
Cdd:TIGR01846 489 VGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1196 LANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITI 1275
Cdd:TIGR01846 569 LAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIII 648
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1678196980 1276 AHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:TIGR01846 649 AHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
415-635 |
4.69e-70 |
|
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: 234.02 E-value: 4.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV 494
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDP 574
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAG 635
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
751-1066 |
1.62e-68 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 233.50 E-value: 1.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 751 FKNAQGNYTYMLIGLSAALIRGLDLPTFALLFAWVFEGFeFVPYGGKMMHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIV 830
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF-SLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 831 SENLGVRFRVAAFRNLLYQDAAYFDNPAHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFINCWQVAIL 910
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 911 GTALIFLLgfIMAGLAFKISIVAAEHMEND---DAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELRKSVYE 987
Cdd:cd18578 160 GLATVPLL--LLAGYLRMRLLSGFEEKNKKayeESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALIS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 988 AVNYCISQNFMYYMSCFCFALAIRIINQGDQTVDKTFRCLMAMMLCCEGIIMSAQFFPQFVGAKSAAGQMFNLINRQPQ 1066
Cdd:cd18578 238 GLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1080-1301 |
2.50e-67 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 226.22 E-value: 2.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYpqRPH-QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRT 1158
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 QMALVGQEPRLFVGTIRENVClglkdvPL-----EKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIAR 1233
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PFgeysdEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGT 1301
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
399-1321 |
1.87e-66 |
|
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: 247.94 E-value: 1.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 399 KIDPYSRHGKKIEKVVG-KVTFENVHFRYpTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQ 477
Cdd:TIGR00957 618 ELEPDSIERRTIKPGEGnSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 478 IDGVdvrdlnlewlrnvVGIVQQEPILFNDTIHNNLLFG---NPDATRETMIRVCKMANahdfIKKMPKGYDTQIGDGGV 554
Cdd:TIGR00957 697 MKGS-------------VAYVPQQAWIQNDSLRENILFGkalNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGV 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQS-----ESVVQSalNNASKGRTTIMIAHRLSTIREADKIVFFEKG 629
Cdd:TIGR00957 760 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifEHVIGP--EGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 630 VIVEAGNHEELVNLGGRYFDLVKAQAfkQDPDEIALEKEEEDQFDEFDKPTVfnrkvSVRNSRSSGRSGSEEFRR--GSL 707
Cdd:TIGR00957 838 KISEMGSYQELLQRDGAFAEFLRTYA--PDEQQGHLEDSWTALVSGEGKEAK-----LIENGMLVTDVVGKQLQRqlSAS 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 708 ANHSFDRFRKasHIPSAEdeafaLRVKETMEKDGEITAG------------FLDIFKnAQGNYTYMLIGLSAALIRGLDL 775
Cdd:TIGR00957 911 SSDSGDQSRH--HGSSAE-----LQKAEAKEETWKLMEAdkaqtgqvelsvYWDYMK-AIGLFITFLSIFLFVCNHVSAL 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 776 PTFALLFAWVFEGfefVPYGGKMMHRLAMSVIAhcaaGLGIwfFQTLSTVMFAIVSENLGV----RFRVAAFRNLLYQDA 851
Cdd:TIGR00957 983 ASNYWLSLWTDDP---MVNGTQNNTSLRLSVYG----ALGI--LQGFAVFGYSMAVSIGGIqasrVLHQDLLHNKLRSPM 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 852 AYFD-NPAhapGSLITRLAADppcvkavvdgrmmqvVYATAAVIACVTIGFINCWQVAIlGTALIFLLgfimaglafkis 930
Cdd:TIGR00957 1054 SFFErTPS---GNLVNRFSKE---------------LDTVDSMIPPVIKMFMGSLFNVI-GALIVILL------------ 1102
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 931 ivaaehmenddAGKIAIEIIENVKTIQLLTRtrRFlnsYENESKKRKRTEL--RKSVYEAVNycisQNFMYYMSCFCFAL 1008
Cdd:TIGR00957 1103 -----------ATPIAAVIIPPLGLLYFFVQ--RF---YVASSRQLKRLESvsRSPVYSHFN----ETLLGVSVIRAFEE 1162
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1009 AIRIINQGDQTVDKTFRCL---------MAMMLCCEG--IIMSAQFF---------PQFVG-AKSAAGQMFNLINRQPQ- 1066
Cdd:TIGR00957 1163 QERFIHQSDLKVDENQKAYypsivanrwLAVRLECVGncIVLFAALFavisrhslsAGLVGlSVSYSLQVTFYLNWLVRm 1242
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1067 TGDLKS-----------------------GTKPEI----RGNILFENVKFSYpqRPH-QPVMKQLQWTALRGQTVALVGP 1118
Cdd:TIGR00957 1243 SSEMETnivaverlkeysetekeapwqiqETAPPSgwppRGRVEFRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGR 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1119 SGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVClGLKDVPLEKINQALELAN 1198
Cdd:TIGR00957 1321 TGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAH 1399
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1199 ANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHR 1278
Cdd:TIGR00957 1400 LKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHR 1479
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 1678196980 1279 LSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQDL 1321
Cdd:TIGR00957 1480 LNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
382-624 |
2.82e-66 |
|
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: 234.10 E-value: 2.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 382 NARVAAASIYKTIDRVPKIDPYSRhgKKIEKVVGKVTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTS 461
Cdd:TIGR02857 289 DGVAAAEALFAVLDAAPRPLAGKA--PVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 462 VGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKM 541
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 542 PKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREAD 621
Cdd:TIGR02857 445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
...
gi 1678196980 622 KIV 624
Cdd:TIGR02857 525 RIV 527
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
415-636 |
5.69e-65 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 219.67 E-value: 5.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYptRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRN 493
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPILFNDTIHNNL-LFGNpdATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIR 572
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGN 636
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
334-661 |
1.68e-64 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 230.55 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 334 MGCGILYGGYLLKVGIIkSPGDV--FIIVVAMLLGAyfLGLISPHLMVLLNARVAAASIYKTIDRVPKIDPYSRHGKkIE 411
Cdd:TIGR01192 254 MMCILVIGTVLVIKGEL-SVGEViaFIGFANLLIGR--LDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPE-LP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 412 KVVGKVTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWL 491
Cdd:TIGR01192 330 NVKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLI 571
Cdd:TIGR01192 408 RKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAIL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDLV 651
Cdd:TIGR01192 488 KNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
330
....*....|
gi 1678196980 652 KAQAFKQDPD 661
Cdd:TIGR01192 568 RRSGLLTNQP 577
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1080-1296 |
1.26e-63 |
|
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: 215.53 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYPQRPHqPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQ 1159
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDP 1239
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1240 KILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRV 1296
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1050-1289 |
2.39e-63 |
|
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: 225.63 E-value: 2.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1050 AKSAAGQMFNLINRQPQ--TGDLKSGTKPEIRgnILFENVKFSYPQRPhqPVMKQLQWTALRGQTVALVGPSGSGKSTCI 1127
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRplAGKAPVTAAPASS--LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1128 GMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLP 1207
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1208 DGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDL 1287
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
..
gi 1678196980 1288 IV 1289
Cdd:TIGR02857 526 IV 527
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
415-650 |
7.57e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 225.47 E-value: 7.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTRkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV 494
Cdd:PRK11160 337 VSLTLNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKmPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDP 574
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDL 650
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
431-650 |
2.26e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 224.34 E-value: 2.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 431 EAKVLNG-LNLTVEPGTSVALVGHSGCGKSTsvgLLTRL--YEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFND 507
Cdd:PRK11174 361 DGKTLAGpLNFTLPAGQRIALVGPSGAGKTS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 508 TIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 588 AQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDL 650
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
142-670 |
5.57e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 223.44 E-value: 5.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 142 FLGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGI 221
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 222 SMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFlekSTgEELEKVgeAGAIAE------ECLMGVRTIQAFNGQe 295
Cdd:PRK10790 151 ALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRY---ST-PIVRRV--RAYLADindgfnEVINGMSVIQQFRQQ- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 296 emvAKYEKQLNSGKKHAIWGGFWSGFFGGIFFFWLMAFMGCGILYGgyLLKVGIIKSPGDVFIIVvamlLGAY--FLGLI 373
Cdd:PRK10790 224 ---ARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILCG--LLMLFGFSASGTIEVGV----LYAFisYLGRL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 374 SPHLM-------VLLNARVAAASIYKTIDRvpkidPYSRHGKKIEKVV-GKVTFENVHFRYptRKEAKVLNGLNLTVEPG 445
Cdd:PRK10790 295 NEPLIelttqqsMLQQAVVAGERVFELMDG-----PRQQYGNDDRPLQsGRIDIDNVSFAY--RDDNLVLQNINLSVPSR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 446 TSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNpDATRETM 525
Cdd:PRK10790 368 GFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 526 IRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGR 605
Cdd:PRK10790 447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT 526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 606 TTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGRYFDLVKAQAFKQDPDEIALEKEEE 670
Cdd:PRK10790 527 TLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREEESL 591
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
89-400 |
9.14e-62 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 213.85 E-value: 9.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 89 DYILLLIGLITSVISGVSQPVLAIISGRMTNVLLVIDPlsKEFKTKTMENVYIFLGLGIFVSINDFCQYMCFQRVCSRMM 168
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDD--DELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 169 TVMRNRYISSILRQNAGWFD--KNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLI 246
Cdd:cd18578 85 RRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 247 PVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIF 326
Cdd:cd18578 165 PLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLS 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 327 FFWLMAFMGCGILYGGYLLKVGIIkSPGDVFIIVVAMLLGAYFLGLISPHLMVLLNARVAAASIYKTIDRVPKI 400
Cdd:cd18578 245 QSLTFFAYALAFWYGGRLVANGEY-TFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1065-1317 |
5.64e-61 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 223.28 E-value: 5.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1065 PQTGDLKSGTKPEIRGNILFENVKFSYpQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMD 1144
Cdd:TIGR03796 461 PEGSAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1145 GQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGG 1224
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGG 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1225 QKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALdrAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKE 1304
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEE 697
|
250
....*....|...
gi 1678196980 1305 LMQLKGKYFELIK 1317
Cdd:TIGR03796 698 LWAVGGAYARLIR 710
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
75-652 |
7.17e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 229.92 E-value: 7.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 75 PVSLLQLFR--FATTFDYILLLIGLItsvISGVSQPVLAIISGRMTNVLLviDPLSKEFKTKTMeNVYIFLgLGIFVSIN 152
Cdd:PTZ00265 810 PNNLRIVYReiFSYKKDVTIIALSIL---VAGGLYPVFALLYAKYVSTLF--DFANLEANSNKY-SLYILV-IAIAMFIS 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 153 DFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFD--KNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVI 230
Cdd:PTZ00265 883 ETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVM 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 231 SLIYEWRLALMMLGLIPVSTICMTLLSRfLEKSTGEELEKVGEAGAI----------------AEECLMGVRTIQAFNGQ 294
Cdd:PTZ00265 963 SFYFCPIVAAVLTGTYFIFMRVFAIRAR-LTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLE 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 295 EEMVAKYEKQL---NSGKKHAIWGGFWSGFFGGIFFFWLMAFmgcGILYGGYLLKVGIIKSpgDVFIIVVAMLLgayFLG 371
Cdd:PTZ00265 1042 DYFCNLIEKAIdysNKGQKRKTLVNSMLWGFSQSAQLFINSF---AYWFGSFLIRRGTILV--DDFMKSLFTFL---FTG 1113
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 372 LISPHLMVLL----NARVAAASIYKTIDRVPKIDPYSRHGKKIEK---VVGKVTFENVHFRYPTRKEAKVLNGLNLTVEP 444
Cdd:PTZ00265 1114 SYAGKLMSLKgdseNAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDS 1193
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 445 GTSVALVGHSGCGKSTSVGLLTRLYE------------------------------------------------------ 470
Cdd:PTZ00265 1194 KKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvf 1273
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 471 PEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIG 550
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVG 1353
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 551 DGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIREADKIVFFEK 628
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNN 1433
|
650 660 670
....*....|....*....|....*....|
gi 1678196980 629 ----GVIVEA-GNHEELVNL-GGRYFDLVK 652
Cdd:PTZ00265 1434 pdrtGSFVQAhGTHEELLSVqDGVYKKYVK 1463
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
171-672 |
7.62e-61 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 219.58 E-value: 7.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 171 MRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDklGVLIRGISMVIAS---VVISLIYEWRLALMMLGLIP 247
Cdd:PRK10789 71 LREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGE--GVLTLVDSLVMGCavlIVMSTQISWQLTLLALLPMP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 248 VSTICMtllsrfleKSTGEELE---KVGEAGAI-----AEECLMGVRTIQAFNGQEEMVAKYEK-QLNSGKKHaiwggfw 318
Cdd:PRK10789 149 VMAIMI--------KRYGDQLHerfKLAQAAFSslndrTQESLTSIRMIKAFGLEDRQSALFAAdAEDTGKKN------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 319 SGFFGGIFFFWLMAFMGCGIlygGYLLKVGiiksPGDVFIIVVAMLLG-----AYFLGL-ISPHL----MVLLNARVAAA 388
Cdd:PRK10789 214 MRVARIDARFDPTIYIAIGM---ANLLAIG----GGSWMVVNGSLTLGqltsfVMYLGLmIWPMLalawMFNIVERGSAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 389 --SIYKTIDRVPKIDPYSRHgkkIEKVVGKVTFENVHFRYPTrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLT 466
Cdd:PRK10789 287 ysRIRAMLAEAPVVKDGSEP---VPEGRGELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 467 RLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYD 546
Cdd:PRK10789 363 RHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYD 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 547 TQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFF 626
Cdd:PRK10789 443 TEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVM 522
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1678196980 627 EKGVIVEAGNHEELVNLGGRYFDLVKAQAFkqdpdEIALEKEEEDQ 672
Cdd:PRK10789 523 QHGHIAQRGNHDQLAQQSGWYRDMYRYQQL-----EAALDDAPEIR 563
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1110-1323 |
9.24e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 219.72 E-value: 9.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERF--YDvtgGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPL 1187
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1188 EKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAR 1267
Cdd:PRK11174 453 EQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS 532
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 1268 EGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQDLAI 1323
Cdd:PRK11174 533 RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
166-614 |
2.41e-60 |
|
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: 216.84 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 166 RMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDgvgdklgVLIRGIS-MVIASVVISL------IYEWRL 238
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQD-------LYVRVIVpAGVALVVGAAavaaiaVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 239 ALMMLGLIPVSTICMTLLSRFLEKSTGEELEK-VGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQlnSGKKHAIWGGF 317
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSLRAARAAEQALARlRGELAAQLTDALDGAAELVASGALPAALAQVEEA--DRELTRAERRA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 318 WSGFFGGIFFFWLMafmgCGILYGGYLLKVGIIKSPGD---VFIIVVAMLLGAYF--LGLISPHLMVLLNARVAAASIYK 392
Cdd:TIGR02868 234 AAATALGAALTLLA----AGLAVLGALWAGGPAVADGRlapVTLAVLVLLPLAAFeaFAALPAAAQQLTRVRAAAERIVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 393 TIDRVPKIDPYSRHGKKIEkVVGKVT--FENVHFRYPTrkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYE 470
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAV-GLGKPTleLRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 471 PEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIG 550
Cdd:TIGR02868 387 PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLG 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 551 DGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRL 614
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
166-654 |
6.21e-60 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 219.44 E-value: 6.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 166 RMMTVMRNRYISSI----LRQNAGWFDKNLSGTITTRLN--DNMERIQDGVGdkLGVLIRGIsMVIASVVISLIYEWRLA 239
Cdd:TIGR03797 202 RLETRMDASLQAAVwdrlLRLPVSFFRQYSTGDLASRAMgiSQIRRILSGST--LTTLLSGI-FALLNLGLMFYYSWKLA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 240 LMMLGLIPVSTICMTLLSRFLeksTGEELEKVGEAGAIAEEclmgvrTIQAFNG---------QEEMVAKYEKQLNSGKK 310
Cdd:TIGR03797 279 LVAVALALVAIAVTLVLGLLQ---VRKERRLLELSGKISGL------TVQLINGisklrvagaENRAFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 311 HA-----IWGGFWSGFFGGIFFFWLMAFMGCGILYGGYLLKVGIIKSPGDVFIIVVAMLLGayflglisphLMVLLNARV 385
Cdd:TIGR03797 350 LElsaqrIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQ----------LSNTLISIL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 386 AAASIYKTIDRVPKIDPYSRHGKKIE-KVVGKVTFENVHFRYptRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTSVG 463
Cdd:TIGR03797 420 AVIPLWERAKPILEALPEVDEAKTDPgKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLR 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 464 LLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGNPDATRETMiRVCKMANAHDFIKKMPK 543
Cdd:TIGR03797 498 LLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAW-EAARMAGLAEDIRAMPM 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 544 GYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NAskgrTTIMIAHRLSTIREAD 621
Cdd:TIGR03797 577 GMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLErlKV----TRIVIAHRLSTIRNAD 652
|
490 500 510
....*....|....*....|....*....|...
gi 1678196980 622 KIVFFEKGVIVEAGNHEELVNLGGRYFDLVKAQ 654
Cdd:TIGR03797 653 RIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1052-1319 |
1.29e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 215.84 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1052 SAAGQMFNLINRQPQTGDLKSGTKPEIRGNILFENVKFSYPQRPhQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLE 1131
Cdd:PRK11160 309 ASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1132 RFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANanrfLGNL---PD 1208
Cdd:PRK11160 388 RAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG----LEKLledDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1209 GIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLI 1288
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260 270
....*....|....*....|....*....|.
gi 1678196980 1289 VYIDDGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1057-1321 |
1.79e-59 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 215.35 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1057 MFNLINR--------------QPQTGDlksGTK--PEIRGNILFENVKFSYPQRPHqPVMKQLQWTALRGQTVALVGPSG 1120
Cdd:PRK10789 276 MFNIVERgsaaysriramlaeAPVVKD---GSEpvPEGRGELDVNIRQFTYPQTDH-PALENVNFTLKPGQMLGICGPTG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1121 SGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANAN 1200
Cdd:PRK10789 352 SGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVH 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1201 RFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLS 1280
Cdd:PRK10789 432 DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLS 511
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1678196980 1281 SIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQDL 1321
Cdd:PRK10789 512 ALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQL 552
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
415-639 |
1.92e-59 |
|
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: 215.00 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTRKEAkVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV 494
Cdd:COG4618 329 GRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNL-LFGNPDAtrETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRD 573
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIaRFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 574 PKVLLLDEATSALDAQSESVVQSALNNA-SKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEE 639
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
141-1313 |
9.77e-58 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 219.85 E-value: 9.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 141 IFLGlgifVSINDFCQYMCFQRVcSRMMTVMRNRYISSILRQNAGWFD---KNL-SGTITTRLNDNMERIQdgvgdKLGV 216
Cdd:PLN03232 347 IFFG----VTFGVLCESQYFQNV-GRVGFRLRSTLVAAIFHKSLRLTHearKNFaSGKVTNMITTDANALQ-----QIAE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 217 LIRGISMVIASVVISLIYEWRL--------ALMMLGLIPVSTIcmtLLSRfLEKSTGEELEKVGEAGAIAEECLMGVRTI 288
Cdd:PLN03232 417 QLHGLWSAPFRIIVSMVLLYQQlgvaslfgSLILFLLIPLQTL---IVRK-MRKLTKEGLQWTDKRVGIINEILASMDTV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 289 QAFNGQEEMVAKYE----KQLNSGKKHAIWGGFWSGFFGGIFFFWLMAFMGCGILYGGYLlkvgiikSPGDVFIIVVAML 364
Cdd:PLN03232 493 KCYAWEKSFESRIQgirnEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDL-------TPARAFTSLSLFA 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 365 LGAYFLGLISPHLMVLLNARVAAASIYKTI---DRVPKIDPysrhgkKIEKVVGKVTFENVHFRYPTRKEAKVLNGLNLT 441
Cdd:PLN03232 566 VLRSPLNMLPNLLSQVVNANVSLQRIEELLlseERILAQNP------PLQPGAPAISIKNGYFSWDSKTSKPTLSDINLE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 442 VEPGTSVALVGHSGCGKSTSV-GLLTRLYEPEQGSVQIdgvdvrdlnlewlRNVVGIVQQEPILFNDTIHNNLLFGNPDA 520
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGSDFE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 521 TRETMIRVCKMANAHDFikKMPKGYD-TQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQ-SESVVQSAL 598
Cdd:PLN03232 707 SERYWRAIDVTALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCM 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 599 NNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNlGGRYFDLVKAQAFKQDpdEIALEKEEEDQFDEFDk 678
Cdd:PLN03232 785 KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SGSLFKKLMENAGKMD--ATQEVNTNDENILKLG- 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 679 PTVfnrKVSVRNsrssgrsgseefrrgslanhsfdrfRKASHIPSAEdEAFALRVKETMEKDGEITAGFLDIFKNAQGN- 757
Cdd:PLN03232 861 PTV---TIDVSE-------------------------RNLGSTKQGK-RGRSVLVKQEERETGIISWNVLMRYNKAVGGl 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 758 YTYMLIGLSAALIRGLDLPTFALLFAWVFE--------GFEFVPYGGKMMHRLAMSViahcaaglgiwffqtlsTVMFAI 829
Cdd:PLN03232 912 WVVMILLVCYLTTEVLRVSSSTWLSIWTDQstpksyspGFYIVVYALLGFGQVAVTF-----------------TNSFWL 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 830 VSENLGV--RFRVAAFRNLLYQDAAYFD-NPAhapGSLITRLAADPPCVKAVVDGRM---MQVVYATAAVIACV-TIGFI 902
Cdd:PLN03232 975 ISSSLHAakRLHDAMLNSILRAPMLFFHtNPT---GRVINRFSKDIGDIDRNVANLMnmfMNQLWQLLSTFALIgTVSTI 1051
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 903 NCWQVAILgtalifLLGFIMAGLAFKISIVAAEHMENDDAGKI------AIEIIENVKTIQLLTRTRRFLNSYENESKKR 976
Cdd:PLN03232 1052 SLWAIMPL------LILFYAAYLYYQSTSREVRRLDSVTRSPIyaqfgeALNGLSSIRAYKAYDRMAKINGKSMDNNIRF 1125
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 977 KRTELRKSVYEAVNYCISQNFMYYMSCfCFAlairIINQGDQTVDKTFRCLMAMMLCCEGIIMSaqFFPQFVGAKSAAGQ 1056
Cdd:PLN03232 1126 TLANTSSNRWLTIRLETLGGVMIWLTA-TFA----VLRNGNAENQAGFASTMGLLLSYTLNITT--LLSGVLRQASKAEN 1198
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1057 MFNLINRQPQTGDLKS-------GTKP----EIRGNILFENVKFSY-PQRPhqPVMKQLQWTALRGQTVALVGPSGSGKS 1124
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSeataiieNNRPvsgwPSRGSIKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGRTGAGKS 1276
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1125 TCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVclglkdVPLEKIN-----QALELANA 1199
Cdd:PLN03232 1277 SMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNdadlwEALERAHI 1350
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1200 NRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRL 1279
Cdd:PLN03232 1351 KDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRL 1430
|
1210 1220 1230
....*....|....*....|....*....|....
gi 1678196980 1280 SSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYF 1313
Cdd:PLN03232 1431 NTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1053-1319 |
9.40e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 208.03 E-value: 9.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1053 AAGQMFNLINRQPQtgDLKSGTKPEIRGNILFENVKFSYpqRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLER 1132
Cdd:PRK10790 314 AGERVFELMDGPRQ--QYGNDDRPLQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1133 FYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGlKDVPLEKINQALELANANRFLGNLPDGIDT 1212
Cdd:PRK10790 390 YYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYT 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1213 EVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYID 1292
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
250 260
....*....|....*....|....*..
gi 1678196980 1293 DGRVQESGTHKELMQLKGKYFELIKKQ 1319
Cdd:PRK10790 549 RGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
410-1313 |
1.46e-56 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 216.14 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 410 IEKVVGKVTFENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSV-GLLTRLYEPEQGSVQIdgvdvrdlnl 488
Cdd:PLN03130 608 LEPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVI---------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 489 ewlRNVVGIVQQEPILFNDTIHNNLLFGNP-DATR-ETMIRVCKMAnaHDfIKKMPKGYDTQIGDGGVQLSGGQKQRVAI 566
Cdd:PLN03130 678 ---RGTVAYVPQVSWIFNATVRDNILFGSPfDPERyERAIDVTALQ--HD-LDLLPGGDLTEIGERGVNISGGQKQRVSM 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAQ-SESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNlGG 645
Cdd:PLN03130 752 ARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 646 RYFDLVKAQAFKQDpDEIALEKEEEDQFDEfDKPTvfnrkvsvrnsrssgrsgseefrrgslANHSFDRFRKASHIPSAE 725
Cdd:PLN03130 831 PLFQKLMENAGKME-EYVEENGEEEDDQTS-SKPV---------------------------ANGNANNLKKDSSSKKKS 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 726 DEAFALRVKETMEKDGEITAGFLDIFKNAQGN-YTYMLIGLSAALIRGLDLPTFALLFAWVFEGfEFVPYGgKMMHRLAM 804
Cdd:PLN03130 882 KEGKSVLIKQEERETGVVSWKVLERYKNALGGaWVVMILFLCYVLTEVFRVSSSTWLSEWTDQG-TPKTHG-PLFYNLIY 959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 805 SVIAhcaaglgiwFFQTLSTVM--FAIVSENL--GVRFRVAAFRNLLYQDAAYFD-NPAhapGSLITRLAAD----PPCV 875
Cdd:PLN03130 960 ALLS---------FGQVLVTLLnsYWLIMSSLyaAKRLHDAMLGSILRAPMSFFHtNPL---GRIINRFAKDlgdiDRNV 1027
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 876 KAVVDGRMMQV--VYATAAVIACVTIgfINCWQVAILgtalifLLGFIMAGLAFKISIVAAEHMENDDAGKIAI---EII 950
Cdd:PLN03130 1028 AVFVNMFLGQIfqLLSTFVLIGIVST--ISLWAIMPL------LVLFYGAYLYYQSTAREVKRLDSITRSPVYAqfgEAL 1099
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 951 ENVKTIqlltrtrRFLNSYENESKKRKRTELRKSVYEAVNycISQNFMY---------YMSCFCFALAI----RIINQgd 1017
Cdd:PLN03130 1100 NGLSTI-------RAYKAYDRMAEINGRSMDNNIRFTLVN--MSSNRWLairletlggLMIWLTASFAVmqngRAENQ-- 1168
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1018 qtvdKTFRCLMAMMLCCEGIIMSaqFFPQFVGAKSAAGQMFNLINRQPQTGDLKSGTKPEIRGN-----------ILFEN 1086
Cdd:PLN03130 1169 ----AAFASTMGLLLSYALNITS--LLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNrpppgwpssgsIKFED 1242
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1087 VKFSY-PQRPhqPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQ 1165
Cdd:PLN03130 1243 VVLRYrPELP--PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1166 EPRLFVGTIRENVclglkDvPLEKIN-----QALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPK 1240
Cdd:PLN03130 1321 APVLFSGTVRFNL-----D-PFNEHNdadlwESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1241 ILLLDEATSALDSESERAVQEALdrAREGRTC--ITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYF 1313
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTI--REEFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1045-1307 |
5.29e-55 |
|
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: 201.90 E-value: 5.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1045 PQFVGAKSAAGQMFNLINRQPQTGDlksGTK-PEIRGNILFENVKFSYPQRPhQPVMKQLQWTALRGQTVALVGPSGSGK 1123
Cdd:COG4618 296 KQFVSARQAYRRLNELLAAVPAEPE---RMPlPRPKGRLSVENLTVVPPGSK-RPILRGVSFSLEPGEVLGVIGPSGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1124 ST---CI-GMLErfydVTGGALRMDGQDIKNISlyhlRTQMA-LVG---QEPRLFVGTIRENVClGLKDVPLEKINQALE 1195
Cdd:COG4618 372 STlarLLvGVWP----PTAGSVRLDGADLSQWD----REELGrHIGylpQDVELFDGTIAENIA-RFGDADPEKVVAAAK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1196 LANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRARE-GRTCIT 1274
Cdd:COG4618 443 LAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVV 522
|
250 260 270
....*....|....*....|....*....|...
gi 1678196980 1275 IAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:COG4618 523 ITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1077-1319 |
6.50e-53 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 198.64 E-value: 6.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1077 EIRGNILFENVKFSYpqRPHQP-VMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYH 1155
Cdd:TIGR03797 447 KLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVGQEPRLFVGTIRENVClGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARAL 1235
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1236 VRDPKILLLDEATSALDSESERAVQEALDRAREGRtcITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFEL 1315
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
....
gi 1678196980 1316 IKKQ 1319
Cdd:TIGR03797 682 ARRQ 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
175-653 |
7.01e-53 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 198.81 E-value: 7.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 175 YISSILRQNAGWFDKNLSGTITTRLNDnMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICMT 254
Cdd:TIGR01193 235 YIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIII 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 255 LLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAK----YEKQLNSGKKHAIWGgfwsgffggifffwl 330
Cdd:TIGR01193 314 LFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKAD--------------- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 331 mafmgcgilYGGYLLKVGIikspgDVFIIVVAMLLGAYF-------LG-------LISPHLMVLLN----------ARVA 386
Cdd:TIGR01193 379 ---------QGQQAIKAVT-----KLILNVVILWTGAYLvmrgkltLGqlitfnaLLSYFLTPLENiinlqpklqaARVA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 387 aasiYKTIDRVPKIDPYSRHGKKI---EKVVGKVTFENVHFRYPTrkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVG 463
Cdd:TIGR01193 445 ----NNRLNEVYLVDSEFINKKKRtelNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 464 LLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFGN-PDATRETMIRVCKMANAHDFIKKMP 542
Cdd:TIGR01193 519 LLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMP 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 543 KGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNAsKGRTTIMIAHRLSTIREADK 622
Cdd:TIGR01193 599 LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDK 677
|
490 500 510
....*....|....*....|....*....|.
gi 1678196980 623 IVFFEKGVIVEAGNHEELVNLGGRYFDLVKA 653
Cdd:TIGR01193 678 IIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1046-1307 |
8.05e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 189.10 E-value: 8.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1046 QFVGAKSAAGQMFNLINRQPQTGDLKSgtKPEIRGNILFENVKFSYPQrPHQPVMKQLQWTALRGQTVALVGPSGSGKST 1125
Cdd:TIGR01842 283 QFSGARQAYKRLNELLANYPSRDPAMP--LPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKST 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1126 CIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGN 1205
Cdd:TIGR01842 360 LARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1206 LPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAR-EGRTCITIAHRLSSIQN 1284
Cdd:TIGR01842 440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGC 519
|
250 260
....*....|....*....|...
gi 1678196980 1285 SDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:TIGR01842 520 VDKILVLQDGRIARFGERDEVLA 542
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
417-640 |
1.42e-49 |
|
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: 175.60 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPtrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPI--LFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIAR 568
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 569 TLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
356-640 |
3.75e-49 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 184.09 E-value: 3.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 356 VFIIVVAML---LGAYFL--GLISPHLMV---LLNARV---------------AAASIYKTIDRVPKIDPYSRHGKKIEK 412
Cdd:TIGR01842 233 YFRIVLQSLvlgLGAYLAidGEITPGMMIagsILVGRAlapidgaiggwkqfsGARQAYKRLNELLANYPSRDPAMPLPE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 413 VVGKVTFENVHFRYPTRKeAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLR 492
Cdd:TIGR01842 313 PEGHLSVENVTIVPPGGK-KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 493 NVVGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIR 572
Cdd:TIGR01842 392 KHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNASK-GRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
417-635 |
8.15e-49 |
|
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: 171.34 E-value: 8.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPtRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlEWLRNVVG 496
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTIHNNLlfgnpdatretmirvckmanahdfikkmpkgydtqigdgGVQLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAG 635
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
419-629 |
1.33e-48 |
|
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: 172.27 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 419 FENVHFRYPTRKEaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIV 498
Cdd:cd03225 2 LKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEP--ILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTL 570
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 571 IRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKG 629
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1080-1316 |
1.43e-48 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 185.71 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYPQrpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQ 1159
Cdd:TIGR01193 472 GDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVGTIRENVCLGLKD-VPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRD 1238
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALDRAREgRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELI 1316
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
420-631 |
1.60e-47 |
|
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: 167.78 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKEAkVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:cd03246 4 ENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEPILFNDTIHNNLLfgnpdatretmirvckmanahdfikkmpkgydtqigdggvqlSGGQKQRVAIARTLIRDPKVLLL 579
Cdd:cd03246 83 QDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 580 DEATSALDAQSESVVQSALNNASK-GRTTIMIAHRLSTIREADKIVFFEKGVI 631
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1084-1296 |
3.32e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALV 1163
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPRLFVGTIRENVclglkDVPLEKINQALELANANRFLG--NLPDGI-DTEVGErggqLSGGQKQRIAIARALVRDPK 1240
Cdd:COG4619 80 PQEPALWGGTVRDNL-----PFPFQLRERKFDRERALELLErlGLPPDIlDKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1241 ILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
95-652 |
1.37e-45 |
|
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: 180.53 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 95 IGLITSVIS---GVSQPVLAIISgrmtNVLLVI---DPLSKEFKTKTMENVYIFLGLGIFVSINDFCQYMCFQRVCSRMM 168
Cdd:TIGR00957 962 IGLFITFLSiflFVCNHVSALAS----NYWLSLwtdDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQAS 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 169 TVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALmmlgLIPV 248
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAV----IIPP 1113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 249 STICMTLLSRFLEKSTGE--ELEKVGEAGAIAE--ECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGG 324
Cdd:TIGR00957 1114 LGLLYFFVQRFYVASSRQlkRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAV 1193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 325 IfffwlMAFMG-CGILYGGyllkvgiikspgdVFIIVVAMLLGAYFLGL-ISPHLMVL--LNARVAAASIYKT-IDRVPK 399
Cdd:TIGR00957 1194 R-----LECVGnCIVLFAA-------------LFAVISRHSLSAGLVGLsVSYSLQVTfyLNWLVRMSSEMETnIVAVER 1255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 400 IDPYSRHGKKIEKVV------------GKVTFENVHFRYptRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLT 466
Cdd:TIGR00957 1256 LKEYSETEKEAPWQIqetappsgwpprGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 467 RLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNL-LFGNpdATRETMIRVCKMANAHDFIKKMPKGY 545
Cdd:TIGR00957 1334 RINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKL 1411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 546 DTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVF 625
Cdd:TIGR00957 1412 DHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV 1491
|
570 580
....*....|....*....|....*..
gi 1678196980 626 FEKGVIVEAGNHEELVNLGGRYFDLVK 652
Cdd:TIGR00957 1492 LDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
418-631 |
1.77e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.06 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGI 497
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VQQEPILFNDTIHNNLLFgnPDATREtmiRVCKMANAHDFIKKM--PKGY-DTQIGDggvqLSGGQKQRVAIARTLIRDP 574
Cdd:COG4619 79 VPQEPALWGGTVRDNLPF--PFQLRE---RKFDRERALELLERLglPPDIlDKPVER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLSTI-READKIVFFEKGVI 631
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
431-1305 |
1.89e-45 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 180.36 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 431 EAKVL-NGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVqidgvdvrdlnleWLRNVVGIVQQEPILFNDTI 509
Cdd:PTZ00243 671 EPKVLlRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 510 HNNLLFGNP-DATR-ETMIRVCKM-ANahdfIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:PTZ00243 738 RGNILFFDEeDAARlADAVRVSQLeAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 587 DAQ-SESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNlGGRYFDLVKAQAFKQDPDEIAL 665
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-TSLYATLAAELKENKDSKEGDA 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 666 EKEEEDQFDEFDKPTVFNRKVSvrnSRSSGRSGSEEFRRGSLANHSFDRFRKAS-HIPSAEDEAFaLRVKETMEKDGEIT 744
Cdd:PTZ00243 893 DAEVAEVDAAPGGAVDHEPPVA---KQEGNAEGGDGAALDAAAGRLMTREEKASgSVPWSTYVAY-LRFCGGLHAAGFVL 968
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 745 A--GFLDIFKNAQG--------------NYTYMLIGLSAALIRGLDLPtfaLLFawvFEGFEFVPYGGKMMHRLAMSVIA 808
Cdd:PTZ00243 969 AtfAVTELVTVSSGvwlsmwstrsfklsAATYLYVYLGIVLLGTFSVP---LRF---FLSYEAMRRGSRNMHRDLLRSVS 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 809 -----------------HCAAGLGI--------------WFFQTLSTVMFAIVSENL---------GVRFRVAAFRNLLY 848
Cdd:PTZ00243 1043 rgtmsffdttplgrilnRFSRDIDIldntlpmsylyllqCLFSICSSILVTSASQPFvlvalvpcgYLYYRLMQFYNSAN 1122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 849 QDAAYFDNPAHAP-GSLITRLAADPPCVKAVvdGRM---MQ-------VVYAtAAVIACVTigfiNCWqvaiLGTALIFL 917
Cdd:PTZ00243 1123 REIRRIKSVAKSPvFTLLEEALQGSATITAY--GKAhlvMQealrrldVVYS-CSYLENVA----NRW----LGVRVEFL 1191
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 918 LGFIMAGLAFKISIVAAEHMENDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRtelrksvyeavnycisqnF 997
Cdd:PTZ00243 1192 SNIVVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVER------------------L 1253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 998 MYYmscfcfalaIRIINQGDQtvdKTFRCLMAMMLCCEGIimsaqffpqfvgAKSAAGQMfnLINRQPQTGdlkSGTKPE 1077
Cdd:PTZ00243 1254 LYY---------TDEVPHEDM---PELDEEVDALERRTGM------------AADVTGTV--VIEPASPTS---AAPHPV 1304
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1078 IRGNILFENVKFSYpqRPHQP-VMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHL 1156
Cdd:PTZ00243 1305 QAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL 1382
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1157 RTQMALVGQEPRLFVGTIRENVCLGLKDVPLEkINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALV 1236
Cdd:PTZ00243 1383 RRQFSMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1237 -RDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PTZ00243 1462 kKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
93-365 |
2.37e-45 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 165.12 E-value: 2.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQPVLAIISGRMTNVLLVIDPLSKEFKTKTMenvYIFLGLGIFVSINDFCQYMCFQRVCSRMMTVMR 172
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYS---LALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 173 NRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTIC 252
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 253 MTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIFFFWLMA 332
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|...
gi 1678196980 333 FMGCGILYGGYLLKVGIIkSPGDVFIIVVAMLL 365
Cdd:pfam00664 238 SYALALWFGAYLVISGEL-SVGDLVAFLSLFAQ 269
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
417-640 |
1.08e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 170.47 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRK--EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWL 491
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQEPIL-FN--DTIHNNLLFG-------NPDATRETMIRVCKMAN-AHDFIKKMPKgydtqigdggvQLSGGQ 560
Cdd:COG1123 341 RRRVQMVFQDPYSsLNprMTVGDIIAEPlrlhgllSRAERRERVAELLERVGlPPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 561 KQRVAIARTLIRDPKVLLLDEATSALDAqseSVVQSALN-----NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEA 634
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV---SVQAQILNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486
|
....*.
gi 1678196980 635 GNHEEL 640
Cdd:COG1123 487 GPTEEV 492
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1080-1301 |
5.60e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 158.73 E-value: 5.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYpqRPHQP-VMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRT 1158
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 QMALVGQEPRLFVGTIRENVclglkDV----PLEKINQALelananrflgnlpdgidtEVGERGGQLSGGQKQRIAIARA 1234
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL-----DPfdeySDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1235 LVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGT 1301
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
415-635 |
5.82e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 158.73 E-value: 5.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTRKEaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV 494
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLLFGNPDATRETMIRVckmanahdfikkmpkgydtQIGDGGVQLSGGQKQRVAIARTLIRDP 574
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAG 635
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
417-640 |
1.10e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.07 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVvG 496
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFND-TIHNNL-----LFGNPDATRETMI-RVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIART 569
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIdELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1084-1305 |
1.23e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 158.50 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYpqRPHQpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDV-----TGGALRMDGQDI--KNISLYHL 1156
Cdd:cd03260 3 LRDLNVYY--GDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1157 RTQMALVGQEPRLFVGTIRENVCLGLK-------DVPLEKINQALELAnanrflgnlpdGIDTEVGER--GGQLSGGQKQ 1227
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKA-----------ALWDEVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1228 RIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
417-624 |
3.30e-43 |
|
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: 156.86 E-value: 3.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEA-KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwlrnvV 495
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 GIVQQEPILFN-DTIHNNLLFG---NPDATRETMIRVCKMANA---HDFIKKMPKgydtqigdggvQLSGGQKQRVAIAR 568
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQGVPKAEARERAEELLELvglSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 569 TLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLS-TIREADKIV 624
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVV 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
419-640 |
5.04e-43 |
|
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: 156.57 E-value: 5.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 419 FENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYE-----PEQGSVQIDGVDVRDL--NLEWL 491
Cdd:cd03260 3 LRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQEPILFNDTIHNNLLFG------NPDATRETMIRVC-KMANAHDFIKKMPKGYDtqigdggvqLSGGQKQRV 564
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlRKAALWDEVKDRLHALG---------LSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 565 AIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
862-1279 |
1.12e-42 |
|
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: 164.84 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 862 GSLITRLAAD-------------PPCVKAVVdgrmmqvvyataAVIACVTIGFINcWQVAILGTALIFLLGFIM---AGL 925
Cdd:TIGR02868 110 GDLLGRLGADvdalqdlyvrvivPAGVALVV------------GAAAVAAIAVLS-VPAALILAAGLLLAGFVAplvSLR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 926 AFKISIVAAEHMENDDAGKIAiEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELRKSVYEAVNYCISQNFMyyMSCFC 1005
Cdd:TIGR02868 177 AARAAEQALARLRGELAAQLT-DALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAA--GLAVL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1006 FALAIRIINQGDQTVDKTFrcLMAMMLCcegiIMSA--QFFP------QFVGAKSAAGQMFNLInRQPQTGDLKS----G 1073
Cdd:TIGR02868 254 GALWAGGPAVADGRLAPVT--LAVLVLL----PLAAfeAFAAlpaaaqQLTRVRAAAERIVEVL-DAAGPVAEGSapaaG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1074 TKPEIRGNILFENVKFSYPQRPhqPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISL 1153
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1154 YHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIAR 1233
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALAR 484
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRL 1279
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
417-629 |
1.28e-42 |
|
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: 154.55 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKE--AKVLNGLNLTVEPGTSVALVGHSGCGKSTsvgLLTRL---YEPEQGSVQIDGVdvrdlnlewl 491
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 rnvVGIVQQEPILFNDTIHNNLLFGNP-DATR-ETMIRVCKMANahDfIKKMPKGYDTQIGDGGVQLSGGQKQRVAIART 569
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKACALEP--D-LEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 570 LIRDPKVLLLDEATSALDAQ-SESVVQSALNNA-SKGRTTIMIAHRLSTIREADKIVFFEKG 629
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHvGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
416-629 |
2.69e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.02 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 416 KVTFENVHFRYPTRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwlrnv 494
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFN-DTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIA 567
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHrlsTIREA----DKIVFFEKG 629
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH---DVDEAvflaDRVVVLSAR 215
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
93-390 |
2.76e-42 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 157.82 E-value: 2.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQPVLAIISGRMTNVLLVIDPLSKEFKTKTMEN---------------VYIFLGLGIFVSINDFCQY 157
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSsagpfekleeemtlyAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 158 MCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWR 237
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 238 LALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGF 317
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 318 WSGFFGGIFFFWLMAFMGCGILYGGYLLkVGIIKSPGDVFIIVVAMLLGAYFLGLISPHLMVLLNARVAAASI 390
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLV-TQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
417-644 |
6.75e-42 |
|
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: 154.90 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPtRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDL-NLEWLRNVV 495
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 GIVQQEPilfnD------TIHNNLLFG--NPDATRETMIR----VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQR 563
Cdd:TIGR04520 80 GMVFQNP----DnqfvgaTVEDDVAFGleNLGVPREEMRKrvdeALKLVGMEDFRDREPH-----------LLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 564 VAIARTLIRDPKVLLLDEATSALDAQS-ESVVQSALN-NASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAG------ 635
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreif 224
|
250
....*....|
gi 1678196980 636 -NHEELVNLG 644
Cdd:TIGR04520 225 sQVELLKEIG 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1085-1296 |
1.27e-41 |
|
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: 150.83 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVG 1164
Cdd:cd03246 4 ENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEPRLFVGTIRENVclglkdvplekinqalelananrflgnlpdgidtevgerggqLSGGQKQRIAIARALVRDPKILLL 1244
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1245 DEATSALDSESERAVQEALDRARE-GRTCITIAHRLSSIQNSDLIVYIDDGRV 1296
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-642 |
1.60e-41 |
|
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: 153.03 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIV 498
Cdd:COG1124 5 RNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPIL-FN------DTIHNNL-LFGNPDATRetmiRVCKMANA----HDFIKKMPKgydtqigdggvQLSGGQKQRVAI 566
Cdd:COG1124 85 FQDPYAsLHprhtvdRILAEPLrIHGLPDREE----RIAELLEQvglpPSFLDRYPH-----------QLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAqsesVVQSA-LN-----NASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEE 639
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVAD 225
|
...
gi 1678196980 640 LVN 642
Cdd:COG1124 226 LLA 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
417-633 |
1.66e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.50 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEA-KVLNGLNLTVEPGTSVALVGHSGCGKST---SVGLLTRlyePEQGSVQIDGVDVRDLN---LE 489
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 490 WLRN-VVGIVQQEPILFND-TIHNN-----LLFGNPDATRETMIR-VCKMANAHDFIKKMPKgydtqigdggvQLSGGQK 561
Cdd:COG1136 82 RLRRrHIGFVFQFFNLLPElTALENvalplLLAGVSRKERRERAReLLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 562 QRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIREADKIVFFEKGVIVE 633
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1082-1295 |
2.17e-41 |
|
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: 151.08 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQ--PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLerfydvTGGALRMDGQdiknislYHLRTQ 1159
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL------LGELEKLSGS-------VSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVGTIRENVCLGLkdvPL--EKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVR 1237
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGK---PFdeERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1238 DPKILLLDEATSALDSES-----ERAVQEALdraREGRTCITIAHRLSSIQNSDLIVYIDDGR 1295
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
91-653 |
2.93e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 166.69 E-value: 2.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIGLITSVISGVSQPVLAIISGRMTnvllvidplSKEFKTKTMENVYIFLGLG-IFVSI-NDFCQYMCFQRVCSRMM 168
Cdd:PLN03232 916 ILLVCYLTTEVLRVSSSTWLSIWTDQST---------PKSYSPGFYIVVYALLGFGqVAVTFtNSFWLISSSLHAAKRLH 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 169 TVMrnryISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDklgvlirgismvIASVVISLIYEWRLALMMLGLipV 248
Cdd:PLN03232 987 DAM----LNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVAN------------LMNMFMNQLWQLLSTFALIGT--V 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 249 STIC----MTLLSRFLE-----KSTGEE---LEKVGEAGAIAE--ECLMGVRTIQAFNGQEEMVAKYEKQLNSGkkhaIW 314
Cdd:PLN03232 1049 STISlwaiMPLLILFYAaylyyQSTSREvrrLDSVTRSPIYAQfgEALNGLSSIRAYKAYDRMAKINGKSMDNN----IR 1124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 315 GGFWSGFFGGIFFFWLMAFMGCGILYGGYLLKVGIIKSPGDVFIIVVAMLLGAYFLGLISPHLMVLLNARVAAASIyKTI 394
Cdd:PLN03232 1125 FTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSL-NSV 1203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 395 DRVPK-IDPYSRHGKKIEK--------VVGKVTFENVHFRYptRKE-AKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGL 464
Cdd:PLN03232 1204 ERVGNyIDLPSEATAIIENnrpvsgwpSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 465 LTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHNNLlfgNP--DATRETMIRVCKMANAHDFIKKMP 542
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPfsEHNDADLWEALERAHIKDVIDRNP 1358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 543 KGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADK 622
Cdd:PLN03232 1359 FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDK 1438
|
570 580 590
....*....|....*....|....*....|..
gi 1678196980 623 IVFFEKGVIVEAGNHEELV-NLGGRYFDLVKA 653
Cdd:PLN03232 1439 ILVLSSGQVLEYDSPQELLsRDTSAFFRMVHS 1470
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
415-675 |
3.24e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 166.45 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYptRKE-AKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRN 493
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPILFNDTIHNNLlfgNP-----DATR-ETMIRvckmANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIA 567
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL---DPfnehnDADLwESLER----AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELV-NLGGR 646
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSA 1466
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1678196980 647 YFDLVK------AQ-----AFKQDPDEIAleKEEEDQFDE 675
Cdd:PLN03130 1467 FSKMVQstgaanAQylrslVFGGDEDRLA--REESKALDG 1504
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
417-642 |
4.81e-41 |
|
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: 151.67 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLRN 493
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPILFND-TIHNNLLF------GNPDATRETMIRVC-KMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVA 565
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFplrehtDLSEAEIRELVLEKlELVGLPGAADKMPS-----------ELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
417-635 |
9.06e-41 |
|
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: 149.59 E-value: 9.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwLRNVvG 496
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNI-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILF-NDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIART 569
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLS-TIREADKIVFFEKGVIVEAG 635
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
417-642 |
1.09e-40 |
|
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: 150.34 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLRN 493
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPILFND-TIHNNLLFGNPDATR--ETMIR-----VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVA 565
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRlsEEEIReivleKLEAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
96-374 |
1.11e-40 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 152.33 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 96 GLITSVISGVSQPVLAIISGRMTNVLLVIDPLSKEFKTktmenVYIFLGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRY 175
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNEL-----ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 176 ISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICMTL 255
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 256 LSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIFFFWLMAFMG 335
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1678196980 336 CGILYGGYLLKVGIIkSPGDVF-IIVVAMLLGAYFLGLIS 374
Cdd:cd18557 236 LVLWYGGYLVLSGQL-TVGELTsFILYTIMVASSVGGLSS 274
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1082-1298 |
2.99e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 148.65 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQ-PVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDIKNIS---LY 1154
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1155 HLR-TQMALVGQE----PRLfvgTIRENVCLGL------KDVPLEKINQALELANANRFLGNLPdgidtevgergGQLSG 1223
Cdd:COG1136 82 RLRrRHIGFVFQFfnllPEL---TALENVALPLllagvsRKERRERARELLERVGLGDRLDHRP-----------SQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1224 GQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLSSIQNSDLIVYIDDGRVQE 1298
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
435-584 |
4.45e-40 |
|
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: 145.48 E-value: 4.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFND-TIHNNL 513
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 514 LFGNPDATRETMIRVCKMANAHDFIkKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATS 584
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
417-635 |
4.51e-40 |
|
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: 148.42 E-value: 4.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEA-KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLR 492
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 493 NVVGIVQQEPI-----------LFNDTIHNNLLFGNPDATRETMIRV-CKMANAHDFIKKMPkgydtqigdggVQLSGGQ 560
Cdd:cd03257 82 KEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLLlVGVGLPEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 561 KQRVAIARTLIRDPKVLLLDEATSALDAqseSVVQSALN-----NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEA 634
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDV---SVQAQILDllkklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
.
gi 1678196980 635 G 635
Cdd:cd03257 228 G 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
417-640 |
7.55e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.83 E-value: 7.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDV--RDLNLEWLRNV 494
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIV-QQepilFNdtihnnlLFgnPDAT-----RETMIRVCKM--ANAH-------------DFIKKMPKgydtqigdgg 553
Cdd:COG1126 79 VGMVfQQ----FN-------LF--PHLTvlenvTLAPIKVKKMskAEAEeramellervglaDKADAYPA---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 554 vQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:COG1126 136 -QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRI 214
|
....*....
gi 1678196980 632 VEAGNHEEL 640
Cdd:COG1126 215 VEEGPPEEF 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1084-1307 |
8.27e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.83 E-value: 8.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPHQPVmkqlqwTAL--------RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS--- 1152
Cdd:COG1123 263 VRNLSKRYPVRGKGGV------RAVddvsltlrRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrs 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1153 LYHLRTQMALVGQEP------RLfvgTIRENVCLGLKDVPL-------EKINQALELAnanrflgnlpdGIDTEVGER-G 1218
Cdd:COG1123 337 LRELRRRVQMVFQDPysslnpRM---TVGDIIAEPLRLHGLlsraerrERVAELLERV-----------GLPPDLADRyP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1219 GQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALD--RAREGRTCITIAHRLSSIQN-SDLIVYIDDGR 1295
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGR 482
|
250
....*....|..
gi 1678196980 1296 VQESGTHKELMQ 1307
Cdd:COG1123 483 IVEDGPTEEVFA 494
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1084-1295 |
8.46e-40 |
|
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: 146.84 E-value: 8.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPhQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALV 1163
Cdd:cd03225 2 LKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPR--LFVGTIRENVCLGLKDVPL------EKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARAL 1235
Cdd:cd03225 81 FQNPDdqFFGPTVEEEVAFGLENLGLpeeeieERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1236 VRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGR 1295
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
417-640 |
8.56e-40 |
|
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: 147.73 E-value: 8.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYP-TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV- 494
Cdd:cd03258 2 IELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 --VGIV-QQEPILFNDTIHNNLLF-----GNPDATRETMIR-VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVA 565
Cdd:cd03258 82 rrIGMIfQHFNLLSSRTVFENVALpleiaGVPKAEIEERVLeLLELVGLEDKADAYPA-----------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQS-ESVVQSALN-NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETtQSILALLRDiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
418-629 |
8.84e-40 |
|
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: 144.69 E-value: 8.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGI 497
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VqqepilfndtihnnllfgnpdatretmirvckmanahdfikkmpkgydtqigdggVQLSGGQKQRVAIARTLIRDPKVL 577
Cdd:cd00267 78 V-------------------------------------------------------PQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 578 LLDEATSALDAQS-ESVVQSALNNASKGRTTIMIAHRLSTIREA-DKIVFFEKG 629
Cdd:cd00267 103 LLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
417-631 |
9.57e-40 |
|
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: 146.87 E-value: 9.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEA-KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWL---- 491
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQEPILFND-TIHNN-----LLFGNPDATRETMIR-VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRV 564
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENvelplLLAGVPKKERRERAEeLLERVGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 565 AIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIREADKIVFFEKGVI 631
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1109-1305 |
1.08e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.45 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKST---CIGMLERFydvTGGALRMDGQDI--KNISLYHLRTQMALVGQEPRLFVG-TIRENVCLGL 1182
Cdd:COG1126 26 KGEVVVIIGPSGSGKSTllrCINLLEEP---DSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPHlTVLENVTLAP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 KDVPLEKINQALELANA--NRFlgnlpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESeraVQ 1260
Cdd:COG1126 103 IKVKKMSKAEAEERAMEllERV------GLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEL---VG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1261 EALD--R--AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:COG1126 174 EVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1082-1306 |
2.00e-39 |
|
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: 146.32 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:COG1122 1 IELENLSFSYPGGT--PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPR--LFVGTIRENVCLGL------KDVPLEKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIAR 1233
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPenlglpREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKELM 1306
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
419-642 |
3.78e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.06 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 419 FENVHFRYPTrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIV 498
Cdd:PRK13632 10 VENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPilfnD------TIHNNLLFG--NPDATRETMIR----VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAI 566
Cdd:PRK13632 89 FQNP----DnqfigaTVEDDIAFGleNKKVPPKKMKDiiddLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGR--TTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
761-1057 |
9.54e-39 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 146.85 E-value: 9.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 761 MLIGLSAALIRGLDLPTFALLFAWVFEGFEFVPYGG----KMMHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIVSENLGV 836
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGEsspdEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 837 RFRVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADppcVKAVVDG---RMMQVVYATAAVIACVTIGFINCWQVAILGTA 913
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSD---TNLIQDGigeKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 914 LIFLLGFIMAGLAFKIS-IVAAEHMENDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELRKSVYEAVNYC 992
Cdd:cd18577 156 TLPLIAIVGGIMGKLLSkYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 993 ISQNFMYYMSCFCFALAIRIINQGDQTVDKTFRCLMAMMLCCEGIIMSAQFFPQFVGAKSAAGQM 1057
Cdd:cd18577 236 LLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1082-1300 |
9.74e-39 |
|
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: 142.45 E-value: 9.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGqdiKNISLYH--LRTQ 1159
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG---VPVSDLEkaLSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVGTIRENVclglkdvplekinqalelananrflgnlpdgidtevgerGGQLSGGQKQRIAIARALVRDP 1239
Cdd:cd03247 77 ISVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1240 KILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESG 1300
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
417-640 |
1.26e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.92 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEA-KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV- 494
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 --VGIVQQepilfndtiHNNLL-----FGN----------PDATRETmiRVCKM---------ANAHdfikkmPKgydtq 548
Cdd:COG1135 82 rkIGMIFQ---------HFNLLssrtvAENvalpleiagvPKAEIRK--RVAELlelvglsdkADAY------PS----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 549 igdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSesvVQSALN-----NASKGRTTIMIAHRLSTIRE-ADK 622
Cdd:COG1135 140 ------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPET---TRSILDllkdiNRELGLTIVLITHEMDVVRRiCDR 210
|
250
....*....|....*...
gi 1678196980 623 IVFFEKGVIVEAGNHEEL 640
Cdd:COG1135 211 VAVLENGRIVEQGPVLDV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
417-629 |
1.33e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 142.33 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEW--LRNV 494
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILF-NDTIHNNLLFGnpdatretmirvckmanahdfikkmpkgydtqigdggvqLSGGQKQRVAIARTLIRD 573
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 574 PKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLS-TIREADKIVFFEKG 629
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1082-1296 |
2.13e-38 |
|
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: 143.01 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYP-QRPHQPVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDIKNISLYHL- 1156
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1157 ---RTQMALVGQE----PRLfvgTIRENVCLGL---KDVPLEKINQALELananrfLGNLpdGIDTEVGERGGQLSGGQK 1226
Cdd:cd03255 78 afrRRHIGFVFQSfnllPDL---TALENVELPLllaGVPKKERRERAEEL------LERV--GLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1227 QRIAIARALVRDPKILLLDEATSALDSESERAVQEAL-DRAREGRTCITIA-HRLSSIQNSDLIVYIDDGRV 1296
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
417-642 |
3.71e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 143.65 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPIL-FN----DTI------HNNLLFGNPDATRETMIRVCKMANAHDFIKKMpkgYDTqigdggvqLSGGQKQRVA 565
Cdd:COG1120 79 YVPQEPPApFGltvrELValgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 566 IARTLIRDPKVLLLDEATSALD--AQSE--SVVQSAlnNASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlaHQLEvlELLRRL--ARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
..
gi 1678196980 641 VN 642
Cdd:COG1120 226 LT 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1101-1249 |
9.44e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 138.55 E-value: 9.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1101 KQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVG-TIRENVC 1179
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 LGLKDVPLEKINQALELANANRFLGnLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATS 1249
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
417-631 |
1.14e-37 |
|
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: 140.74 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDV--RDLNLEWLRNV 494
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILF-NDTIHNNLLFGnpdatretMIRVCKM------ANAHDFIKKMpkGYDTQIGDGGVQLSGGQKQRVAIA 567
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLA--------PIKVKGMskaeaeERALELLEKV--GLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQ-SESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
417-640 |
1.54e-37 |
|
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: 148.90 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPE---QGSVQIDGVDVRDLNLEWLRN 493
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPI--LFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVA 565
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEI 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
418-646 |
2.77e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 140.76 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVvGI 497
Cdd:COG4555 3 EVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VQQEPILF-NDTIHNNL-----LFGNPDATRETMIRvckmanahDFIKK--MPKGYDTQIGDggvqLSGGQKQRVAIART 569
Cdd:COG4555 79 LPDERGLYdRLTVRENIryfaeLYGLFDEELKKRIE--------ELIELlgLEEFLDRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVNLGGR 646
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
417-635 |
2.80e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLRN 493
Cdd:COG2884 2 IRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQE-PILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPkgydtqigdggVQLSGGQKQRVAI 566
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 567 ARTLIRDPKVLLLDEATSALD-AQSESVVQsALNNASKGRTTIMIA-HRLSTIREADK-IVFFEKGVIVEAG 635
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDpETSWEIME-LLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
417-642 |
3.50e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 140.51 E-value: 3.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILF-NDTIHNNL-----LFGNPDATREtmirvckmANAHDFIKKM---PKGYDTQIGDggvQLSGGQKQRVAIA 567
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIalvpkLLKWPKEKIR--------ERADELLALVgldPAEFADRYPH---ELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRL-STIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
415-641 |
6.59e-37 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 140.43 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTRKEAkVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV 494
Cdd:cd03288 18 GEIKIHDLCVRYENNLKP-VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLlfgNPD--ATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIR 572
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELV 641
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1084-1300 |
1.67e-36 |
|
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: 138.02 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYP-QRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS---LYHLRTQ 1159
Cdd:cd03257 4 VKNLSVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQE------PRLfvgTIRENVCLGLKDV-PLEKINQALELANANRFLGNLPDGIdteVGERGGQLSGGQKQRIAIA 1232
Cdd:cd03257 84 IQMVFQDpmsslnPRM---TIGEQIAEPLRIHgKLSKKEARKEAVLLLLVGVGLPEEV---LNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1085-1307 |
1.79e-36 |
|
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: 138.78 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPH-QPVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDIKNISLYHLRTQM 1160
Cdd:COG1124 5 RNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPRLFV---GTIRENV-----CLGLKDVPlEKINQALELAnanrflgnlpdGIDTEVGER-GGQLSGGQKQRIAI 1231
Cdd:COG1124 82 QMVFQDPYASLhprHTVDRILaeplrIHGLPDRE-ERIAELLEQV-----------GLPPSFLDRyPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1232 ARALVRDPKILLLDEATSALDSeserAVQ-EALD-----RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKE 1304
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
...
gi 1678196980 1305 LMQ 1307
Cdd:COG1124 226 LLA 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
417-640 |
1.92e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTsvgLLtR----LYEPEQGSVQIDGVDVRDLNLEwLR 492
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTT---LL-RmiagFETPDSGRILLDGRDVTGLPPE-KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 493 NVvGIVQQEPILF-NDTIHNNLLFG-----NPDATRET----MIRVCKMAnahDFIKKMPKgydtqigdggvQLSGGQKQ 562
Cdd:COG3842 78 NV-GMVFQDYALFpHLTVAENVAFGlrmrgVPKAEIRArvaeLLELVGLE---GLADRYPH-----------QLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 563 RVAIARTLIRDPKVLLLDEATSALDAQS-ESV------VQSALnnaskGRTTIMIAHRLStirEA----DKIVFFEKGVI 631
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLrEEMreelrrLQREL-----GITFIYVTHDQE---EAlalaDRIAVMNDGRI 214
|
....*....
gi 1678196980 632 VEAGNHEEL 640
Cdd:COG3842 215 EQVGTPEEI 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1085-1306 |
3.26e-36 |
|
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: 138.25 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVG 1164
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEPRLFVG-TIRENVCLG----------LKDVPLEKINQALELAN----ANRFLGnlpdgidtevgerggQLSGGQKQRI 1229
Cdd:COG1120 82 QEPPAPFGlTVRELVALGryphlglfgrPSAEDREAVEEALERTGlehlADRPVD---------------ELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1230 AIARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKELM 1306
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1082-1305 |
3.89e-36 |
|
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: 137.33 E-value: 3.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQ-PVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERFydvTGGALRMDGQDIKNIS---LY 1154
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLERP---TSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1155 HLRTQMALVGQEPRLFVG-TIRENVCLGL------KDVPLEKINQALELANANRFLGNLPdgidtevgergGQLSGGQKQ 1227
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLeiagvpKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1228 RIAIARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKE 1304
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
.
gi 1678196980 1305 L 1305
Cdd:cd03258 228 V 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1082-1319 |
3.96e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.12 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLyHLRTQMA 1161
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVG-TIRENVCL--GLKDVPL----EKINQALELANanrflgnLPDGIDTEVGerggQLSGGQKQRIAIARA 1234
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfaRLYGLPRkearERIDELLELFG-------LTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1235 LVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQ--LKG 1310
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKArlLED 225
|
....*....
gi 1678196980 1311 KYFELIKKQ 1319
Cdd:COG1131 226 VFLELTGEE 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
420-631 |
4.60e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 134.83 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNvVGIVQ 499
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEPILFND-TIHNNLlfgnpdatretmirvckmanahdfikkmpkgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLL 578
Cdd:cd03230 80 EEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 579 LDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1082-1277 |
4.80e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.91 E-value: 4.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRP-HQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKnislyHLRTQM 1160
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPRLFv-gTIRENVCLGLKDVPL------EKINQALELANANRFLGNLPdgidtevgergGQLSGGQKQRIAIAR 1233
Cdd:COG1116 83 GVVFQEPALLpwlTVLDNVALGLELRGVpkaerrERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAH 1277
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1082-1306 |
6.50e-36 |
|
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: 136.66 E-value: 6.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVG-TIRENVCL--GLKDVPLEKINQ-ALELANanrfLGNLPDGidtEVGER-GGQLSGGQKQRIAIARALV 1236
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALvpKLLKWPKEKIRErADELLA----LVGLDPA---EFADRyPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1237 RDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRL-SSIQNSDLIVYIDDGRVQESGTHKELM 1306
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
420-635 |
7.19e-36 |
|
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: 134.49 E-value: 7.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QepilfndtihnnllfgnpdatretmirVCKMANAHDFIKKmpkGYDTqigdggvqLSGGQKQRVAIARTLIRDPKVLLL 579
Cdd:cd03214 80 Q---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 580 DEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAG 635
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1082-1323 |
8.64e-36 |
|
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: 136.53 E-value: 8.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKnISLYHLRTQMA 1161
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVG-TIRENV--CLGLKDVPLEKINQALElaNANRFLGnLPDGIDTEVGErggqLSGGQKQRIAIARALVRD 1238
Cdd:COG4555 78 VLPDERGLYDRlTVRENIryFAELYGLFDEELKKRIE--ELIELLG-LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALDRAREGRTCITIA-HRLSSIQN-SDLIVYIDDGRVQESGTHKELMQLKGK----- 1311
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEenled 230
|
250
....*....|...
gi 1678196980 1312 -YFELIKKQDLAI 1323
Cdd:COG4555 231 aFVALIGSEEGEA 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1084-1307 |
1.08e-35 |
|
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: 143.51 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPHqPVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQM 1160
Cdd:COG1123 7 VRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTlalALMGLLPHGGRISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPR--LFVGTIRENVCLGL------KDVPLEKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIA 1232
Cdd:COG1123 86 GMVFQDPMtqLNPVTVGDQIAEALenlglsRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESERAVQEALD--RAREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-640 |
1.33e-35 |
|
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: 138.26 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRK-EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEP---EQGSVQIDGVDVRDLNLEWLRNV- 494
Cdd:COG0444 5 RNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 ---VGIVQQEPIL-FN----------DTIHNNLLFGNPDATRET--MIRVCKMANAHDFIKKMPkgydtqigdggVQLSG 558
Cdd:COG0444 85 greIQMIFQDPMTsLNpvmtvgdqiaEPLRIHGGLSKAEARERAieLLERVGLPDPERRLDRYP-----------HELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 559 GQKQRVAIARTLIRDPKVLLLDEATSALDAqseSVVQSALN-----NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIV 632
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDV---TIQAQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMYAGRIV 230
|
....*...
gi 1678196980 633 EAGNHEEL 640
Cdd:COG0444 231 EEGPVEEL 238
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
417-631 |
1.64e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLnlewlRNVVG 496
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IV-QQE------PILFNDTI------HNNLLFGNPDATRETMIRVCKMANAHDFIKKmpkgydtQIGdggvQLSGGQKQR 563
Cdd:COG1121 79 YVpQRAevdwdfPITVRDVVlmgrygRRGLFRRPSRADREAVDEALERVGLEDLADR-------PIG----ELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 564 VAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1080-1320 |
1.70e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 136.19 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYpQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQ 1159
Cdd:cd03288 18 GEIKIHDLCVRY-ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVGTIRENV---CLGLKDvpleKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALV 1236
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLdpeCKCTDD----RLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1237 RDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFELI 1316
Cdd:cd03288 173 RKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252
|
....
gi 1678196980 1317 KKQD 1320
Cdd:cd03288 253 VRTD 256
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1097-1296 |
2.29e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 134.19 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERFydvTGGALRMDGQDIKN--ISLYHLRTQMALVGQEPRLFV 1171
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEEP---DSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1172 G-TIRENVCLGLKDVPLEKINQALELANanRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSA 1250
Cdd:cd03262 90 HlTVLENITLAPIKVKGMSKAEAEERAL--ELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1251 LDSEserAVQEALD----RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:cd03262 166 LDPE---LVGEVLDvmkdLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1085-1315 |
2.34e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 136.30 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVG 1164
Cdd:PRK13635 9 EHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEP-RLFVG-TIRENVCLGLKD--VP----LEKINQALELANANRFLGNLPdgidtevgergGQLSGGQKQRIAIARALV 1236
Cdd:PRK13635 88 QNPdNQFVGaTVQDDVAFGLENigVPreemVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1237 RDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFE 1314
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
.
gi 1678196980 1315 L 1315
Cdd:PRK13635 237 I 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1109-1300 |
2.47e-35 |
|
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: 134.18 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYhlRTQMALVGQEPRLFVG-TIRENVCLGLKD--V 1185
Cdd:cd03259 25 PGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTVAENIAFGLKLrgV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1186 PLEKINQ----ALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQE 1261
Cdd:cd03259 103 PKAEIRArvreLLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678196980 1262 ALDR--AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESG 1300
Cdd:cd03259 172 ELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1084-1295 |
4.44e-35 |
|
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: 131.21 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALV 1163
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQeprlfvgtirenvclglkdvplekinqalelananrflgnlpdgidtevgerggqLSGGQKQRIAIARALVRDPKILL 1243
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1244 LDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGR 1295
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1082-1277 |
6.29e-35 |
|
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: 133.37 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQ-RPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlyhlrTQM 1160
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPRLFV-GTIRENVCLGLKDVPL------EKINQALELANANRFLGNLPdgidtevgergGQLSGGQKQRIAIAR 1233
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVpkaearERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAH 1277
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1082-1296 |
8.28e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.03 E-value: 8.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPqrPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS---LYHLRT 1158
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 QMALVGQEPRLfVG--TIRENVCLG-----------LKDVPLEKINQALELananrfLGNLpdGIDTEVGERGGQLSGGQ 1225
Cdd:COG3638 81 RIGMIFQQFNL-VPrlSVLTNVLAGrlgrtstwrslLGLFPPEDRERALEA------LERV--GLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1226 KQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRA--REGRTCITIAHRLS-SIQNSDLIVYIDDGRV 1296
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDlARRYADRIIGLRDGRV 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1082-1323 |
9.15e-35 |
|
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: 134.48 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS-LYHLRTQM 1160
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEP-RLFVGTI-RENVCLGL--KDVPLEKI----NQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIA 1232
Cdd:TIGR04520 80 GMVFQNPdNQFVGATvEDDVAFGLenLGVPREEMrkrvDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESERAVQEALDRAR--EGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKg 1310
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV- 227
|
250
....*....|...
gi 1678196980 1311 kyfELIKKQDLAI 1323
Cdd:TIGR04520 228 ---ELLKEIGLDV 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1082-1301 |
3.49e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.82 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRpHQPVmkqlqwTAL--------RGQTVALVGPSGSGKST---CIGMLERFydvTGGALRMDGQDIKN 1150
Cdd:COG1135 2 IELENLSKTFPTK-GGPV------TALddvsltieKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1151 IS---LYHLRTQMALVGQEPRLFVG-TIRENVCLGLK--DVPLEKINQ-ALELAN-------ANRFlgnlPDgidtevge 1216
Cdd:COG1135 72 LSereLRAARRKIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKrVAELLElvglsdkADAY----PS-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1217 rggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQN-SDLIVYIDD 1293
Cdd:COG1135 140 ---QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLEN 216
|
....*...
gi 1678196980 1294 GRVQESGT 1301
Cdd:COG1135 217 GRIVEQGP 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1082-1307 |
4.41e-34 |
|
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: 131.64 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDIKNIS---LYH 1155
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVllkLIIGLLR---PDSGEILVDGQDITGLSekeLYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVGQEPRLFVG-TIRENVCLGLK---DVPLEKINQ----ALELAN----ANRFlgnlPdgidtevgergGQLSG 1223
Cdd:COG1127 80 LRRRIGMLFQGGALFDSlTVFENVAFPLRehtDLSEAEIRElvleKLELVGlpgaADKM----P-----------SELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1224 GQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*..
gi 1678196980 1301 THKELMQ 1307
Cdd:COG1127 225 TPEELLA 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1082-1305 |
5.59e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHlRtQMA 1161
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-R-NVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFv-gTIRENVCLGLK--DVP----LEKINQALELAN----ANRFlgnlPDgidtevgerggQLSGGQKQRIA 1230
Cdd:COG3842 81 MVFQDYALFphlTVAENVAFGLRmrGVPkaeiRARVAELLELVGleglADRY----PH-----------QLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1231 IARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLS---SIqnSDLIVYIDDGRVQESGTHKEL 1305
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
420-646 |
2.05e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPtRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:PRK13635 9 EHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEPilfnD------TIHNNLLFG--NPDATRETMIRVCKMA----NAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIA 567
Cdd:PRK13635 88 QNP----DnqfvgaTVQDDVAFGleNIGVPREEMVERVDQAlrqvGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGG 645
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
.
gi 1678196980 646 R 646
Cdd:PRK13635 233 M 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1082-1295 |
6.42e-33 |
|
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: 125.76 E-value: 6.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYH--LRTQ 1159
Cdd:cd03229 1 LELKNVSKRYGQKT---VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVG-TIRENVCLGLkdvplekinqalelananrflgnlpdgidtevgerggqlSGGQKQRIAIARALVRD 1238
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALGL---------------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALD--RAREGRTCITIAHRLSSIQN-SDLIVYIDDGR 1295
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1082-1307 |
7.27e-33 |
|
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: 127.62 E-value: 7.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPqrpHQPVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDI---KNISLYH 1155
Cdd:cd03261 1 IELRGLTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTllrLIVGLLR---PDSGEVLIDGEDIsglSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVGQEPRLFVG-TIRENVCLGLK---DVPLEKINQ----ALELANanrflgnLPDGIDtevgERGGQLSGGQKQ 1227
Cdd:cd03261 75 LRRRMGMLFQSGALFDSlTVFENVAFPLRehtRLSEEEIREivleKLEAVG-------LRGAED----LYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1228 RIAIARALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKE 1304
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEE 223
|
...
gi 1678196980 1305 LMQ 1307
Cdd:cd03261 224 LRA 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1082-1307 |
8.03e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.90 E-value: 8.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrphQPVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLErfyDVTGGALRMDGQDIK--NISLYHL 1156
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDGLKVNdpKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1157 RTQMALVGQEPRLFVG-TIRENVCLGLKDVPLEKINQALELANAnrFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARAL 1235
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPLRVRGASKEEAEKQARE--LLAKV--GLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1236 VRDPKILLLDEATSALDSESERAVQEAL-DRAREGRTCITIAHRLSSIQN--SDLIvYIDDGRVQESGTHKELMQ 1307
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvaSRLI-FIDKGRIAEDGDPQVLIK 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
415-642 |
1.20e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.58 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTsvgLLtR----LYEPEQGSVQIDGVDVRDLNLEw 490
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 LRNVvGIVQQEPILF-NDTIHNNLLFG-----NPDATRETMIR-VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQR 563
Cdd:COG3839 74 DRNI-AMVFQSYALYpHMTVYENIAFPlklrkVPKAEIDRRVReAAELLGLEDLLDRKPK-----------QLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 564 VAIARTLIRDPKVLLLDEATSALDAQSEsvVQ-----SALNNASkGRTTIMIAHRLS---TIreADKIVFFEKGVIVEAG 635
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLR--VEmraeiKRLHRRL-GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVG 216
|
....*..
gi 1678196980 636 NHEELVN 642
Cdd:COG3839 217 TPEELYD 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1082-1296 |
1.27e-32 |
|
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: 127.30 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS---LYHLRT 1158
Cdd:cd03256 1 IEVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 QMALVGQEPRLfVG--TIRENVCLG-----------LKDVPLEKINQALELANanRFlgnlpdGIDTEVGERGGQLSGGQ 1225
Cdd:cd03256 79 QIGMIFQQFNL-IErlSVLENVLSGrlgrrstwrslFGLFPKEEKQRALAALE--RV------GLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1226 KQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRA--REGRTCITIAHRLSSI-QNSDLIVYIDDGRV 1296
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
420-661 |
1.30e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 128.31 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:PRK13647 8 EDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEP--ILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLI 571
Cdd:PRK13647 86 QDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIA-HRLSTIRE-ADKIVFFEKGVIVEAG-----NHEELVNLG 644
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIVEQA 234
|
250
....*....|....*..
gi 1678196980 645 GRYFDLVkAQAFKQDPD 661
Cdd:PRK13647 235 GLRLPLV-AQIFEDLPE 250
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1082-1305 |
2.53e-32 |
|
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: 126.20 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYhlRTQMA 1161
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVG-TIRENVCLGL------KDVPLEKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARA 1234
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLrlkklpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1235 LVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
435-642 |
3.49e-32 |
|
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: 126.99 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV----VGIVQQEPILF-NDTI 509
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 510 HNNLLF-----GNPDATRETM-IRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEAT 583
Cdd:cd03294 120 LENVAFglevqGVPRAEREERaAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 584 SALDAQSESVVQSALNN--ASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:cd03294 189 SALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
419-631 |
4.53e-32 |
|
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: 124.57 E-value: 4.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 419 FENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLnlewlRNVVGIV 498
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 -QQE------PILFNDTI------HNNLLFGNPDATRETMIRVCKMANAHDFIKKmpkgydtQIGdggvQLSGGQKQRVA 565
Cdd:cd03235 74 pQRRsidrdfPISVRDVVlmglygHKGLFRRLSKADKAKVDEALERVGLSELADR-------QIG----ELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
417-642 |
8.41e-32 |
|
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: 124.66 E-value: 8.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVrdLNLEWLRNVVG 496
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFND-TIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIART 569
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLStirEA----DKIVFFEKGVIVEAGNHEELVN 642
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQE---EAltmsDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
418-640 |
1.79e-31 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 123.83 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV--- 494
Cdd:cd03256 2 EVENLSKTYPNGKKA--LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VG-IVQQEPILFNDTIHNNLLFGnpdatretmirvckMANAHDFIKKMPKGY---DTQIG-----DGGV---------QL 556
Cdd:cd03256 80 IGmIFQQFNLIERLSVLENVLSG--------------RLGRRSTWRSLFGLFpkeEKQRAlaaleRVGLldkayqradQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 557 SGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSAL--NNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVE 633
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVF 225
|
....*..
gi 1678196980 634 AGNHEEL 640
Cdd:cd03256 226 DGPPAEL 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1081-1307 |
2.41e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 123.33 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1081 NILFENVKFSYPQRPhqpvmKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDiknislyHLRTQ- 1159
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-------LTALPp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 ----MALVGQEPRLFVG-TIRENVCLGLK------DVPLEKINQALE---LANanrFLGNLPdgidtevgergGQLSGGQ 1225
Cdd:COG3840 69 aerpVSMLFQENNLFPHlTVAQNIGLGLRpglkltAEQRAQVEQALErvgLAG---LLDRLP-----------GQLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1226 KQRIAIARALVRDPKILLLDEATSALDSeserAV-QEALD-----RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQE 1298
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDP----ALrQEMLDlvdelCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAA 210
|
....*....
gi 1678196980 1299 SGTHKELMQ 1307
Cdd:COG3840 211 DGPTAALLD 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
417-632 |
3.17e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.63 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV-- 494
Cdd:COG3638 3 LELRNLSKRYPGGTPA--LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 -VGIVQQEPILFN--DTIHNNL------------LFGN-PDATREtmirvckmaNAHDFIKKM---PKGY---Dtqigdg 552
Cdd:COG3638 81 rIGMIFQQFNLVPrlSVLTNVLagrlgrtstwrsLLGLfPPEDRE---------RALEALERVglaDKAYqraD------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 553 gvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKG 629
Cdd:COG3638 146 --QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRriAREDGITVVVNLHQVDLARRyADRIIGLRDG 223
|
...
gi 1678196980 630 VIV 632
Cdd:COG3638 224 RVV 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
416-640 |
3.78e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.61 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 416 KVTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYE--PEQ---GSVQIDGVDV--RDLNL 488
Cdd:COG1117 11 KIEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 489 EWLRNVVGIVQQEPILFNDTIHNNLLFG-------NPDATRETMIRVCKMANAHDFIK---KMPkgydtqigdgGVQLSG 558
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAALWDEVKdrlKKS----------ALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 559 GQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNH 637
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFGPT 237
|
...
gi 1678196980 638 EEL 640
Cdd:COG1117 238 EQI 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
417-635 |
4.10e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.07 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAKV-LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLR 492
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 493 NVVGIVQQepilfndtiHNNLL-----FGN----------PDATRETmiRVCKM------ANAHDfikKMPKgydtqigd 551
Cdd:PRK11153 82 RQIGMIFQ---------HFNLLssrtvFDNvalplelagtPKAEIKA--RVTELlelvglSDKAD---RYPA-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 552 ggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSesvVQSALN-----NASKGRTTIMIAHRLSTIRE-ADKIVF 625
Cdd:PRK11153 140 ---QLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT---TRSILEllkdiNRELGLTIVLITHEMDVVKRiCDRVAV 213
|
250
....*....|
gi 1678196980 626 FEKGVIVEAG 635
Cdd:PRK11153 214 IDAGRLVEQG 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1082-1305 |
8.46e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 8.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEP-RLFVG-TIRENVCLGL--KDVPL----EKINQALELANANRFLGNLPdgidtevgergGQLSGGQKQRIAIAR 1233
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGLenKGIPHeemkERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
420-632 |
9.98e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.44 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYptRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvdvRDLNLEWLRNVVGIVQ 499
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEP--ILFNDTIHNNLLFGNPDATRETMI--RVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPK 575
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGNEQaeTVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 576 VLLLDEATSALDAQS-ESVVQSALNNASKGRTTIMIAHRLSTI-READKIVFFEKGVIV 632
Cdd:cd03226 147 LLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
417-632 |
1.69e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 118.30 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTrkeAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRdlnlewlrnvvg 496
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 ivqqepilfndtihnnllFGNPDATRETMIRVckmanAHdfikkmpkgydtqigdggvQLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03216 66 ------------------FASPRDARRAGIAM-----VY-------------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 577 LLLDEATSAL-DAQSESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIV 632
Cdd:cd03216 104 LILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1082-1317 |
1.73e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEP-RLFVG-TIRENVCLGL--KDVPLEK----INQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIAR 1233
Cdd:PRK13632 87 IIFQNPdNQFIGaTVEDDIAFGLenKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDRAREGR--TCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKgK 1311
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK-E 234
|
....*.
gi 1678196980 1312 YFELIK 1317
Cdd:PRK13632 235 ILEKAK 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1109-1307 |
2.11e-30 |
|
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: 121.60 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHL----RTQMALVGQEPRLFVG-TIRENVCLGL- 1182
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLENVAFGLe 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 -----KDVPLEKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESER 1257
Cdd:cd03294 129 vqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1258 AVQEALDR--AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:cd03294 198 EMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
420-640 |
2.19e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.10 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTsvgLLtR----LYEPEQGSVQIDGVD------VRDlnle 489
Cdd:COG1118 6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTT---LL-RiiagLETPDSGRIVLNGRDlftnlpPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 490 wlRNVvGIVQQEPILF-NDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQ 562
Cdd:COG1118 75 --RRV-GFVFQHYALFpHMTVAENIAFGlrvrppSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 563 RVAIARTLIRDPKVLLLDEATSALDAQS----ESVVQSALNNAskGRTTIMIAH------RLstireADKIVFFEKGVIV 632
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIE 213
|
....*...
gi 1678196980 633 EAGNHEEL 640
Cdd:COG1118 214 QVGTPDEV 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
61-642 |
2.65e-30 |
|
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: 130.80 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 61 LCRCDLSEQVLEFQPVSLLQLFRFATT---FDYILLLIGLITSVISGVSQPVLAIISGRMTNVLLV-------IDPLSKE 130
Cdd:TIGR01271 836 LKECFADERENVFETTTWNTYLRYITTnrnLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNYVdqqhanaSSPDVQK 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 131 FKTKT-MENVYIFLglgIFVSINDFCQYMCFQR---VCSRMMTV---MRNRYISSILRQNAGWFDKNLSGTITTRLNDNM 203
Cdd:TIGR01271 916 PVIITpTSAYYIFY---IYVGTADSVLALGFFRglpLVHTLLTVskrLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDM 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 204 ERIQDGVGDKLGVLIRGISMVIASV-VISLIYEWrlalMMLGLIPVSTICMTLLSRFLEksTGEELEKVgEAGAIAE--- 279
Cdd:TIGR01271 993 AIIDDMLPLTLFDFIQLTLIVLGAIfVVSVLQPY----IFIAAIPVAVIFIMLRAYFLR--TSQQLKQL-ESEARSPifs 1065
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 280 ---ECLMGVRTIQAFNGQEEMVAKYEKQLNSgkkHAiwggfwsgFFGGIFFFWLMAF-MGCGILYGGYLLKVGII----- 350
Cdd:TIGR01271 1066 hliTSLKGLWTIRAFGRQSYFETLFHKALNL---HT--------ANWFLYLSTLRWFqMRIDIIFVFFFIAVTFIaigtn 1134
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 351 -KSPGDVFIIV-VAMLlgayflglISPHLMVLLNARVAAASIYKTIDRVPK-ID-------PYSRHGKKIEKVV------ 414
Cdd:TIGR01271 1135 qDGEGEVGIILtLAMN--------ILSTLQWAVNSSIDVDGLMRSVSRVFKfIDlpqeeprPSGGGGKYQLSTVlvienp 1206
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 ---------GKVTFENVHFRYpTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEqGSVQIDGVDVRD 485
Cdd:TIGR01271 1207 haqkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNS 1284
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 486 LNLEWLRNVVGIVQQEPILFNDTIHNNLlfgNPDA--TRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQR 563
Cdd:TIGR01271 1285 VTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQL 1361
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 564 VAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1082-1305 |
4.53e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.95 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDIkNISLyHLRT 1158
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDL-FTNL-PPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 -QMALVGQEPRLFVG-TIRENVCLGLKDVPL------EKINQALELAN----ANRFlgnlPdgidtevgergGQLSGGQK 1226
Cdd:COG1118 75 rRVGFVFQHYALFPHmTVAENIAFGLRVRPPskaeirARVEELLELVQleglADRY----P-----------SQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1227 QRIAIARALVRDPKILLLDEATSALDS----ESERAVQEALDraREGRTCITIAH------RLssiqnSDLIVYIDDGRV 1296
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRI 212
|
....*....
gi 1678196980 1297 QESGTHKEL 1305
Cdd:COG1118 213 EQVGTPDEV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1082-1307 |
4.77e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKST---CI-GMLErfydVTGGALRMDGQDIKnislyHLR 1157
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTllkAIlGLLP----PTSGTVRLFGKPPR-----RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1158 TQMALVGQE---PRLFVGTIRENVCLGL-KDVPL---------EKINQALELAN----ANRFLGnlpdgidtevgerggQ 1220
Cdd:COG1121 75 RRIGYVPQRaevDWDFPITVRDVVLMGRyGRRGLfrrpsradrEAVDEALERVGledlADRPIG---------------E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1221 LSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSI-QNSDLIVYIDDGRVqE 1298
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLV-A 218
|
....*....
gi 1678196980 1299 SGTHKELMQ 1307
Cdd:COG1121 219 HGPPEEVLT 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1109-1305 |
4.81e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.53 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGA-----LRMDGQDI--KNISLYHLRTQMALVGQEPRLFVGTIRENVCLG 1181
Cdd:COG1117 36 ENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1182 L-------KDVPLEKINQALELANanrflgnLPDgidtEVGER----GGQLSGGQKQRIAIARALVRDPKILLLDEATSA 1250
Cdd:COG1117 116 LrlhgiksKSELDEIVEESLRKAA-------LWD----EVKDRlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1251 LDSESERAVQEALDRAREGRTCITIAH------RLssiqnSDLIVYIDDGRVQESGTHKEL 1305
Cdd:COG1117 185 LDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
417-635 |
9.13e-30 |
|
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: 118.13 E-value: 9.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwLRNVVG 496
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTL 570
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 571 IRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAH-RLSTIREADKIVFFEKGVIVEAG 635
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1084-1292 |
1.23e-29 |
|
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: 117.63 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKST---CI-GMLERfydvTGGALRMDGQDIKNIslyhlRTQ 1159
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkAIlGLLKP----TSGSIRVFGKPLEKE-----RKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQE---PRLFVGTIRENVCLGL--KDVPL--------EKINQALE----LANANRFLGnlpdgidtevgerggQLS 1222
Cdd:cd03235 70 IGYVPQRrsiDRDFPISVRDVVLMGLygHKGLFrrlskadkAKVDEALErvglSELADRQIG---------------ELS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1223 GGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQNS-DLIVYID 1292
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1036-1278 |
1.42e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 125.69 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1036 GIIMSAQFFPQFVGAKS------------AAG-----QMFNLINRQPQTGDLKSGTKPEIRGNILFENVKFSYPQrpHQP 1098
Cdd:COG4178 300 GLMQAASAFGQVQGALSwfvdnyqslaewRATvdrlaGFEEALEAADALPEAASRIETSEDGALALEDLTLRTPD--GRP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1099 VMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERFYdvTGGALRMDGQDiknislyhlrtqMALVGQEPRLFVGTIR 1175
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTllrAIAGLWPYG--SGRIARPAGAR------------VLFLPQRPYLPLGTLR 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVC--LGLKDVPLEKINQALELANanrfLGNLPDGIDTEvgERGGQ-LSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:COG4178 444 EALLypATAEAFSDAELREALEAVG----LGHLAERLDEE--ADWDQvLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
250 260
....*....|....*....|....*.
gi 1678196980 1253 SESERAVQEALDRAREGRTCITIAHR 1278
Cdd:COG4178 518 EENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
417-642 |
1.65e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.52 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAkVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPE---QGSVQIDGVDVRDLNLEWLRN 493
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEP--ILFNDTIHNNLLFG--NPDATRETMIRVCKMANAH----DFIKKMPKgydtqigdggvQLSGGQKQRVA 565
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADvgmlDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
93-390 |
2.46e-29 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 119.19 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQPVLAIISGRMTNVLLVIDPLSKEFKTktmenVYIFLGLGIFVSINDFCQYMCFQRVCSRMMTVMR 172
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWI-----ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 173 NRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTIC 252
Cdd:cd07346 76 RDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 253 MTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIFFFWLMA 332
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 333 FMGCGILYGGYLLKVGIIkSPGD--VFIIVVAMLLGAyfLGLISPHLMVLLNARVAAASI 390
Cdd:cd07346 236 GTALVLLYGGYLVLQGSL-TIGElvAFLAYLGMLFGP--IQRLANLYNQLQQALASLERI 292
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
417-642 |
2.66e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.50 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRD--LNLEWLRNV 494
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFND-TIHNNLLFGnPDATReTMIRVCKMANAHDFIKKMpkGYDTQIGDGGVQLSGGQKQRVAIARTLIRD 573
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFG-PLRVR-GASKEEAEKQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 574 PKVLLLDEATSALDAQ-SESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK09493 155 PKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1085-1296 |
3.78e-29 |
|
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: 114.80 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLyHLRTQMALVG 1164
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEPRLFVG-TIRENVclglkdvplekinqalelananrflgnlpdgidtevgerggQLSGGQKQRIAIARALVRDPKILL 1243
Cdd:cd03230 80 EEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1244 LDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
420-642 |
1.10e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.46 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRY--PTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRD--LNLEWLRNVV 495
Cdd:PRK13637 6 ENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 GIVQQEP--ILFNDTIHNNLLFGNPD---ATRETMIRVCKMANA-----HDFIKKMPkgydtqigdggVQLSGGQKQRVA 565
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFGPINlglSEEEIENRVKRAMNIvgldyEDYKDKSP-----------FELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1085-1300 |
1.56e-28 |
|
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: 113.30 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVG 1164
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QeprlfvgtirenvclglkdvplekinqALELANANRFLgnlpdgidtevgERG-GQLSGGQKQRIAIARALVRDPKILL 1243
Cdd:cd03214 80 Q---------------------------ALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1244 LDEATSALDSESERAVQEALDR--AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESG 1300
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1109-1307 |
1.67e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 117.91 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS---LYHLRTQMALVGQEP------RLFVGTI----- 1174
Cdd:COG4608 43 RGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnpRMTVGDIiaepl 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1175 RENvclGLKDV--PLEKINQALEL-----ANANRFlgnlPdgidtevgergGQLSGGQKQRIAIARALVRDPKILLLDEA 1247
Cdd:COG4608 123 RIH---GLASKaeRRERVAELLELvglrpEHADRY----P-----------HEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1248 TSALDSeSERA--------VQEALdrareGRTCITIAHRLSSIQnsdlivYIDD-------GRVQESGTHKELMQ 1307
Cdd:COG4608 185 VSALDV-SIQAqvlnlledLQDEL-----GLTYLFISHDLSVVR------HISDrvavmylGKIVEIAPRDELYA 247
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
429-640 |
1.85e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 117.91 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 429 RKEAKV--LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLRNVVGIVQQ--- 500
Cdd:COG4608 26 RTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQdpy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 501 --------------EPILfndtIHNNLlfgnPDATRETmiRVCKMANA----HDFIKKMPKgydtqigdggvQLSGGQKQ 562
Cdd:COG4608 106 aslnprmtvgdiiaEPLR----IHGLA----SKAERRE--RVAELLELvglrPEHADRYPH-----------EFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 563 RVAIARTLIRDPKVLLLDEATSALD----AQsesVV------QSALnnaskGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKI 236
|
....*....
gi 1678196980 632 VEAGNHEEL 640
Cdd:COG4608 237 VEIAPRDEL 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
417-675 |
1.94e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRK--EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIdGVDV-----RDLNLE 489
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 490 WLRNVVGIVQQ--EPILFNDTIHNNLLFG--NPDATREtmirvckmaNAHDFIKKMPK--GYDTQIGDGG-VQLSGGQKQ 562
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEE---------DAKQKAREMIElvGLPEELLARSpFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 563 RVAIARTLIRDPKVLLLDEATSALD--AQSESVVQSALNNASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAG---- 635
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDpkGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGtpre 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1678196980 636 ---NHEELVNLGgryFDLVKAQAFKQdpdeiALEKEEEDQFDE 675
Cdd:PRK13634 233 ifaDPDELEAIG---LDLPETVKFKR-----ALEEKFGISFPK 267
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
434-642 |
2.40e-28 |
|
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: 114.74 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwLRNVvGIVQQEPILF-NDTIHNN 512
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRDI-SYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFG-----NPDATRETMIR-VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:cd03299 92 IAYGlkkrkVDKKEIERKVLeIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 587 DAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:cd03299 161 DVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1082-1300 |
3.17e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.99 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPqrPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS---LYHLRT 1158
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 QMALVGQEPRLFVG-TIRENVCLGL------KDVPLEKINQALE---LAN-ANRFlgnlPDgidtevgerggQLSGGQKQ 1227
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALPLrvtgksRKEIRRRVREVLDlvgLSDkAKAL----PH-----------ELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 1228 RIAIARALVRDPKILLLDEATSALDSESERAVQEALDRA-REGRTCItIA-HRLSSIQNSDL-IVYIDDGRVQESG 1300
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVL-IAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
418-642 |
3.45e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYPT-RKEAkvlnglNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlewlrnvvg 496
Cdd:COG3840 3 RLDDLTYRYGDfPLRF------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 iVQQEP--ILFND-------TIHNNLLFG-NPD-----ATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQK 561
Cdd:COG3840 68 -PAERPvsMLFQEnnlfphlTVAQNIGLGlRPGlkltaEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 562 QRVAIARTLIRDPKVLLLDEATSALDAqsesvvqsALN----------NASKGRTTIMIAHRLS-TIREADKIVFFEKGV 630
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDP--------ALRqemldlvdelCRERGLTVLMVTHDPEdAARIADRVLLVADGR 207
|
250
....*....|..
gi 1678196980 631 IVEAGNHEELVN 642
Cdd:COG3840 208 IAADGPTAALLD 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
417-640 |
3.67e-28 |
|
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: 114.36 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPtrkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwLRNVvG 496
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNV-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFND-TIHNNLLFG----------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVA 565
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1082-1301 |
4.11e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.21 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQ-PVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDIKNIS---LY 1154
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSekeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1155 HLRTQMALVGQEPRLFVG-TIRENVCLglkdvplekinqALELANANRflgnlpDGIDTEVGE---RGG----------Q 1220
Cdd:PRK11153 79 KARRQIGMIFQHFNLLSSrTVFDNVAL------------PLELAGTPK------AEIKARVTElleLVGlsdkadrypaQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1221 LSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEAL-DRARE-GRTCITIAHRLSSI-QNSDLIVYIDDGRVQ 1297
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkDINRElGLTIVLITHEMDVVkRICDRVAVIDAGRLV 220
|
....
gi 1678196980 1298 ESGT 1301
Cdd:PRK11153 221 EQGT 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
417-635 |
5.94e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 112.26 E-value: 5.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHF---RYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLT--RLYEPEQGSVQIDGvdvRDLNLEWL 491
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING---RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQEPILF-NDTIhnnllfgnpdatRETMirvckmanahDFIKKMpKGydtqigdggvqLSGGQKQRVAIARTL 570
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTV------------RETL----------MFAAKL-RG-----------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 571 IRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLST--IREADKIVFFEKGVIVEAG 635
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
419-640 |
8.73e-28 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 113.55 E-value: 8.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 419 FENVHFRYPTRKeaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN----LEWLRNV 494
Cdd:TIGR02315 4 VENLSKVYPNGK--QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLLFGNPDATreTMIRVC-KMANAHDFIKKMP-------KGYDTQIGDggvQLSGGQKQRVAI 566
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYK--PTWRSLlGRFSEEDKERALSalervglADKAYQRAD---QLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKriNKEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSEL 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1109-1305 |
9.80e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.33 E-value: 9.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKST---CIGMLErfyDVTGGALRMDGQDIKnislyHLRTQ---MALVGQEPRLFVG-TIRENVCLG 1181
Cdd:COG3839 28 DGEFLVLLGPSGCGKSTllrMIAGLE---DPTSGEILIGGRDVT-----DLPPKdrnIAMVFQSYALYPHmTVYENIAFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1182 LK--DVPLEKINQA-------LELANanrFLGNLPdgidtevgergGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:COG3839 100 LKlrKVPKAEIDRRvreaaelLGLED---LLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1253 SE------SE-RAVQEALdrareGRTCI----------TIAHRlssiqnsdlIVYIDDGRVQESGTHKEL 1305
Cdd:COG3839 166 AKlrvemrAEiKRLHRRL-----GTTTIyvthdqveamTLADR---------IAVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
417-642 |
1.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.93 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN-LEWLRNVV 495
Cdd:PRK13644 2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 GIVQQEP--ILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIA 567
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGpenlclPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQS-ESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
434-640 |
1.38e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.92 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDV---RDLN-----LEWLRNVVGIVQQEpilF 505
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQN---F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 506 NDTIHNNLLfgnpdatrETMIRvckmanAHDFIKKMPKGYDTQ--------IGDGGVQ------LSGGQKQRVAIARTLI 571
Cdd:PRK11264 95 NLFPHRTVL--------ENIIE------GPVIVKGEPKEEATArarellakVGLAGKEtsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 572 RDPKVLLLDEATSALDAQsesVVQSALNN----ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK11264 161 MRPEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
420-635 |
1.38e-27 |
|
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: 111.90 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSvALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDlNLEWLRNVVGIVQ 499
Cdd:cd03264 4 ENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEPILF-NDTI-----HNNLLFGNPDAT-RETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIR 572
Cdd:cd03264 79 QEFGVYpNFTVrefldYIAWLKGIPSKEvKARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1108-1300 |
1.58e-27 |
|
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: 111.62 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1108 LRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDI----KNISLYHLRTQMALVGQEPRLFVG-TIRENVC 1179
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTllrCIAGLEK---PDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 LGLKdvpleKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAV 1259
Cdd:cd03297 98 FGLK-----RKRNREDRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678196980 1260 QEALDR--AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:cd03297 171 LPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
417-611 |
2.06e-27 |
|
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: 111.35 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLRN 493
Cdd:cd03292 1 IEFINVTKTYPNGTAA--LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQE-PILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAI 566
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIA 611
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1082-1300 |
2.33e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 111.05 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPqrpHQPVMKQLQWTalRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKniSLYHLRTQMA 1161
Cdd:cd03298 1 VRLDKIRFSYG---EQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVG-TIRENVCLGLkdVPLEKIN----QALELANANRflgnlpdGIDTEVGERGGQLSGGQKQRIAIARALV 1236
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGL--SPGLKLTaedrQAIEVALARV-------GLAGLEKRLPGELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1237 RDPKILLLDEATSALDSESERAVQEALD--RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLdlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
417-676 |
2.34e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.29 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEP--ILFNDTIHNNLLFG--NPDATRETMI-RV---CKMANAHDFIKKMPkgydtqigdggVQLSGGQKQRVAIAR 568
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGleNKGIPHEEMKeRVneaLELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 569 TLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLGGR 646
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1678196980 647 YFDL--------VKAQAFKQD----PDEIALEKEEEDQFDEF 676
Cdd:PRK13650 234 LLQLgldipfttSLVQSLRQNgydlPEGYLTEKELEEQLWEL 275
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1091-1305 |
2.89e-27 |
|
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: 111.06 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1091 YPQRPHqPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLerfydvtGGALRMDGQDIKnISLYHLRTQMALVGQE---- 1166
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML-------TGELRPTSGTAY-INGYSIRTDRKAARQSlgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1167 PR---LFVG-TIRENV--CLGLKDVPLEKINQALELAnanRFLGNLPDGIDTEVGerggQLSGGQKQRIAIARALVRDPK 1240
Cdd:cd03263 81 PQfdaLFDElTVREHLrfYARLKGLPKSEIKEEVELL---LRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 1241 ILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1109-1304 |
3.07e-27 |
|
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: 111.66 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlyHLRTQMALVGQEPRLFVG-TIRENVCLGLKDVPL 1187
Cdd:cd03299 24 RGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDISYVPQNYALFPHmTVYKNIAYGLKKRKV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1188 EKINQALELANANRFLGnlpdgIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAR 1267
Cdd:cd03299 102 DKKEIERKVLEIAEMLG-----IDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 1268 E--GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKE 1304
Cdd:cd03299 177 KefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1109-1307 |
3.42e-27 |
|
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: 110.99 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLyHLRTQM--ALVGQEPRLFVG-TIRENVCLGLKDV 1185
Cdd:cd03224 25 EGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-HERARAgiGYVPEGRRIFPElTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1186 PLEKINQALElananRFLGNLPDgIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR 1265
Cdd:cd03224 104 RRAKRKARLE-----RVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678196980 1266 AREGRTCITI----AHRLSSIqnSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:cd03224 178 LRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
416-673 |
3.99e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.95 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 416 KVTFENVHFRYP--TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDV----RDLNLE 489
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 490 WLRNVVGIVQQ--EPILFNDTIHNNLLFGnPDATRETMIRVckMANAHDFIkkMPKGYDTQI-GDGGVQLSGGQKQRVAI 566
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEV--KNYAHRLL--MDLGFSRDVmSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEELVNL 643
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
250 260 270
....*....|....*....|....*....|
gi 1678196980 644 GGRYFDLVKAQafkqdPDEIALEKEEEDQF 673
Cdd:PRK13646 237 KKKLADWHIGL-----PEIVQLQYDFEQKY 261
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
417-623 |
3.99e-27 |
|
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: 110.26 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVvG 496
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFND-TIHNNLLF----GNPDATRETmirvckmanAHDFIKKM-PKGY-DTQIGdggvQLSGGQKQRVAIART 569
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaalYGLRADREA---------IDEALEAVgLAGLaDLPVR----QLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIREADKI 623
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
420-624 |
5.70e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.57 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:PRK10247 11 QNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEPILFNDTIHNNLLFgnPDATRETMIRVCKMAnahDFIKKMpkGYDTQIGDGGV-QLSGGQKQRVAIARTLIRDPKVLL 578
Cdd:PRK10247 88 QTPTLFGDTVYDNLIF--PWQIRNQQPDPAIFL---DDLERF--ALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678196980 579 LDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIREADKIV 624
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHryVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
93-365 |
1.39e-26 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 111.36 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQPVLAIISGRMTNVLlvidplskeFKTKTMENVYI--FLGLGIFV--SINDFCQYMCFQRVCSRMM 168
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDI---------FVEKDLEALLLvpLAIIGLFLlrGLASYLQTYLMAYVGQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 169 TVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPV 248
Cdd:cd18552 72 RDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 249 STICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIwggfwSGFFGGIFFF 328
Cdd:cd18552 152 AALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM-----KIARARALSS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1678196980 329 WLMAFMG----CGIL-YGGYLLKVGIIkSPGDVFIIVVAMLL 365
Cdd:cd18552 227 PLMELLGaiaiALVLwYGGYQVISGEL-TPGEFISFITALLL 267
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
415-641 |
1.41e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 118.73 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYptRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTSvgLLT--RLYEPEQGSVQIDGVDVRDLNLEWL 491
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTL--LLTfmRMVEVCGGEIRVNGREIGAYGLREL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQEPILFNDTIHNNLlfgNP--DATRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIART 569
Cdd:PTZ00243 1383 RRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 570 LI-RDPKVLLLDEATS----ALDAQSESVVQSALNNaskgRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELV 641
Cdd:PTZ00243 1460 LLkKGSGFILMDEATAnidpALDRQIQATVMSAFSA----YTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1096-1304 |
1.47e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.12 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1096 HQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISL--YHLRTqmalVGQEPRLFVG- 1172
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAenRHVNT----VFQSYALFPHm 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1173 TIRENVCLGLK--DVPLEKIN----QALELAN----ANRflgnlpdgidtevgeRGGQLSGGQKQRIAIARALVRDPKIL 1242
Cdd:PRK09452 102 TVFENVAFGLRmqKTPAAEITprvmEALRMVQleefAQR---------------KPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1243 LLDEATSALDSESERAVQEALDR-ARE-GRTCITIAH-RLSSIQNSDLIVYIDDGRVQESGTHKE 1304
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKAlQRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1084-1276 |
1.71e-26 |
|
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: 108.34 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKnISLYHLRTQMALV 1163
Cdd:COG4133 5 AENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPRLFVG-TIRENVCL--GLK--DVPLEKINQALELananrfLGnLPDGIDTEVGerggQLSGGQKQRIAIARALVRD 1238
Cdd:COG4133 81 GHADGLKPElTVRENLRFwaALYglRADREAIDEALEA------VG-LAGLADLPVR----QLSAGQKRRVALARLLLSP 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALDRAREGRTCITIA 1276
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1109-1307 |
1.71e-26 |
|
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: 115.55 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTcIGM----LERfydvTGGALRMDGQDIKNIS---LYHLRTQMALVGQEP------RLFVG-TI 1174
Cdd:COG4172 311 RGETLGLVGESGSGKST-LGLallrLIP----SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPfgslspRMTVGqII 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1175 RENvcLGLKDVPL------EKINQALELAnanrflgnlpdGIDTEVGER-GGQLSGGQKQRIAIARALVRDPKILLLDEA 1247
Cdd:COG4172 386 AEG--LRVHGPGLsaaerrARVAEALEEV-----------GLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1248 TSALDseseRAVQ-EALD-----RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:COG4172 453 TSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
433-643 |
1.74e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN-LEWLRNVVGIVQQEPILFND-TIH 510
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 511 NNLLFGNPdATRETMIRVCKM-ANAHDFIKKM-----PkgyDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATS 584
Cdd:COG1129 98 ENIFLGRE-PRRGGLIDWRAMrRRARELLARLgldidP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 585 ALDAqSES-----VVQSaLnnASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG-----NHEELVNL 643
Cdd:COG1129 170 SLTE-REVerlfrIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
426-640 |
1.87e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.87 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 426 YPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYE--PE---QGSVQIDGVDV---RDLNLEwLRNVVGI 497
Cdd:PRK14239 14 YYNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIyspRTDTVD-LRKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VQQEPILFNDTIHNNLLFG-------NPDATRETMIRVCKMANAHDFIKKmpKGYDTQIGdggvqLSGGQKQRVAIARTL 570
Cdd:PRK14239 91 VFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 571 IRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
417-629 |
1.95e-26 |
|
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: 108.75 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDlNLEWLRNVVG 496
Cdd:cd03263 1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFND-TIHNNLLF-----GNPDATR----ETMIRVCKManaHDFIKKMPKgydtqigdggvQLSGGQKQRVAI 566
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIkeevELLLRVLGL---TDKANKRAR-----------TLSGGMKRKLSL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHrlsTIREA----DKIVFFEKG 629
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAealcDRIAIMSDG 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
434-643 |
3.09e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.35 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwlRNVVGIVQQEPILF-NDTIHNN 512
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFG-----NPDAtrETMIRV---CKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATS 584
Cdd:PRK09452 107 VAFGlrmqkTPAA--EITPRVmeaLRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 585 ALDAQSESVVQSALNNASK--GRTTIMIAHRLstiREA----DKIVFFEKGVIVEAGN----HEELVNL 643
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRklGITFVFVTHDQ---EEAltmsDRIVVMRDGRIEQDGTpreiYEEPKNL 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
417-644 |
4.14e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEP--ILFNDTIHNNLLFG--NPDATRETMIR-VCKMANAHDFIKKmpKGYDTQigdggvQLSGGQKQRVAIARTLI 571
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGleNHAVPYDEMHRrVSEALKQVDMLER--ADYEPN------ALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNLG 644
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
434-1306 |
4.61e-26 |
|
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: 116.93 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVdvrdlnlewlrnvVGIVQQEPILFNDTIHNNL 513
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 514 LFG-NPDATRET-MIRVCKManaHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSE 591
Cdd:TIGR01271 508 IFGlSYDEYRYTsVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 592 -SVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVN---------LGGRYFDLVKA-------- 653
Cdd:TIGR01271 585 kEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAkrpdfssllLGLEAFDNFSAerrnsilt 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 654 ----------------------QAFKQDPDEIALEK----------------------------EEEDQFDEfdkptVFN 683
Cdd:TIGR01271 665 etlrrvsidgdstvfsgpetikQSFKQPPPEFAEKRkqsiilnpiasarkfsfvqmgpqkaqatTIEDAVRE-----PSE 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 684 RKVSV------------RNSRSSGRSGSEEFRRGSL------ANHSFDR-------FRKASHIPSAEDEAFALRV-KETM 737
Cdd:TIGR01271 740 RKFSLvpedeqgeeslpRGNQYHHGLQHQAQRRQSVlqlmthSNRGENRreqlqtsFRKKSSITQQNELASELDIySRRL 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 738 EKDG--EITAG---------FLDIFKNAQGNYT------YMLIGLSAALIRGLDLPTFA------LLFAWVFEGFEFVPY 794
Cdd:TIGR01271 820 SKDSvyEISEEineedlkecFADERENVFETTTwntylrYITTNRNLVFVLIFCLVIFLaevaasLLGLWLITDNPSAPN 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 795 GGKMMHRLAMS--------------------VIAHCAAGLGIWFFQTLSTVMFAI-VSENLGVRFRVAAFRNLLyqdAAY 853
Cdd:TIGR01271 900 YVDQQHANASSpdvqkpviitptsayyifyiYVGTADSVLALGFFRGLPLVHTLLtVSKRLHEQMLHSVLQAPM---AVL 976
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 854 fdNPAHApGSLITRLAADppcvKAVVDGRMMQVVYATAAVIACV--TIGFINCWQVAILGTALIFLLGFIMAGLAFKISI 931
Cdd:TIGR01271 977 --NTMKA-GRILNRFTKD----MAIIDDMLPLTLFDFIQLTLIVlgAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTS 1049
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 932 VAAEHMENDDAGKIAIEIIENVK---TIQLLTRTRRFLNSYeneskkrkrtelrksvYEAVNYCISQNFMYYMSCFCFAL 1008
Cdd:TIGR01271 1050 QQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLF----------------HKALNLHTANWFLYLSTLRWFQM 1113
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1009 AIRII----------------NQGDQTVDKTFRCLMAMMLCCEGIIMSAqffPQFVGAKSAAGQMFNLINRQPQTGDLKS 1072
Cdd:TIGR01271 1114 RIDIIfvfffiavtfiaigtnQDGEGEVGIILTLAMNILSTLQWAVNSS---IDVDGLMRSVSRVFKFIDLPQEEPRPSG 1190
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1073 GTKPEIRGNIL-FEN--VKFSYPQRPH--------------QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYD 1135
Cdd:TIGR01271 1191 GGGKYQLSTVLvIENphAQKCWPSGGQmdvqgltakyteagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS 1270
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1136 vTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENV--CLGLKDVPLEKINQALELANAnrfLGNLPDGIDTE 1213
Cdd:TIGR01271 1271 -TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdpYEQWSDEEIWKVAEEVGLKSV---IEQFPDKLDFV 1346
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1214 VGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDD 1293
Cdd:TIGR01271 1347 LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEG 1426
|
1050
....*....|...
gi 1678196980 1294 GRVQESGTHKELM 1306
Cdd:TIGR01271 1427 SSVKQYDSIQKLL 1439
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
434-638 |
6.04e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDG--------VDVRDLNLewLRNVVGIVQQE---- 501
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRL--LRQKVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 502 PILfndTIHNNLLfgnpdatrETMIRVCKMANAHDFIKKMPKGYDTQIGDGG----VQLSGGQKQRVAIARTLIRDPKVL 577
Cdd:COG4161 95 PHL---TVMENLI--------EAPCKVLGLSKEQAREKAMKLLARLRLTDKAdrfpLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 578 LLDEATSALDAQSESVVQSALNNASK-GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHE 638
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
417-640 |
6.07e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.02 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAK---VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEW-LR 492
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 493 NVVGIVQQEP--ILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRV 564
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 565 AIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
420-640 |
6.51e-26 |
|
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: 107.13 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwLRNVVGI-- 497
Cdd:cd03224 4 ENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VQQEPILFND-TIHNNLLFG----NPDATRETMIRVCKManahdFikkmPKGYDTQIGDGGvQLSGGQKQRVAIARTLIR 572
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGayarRRAKRKARLERVYEL-----F----PRLKERRKQLAG-TLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 573 DPKVLLLDEATSALdaqSESVVQ---SALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:cd03224 150 RPKLLLLDEPSEGL---APKIVEeifEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1109-1301 |
8.29e-26 |
|
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: 107.52 E-value: 8.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLyHLRTQMALVG--QEPRLFVG-TIRENVCLGL--- 1182
Cdd:cd03219 25 PGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIARLGIGRtfQIPRLFPElTVLENVMVAAqar 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 ----------KDVPLEKINQALELAnanRFLGnLPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:cd03219 104 tgsglllaraRREEREARERAEELL---ERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1253 SESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGT 1301
Cdd:cd03219 176 PEETEELAELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1085-1300 |
9.66e-26 |
|
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: 106.57 E-value: 9.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHlrTQMALVG 1164
Cdd:cd03301 4 ENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEPRLFVG-TIRENVCLGLK--DVPLEKINQALElaNANRFLGnlpdgIDTEVGERGGQLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03301 79 QNYALYPHmTVYDNIAFGLKlrKVPKDEIDERVR--EVAELLQ-----IEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1242 LLLDEATSALDSESERAVQEALDR--AREGRTCITIAH-RLSSIQNSDLIVYIDDGRVQESG 1300
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1082-1278 |
1.19e-25 |
|
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: 104.54 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMdgqdiknislyHLRTQMA 1161
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVGTIRENVCLGLKDVplekinqalelananrflgnlpdgidtevgerggqLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678196980 1242 LLLDEATSALDSESERAVQEALDraREGRTCITIAHR 1278
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
415-642 |
1.38e-25 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 108.02 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYpTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEqGSVQIDGVDVRDLNLEWLRNV 494
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQEPILFNDTIHNNLlfgNPDA--TRETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIR 572
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
418-668 |
1.40e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYPTRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwlRNVVg 496
Cdd:COG4525 5 TVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--RGVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 iVQQEPILFNDTIHNNLLF-----GNPDATREtmirvckmANAHDFIKKMpkGYDTQIGDGGVQLSGGQKQRVAIARTLI 571
Cdd:COG4525 82 -FQKDALLPWLNVLDNVAFglrlrGVPKAERR--------ARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHrlsTIREAdkiVFFEKGVIVEAGN-----HEELVNLG 644
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH---SVEEA---LFLATRLVVMSPGpgrivERLELDFS 224
|
250 260
....*....|....*....|....
gi 1678196980 645 GRYFDLVKAQAFKQDPDEIALEKE 668
Cdd:COG4525 225 RRFLAGEDARAIKSDPAFIALREE 248
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
438-635 |
1.42e-25 |
|
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: 106.04 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 438 LNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRdlNLEWLRNVVGIVQQEPILFND-TIHNNLLFG 516
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 517 -NP-----DATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQS 590
Cdd:cd03298 95 lSPglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678196980 591 ESVVQSALNN--ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1085-1296 |
1.71e-25 |
|
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: 105.42 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYpqRPHQPVMKQLQWTALRGQTVALVGPSGSGKST----CIGMLERfydvTGGALRMDGqdiKNISLYHLRTQM 1160
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTlakiLAGLIKE----SSGSILLNG---KPIKAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPR--LFVGTIRENVCLGLKDVP--LEKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALV 1236
Cdd:cd03226 74 GYVMQDVDyqLFTDSVREELLLGLKELDagNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1237 RDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
420-640 |
2.10e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEP--ILFNDTIHNNLLFG--NPDATRETMIRVCKMA----NAHDFIKKMPkgydtqigdggVQLSGGQKQRVAIARTLI 571
Cdd:PRK13642 88 QNPdnQFVGATVEDDVAFGmeNQGIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALNNASKGR--TTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1097-1277 |
2.23e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.92 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALvgQEPRLFVG-TIR 1175
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF--QSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCLGLKDVPLEK------INQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATS 1249
Cdd:PRK11607 110 QNIAFGLKQDKLPKaeiasrVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190
....*....|....*....|....*....|
gi 1678196980 1250 ALDSE-SERAVQEALD-RAREGRTCITIAH 1277
Cdd:PRK11607 179 ALDKKlRDRMQLEVVDiLERVGVTCVMVTH 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
424-640 |
2.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.40 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 424 FRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRD----------------LN 487
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelitnpyskkiKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 488 LEWLRNVVGIVQQEP--ILFNDTIHNNLLFGnPDATRETMIRVCKMANAHdfIKKMPKGYDTqIGDGGVQLSGGQKQRVA 565
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFY--LNKMGLDDSY-LERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSES-VVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1114-1305 |
2.71e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.54 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGMLERFYDV-----TGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVG-TIRENVCLGLKDVPL 1187
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlSIFENVALGLKLNRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1188 --------EKINQALELANanrflgnLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAV 1259
Cdd:PRK14247 113 vkskkelqERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678196980 1260 QEALDRAREGRTCITIAH-RLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK14247 186 ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
444-635 |
2.91e-25 |
|
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: 105.07 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 444 PGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRD----LNLEWLRNVVGIVQQEPILF-NDTIHNNLLFGNP 518
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 519 -DATRETMIRVCKMANAHDFikkmpkgydTQIGDGGV-QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQS 596
Cdd:cd03297 102 rKRNREDRISVDELLDLLGL---------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678196980 597 ALNNASK--GRTTIMIAHRLSTI-READKIVFFEKGVIVEAG 635
Cdd:cd03297 173 ELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
429-633 |
2.93e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 106.81 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 429 RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLE----WLRNVVGIVQQEPIL 504
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrraFRRDVQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 505 FNDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMpkGYDTQIGDG-GVQLSGGQKQRVAIARTLIRDPKVLLLDEAT 583
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMV--GLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 584 SALDAQSESVVQSALN--NASKGRTTIMIAHRLSTI-READKIVFFEKGVIVE 633
Cdd:TIGR02769 179 SNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1114-1306 |
3.06e-25 |
|
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: 109.03 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGM---LERfydVTGGALRMDG---QDI-KNISL-YHLRtQMALVGQEPRLFVG-TIRENVCLGLKD 1184
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlQDSaRGIFLpPHRR-RIGYVFQEARLFPHlSVRGNLLYGRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1185 VPleKINQALELANANRFLGnlpdgIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALD 1264
Cdd:COG4148 105 AP--RAERRISFDEVVELLG-----IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678196980 1265 RAREgRTCITI---AHRLSSIQN-SDLIVYIDDGRVQESGTHKELM 1306
Cdd:COG4148 178 RLRD-ELDIPIlyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
420-640 |
3.18e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 111.70 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRK--------EAKVLNGLNLTVEPGTSVALVGHSGCGKSTsVGL-LTRLyEPEQGSVQIDGVDVRDLN--- 487
Cdd:COG4172 279 RDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKST-LGLaLLRL-IPSEGEIRFDGQDLDGLSrra 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 488 LEWLRNVVGIVQQEPilFN---------DTIHNNLLFGNPDATR-ETMIRVCKM-------ANA-----HDFikkmpkgy 545
Cdd:COG4172 357 LRPLRRRMQVVFQDP--FGslsprmtvgQIIAEGLRVHGPGLSAaERRARVAEAleevgldPAArhrypHEF-------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 546 dtqigdggvqlSGGQKQRVAIARTLIRDPKVLLLDEATSALD----AQsesVVQ--SALnNASKGRTTIMIAHRLSTIRE 619
Cdd:COG4172 427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQ---ILDllRDL-QREHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|..
gi 1678196980 620 -ADKIVFFEKGVIVEAGNHEEL 640
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1082-1296 |
5.22e-25 |
|
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: 104.41 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPqrPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNI---SLYHLRT 1158
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 QMALVGQEPRLFVG-TIRENVCLGL-------KDVPlEKINQALELAnanrflgnlpdGIDTEVGERGGQLSGGQKQRIA 1230
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevtgvppREIR-KRVPAALELV-----------GLSHKHRALPAELSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1231 IARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQN--SDLIVYIDDGRV 1296
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
911-1317 |
5.27e-25 |
|
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: 113.50 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 911 GTALIFLLGFIMAGLAFKISIVAAEHMENDDAG-KIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTeLRKSVYEAV 989
Cdd:TIGR00957 463 GVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRiKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKV-LKKSAYLHA 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 990 nyciSQNFMYYMSCFCFAL---AIRIINQGDQTVD--KTFRCLMAMMLCCEGIIMSAQFFPQFVGAKSAAGQMFNLINRQ 1064
Cdd:TIGR00957 542 ----VGTFTWVCTPFLVALitfAVYVTVDENNILDaeKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1065 ---PQTGDLKSgTKPEIRGNILFENVKFSYpQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGAL 1141
Cdd:TIGR00957 618 elePDSIERRT-IKPGEGNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1142 RMDGQdiknislyhlrtqMALVGQEPRLFVGTIRENVCLGlKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQL 1221
Cdd:TIGR00957 696 HMKGS-------------VAYVPQQAWIQNDSLRENILFG-KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNL 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1222 SGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEAL---DRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQE 1298
Cdd:TIGR00957 762 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
410
....*....|....*....
gi 1678196980 1299 SGTHKELMQLKGKYFELIK 1317
Cdd:TIGR00957 842 MGSYQELLQRDGAFAEFLR 860
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
91-375 |
6.12e-25 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 106.36 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIGLITSVISgVSQPVLAiisGRmtnvllVIDPLSKefKTKTMENVYIFLGLGIFVSI-NDFCQYMcFQRVCSRMMT 169
Cdd:cd18551 3 LALLLSLLGTAAS-LAQPLLV---KN------LIDALSA--GGSSGGLLALLVALFLLQAVlSALSSYL-LGRTGERVVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 170 VMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVS 249
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 250 TICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIFFFW 329
Cdd:cd18551 150 FLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1678196980 330 LMAFMGCGILYGGYLLKVGIIkSPGDvfiiVVAMLLgaYFLGLISP 375
Cdd:cd18551 230 VQLALLVVLGVGGARVASGAL-TVGT----LVAFLL--YLFQLITP 268
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1114-1305 |
6.39e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.24 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGMLERFYDV-----TGGALRMDGQDI--KNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKdVP 1186
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLR-LK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 LEKINQALELANANRFLG-NLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR 1265
Cdd:PRK14239 114 GIKDKQVLDEAVEKSLKGaSIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678196980 1266 AREGRTCITIAHRL---SSIqnSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK14239 194 LKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1109-1305 |
6.74e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 107.06 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKST---CIGMLERFYDVTGGALRMDGQDIKNIS---LYHLR-TQMALVGQE------PRLfvgTIR 1175
Cdd:COG0444 30 RGETLGLVGESGSGKSTlarAILGLLPPPGITSGEILFDGEDLLKLSekeLRKIRgREIQMIFQDpmtslnPVM---TVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCLGL-------KDVPLEKINQALE---LANANRFLGNLPdgidtevgergGQLSGGQKQRIAIARALVRDPKILLLD 1245
Cdd:COG0444 107 DQIAEPLrihgglsKAEARERAIELLErvgLPDPERRLDRYP-----------HELSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1246 EATSALDSeSERAvqEALD-----RAREGRTCITIAHRLSsiqnsdLIVYIDD-------GRVQESGTHKEL 1305
Cdd:COG0444 176 EPTTALDV-TIQA--QILNllkdlQRELGLAILFITHDLG------VVAEIADrvavmyaGRIVEEGPVEEL 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1109-1298 |
7.39e-25 |
|
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: 104.44 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGM---LERfydVTGGALRMDGQDIKNIS---LYHLRTQ-MALVGQE----PRLfvgTIREN 1177
Cdd:COG4181 37 AGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedaRARLRARhVGFVFQSfqllPTL---TALEN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1178 VCLglkdvPLEKINQALELANANRFLGnlpdgidtEVG--ERG----GQLSGGQKQRIAIARALVRDPKILLLDEATSAL 1251
Cdd:COG4181 111 VML-----PLELAGRRDARARARALLE--------RVGlgHRLdhypAQLSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678196980 1252 DSESERAVQEAL-DRARE-GRTCITIAHRLSSIQNSDLIVYIDDGRVQE 1298
Cdd:COG4181 178 DAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
761-1032 |
8.21e-25 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 105.80 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 761 MLIGLSAALIRGLDLPTFALLFAWVFEGFEfvpyGGKMMHRLAMSVIAHCAAGLGI--WFFQTLSTVMFAIVSENLGVRF 838
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLL----PDGDPETQALNVYSLALLLLGLaqFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 839 RVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFINCWQVAILGTALIFLL 918
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 919 GFIMAGLAFKISIVAAEHME-NDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELRKSVYEAVNYCISQNF 997
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKaVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 1678196980 998 MYYMSCFCFALAIRIINQGDQTVDK--TFRCLMAMML 1032
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLF 271
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
420-634 |
9.57e-25 |
|
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: 104.05 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKEA-KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN----LEWLRNV 494
Cdd:COG4181 12 RGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLRARH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VGIVQQ-EPILFNDTIHNNL-----LFGNPDAtretmirvckMANAHDFIKKM---------PKgydtqigdggvQLSGG 559
Cdd:COG4181 92 VGFVFQsFQLLPTLTALENVmlpleLAGRRDA----------RARARALLERVglghrldhyPA-----------QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 560 QKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEA 634
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
437-589 |
1.10e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.33 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 437 GLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPE---QGSVQIDGVDVRDLNLEwLRNVvGIVQQEPILF-NDTIHNN 512
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE-QRRI-GILFQDDLLFpHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFGNPDAT-----RETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:COG4136 97 LAFALPPTIgraqrRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
..
gi 1678196980 588 AQ 589
Cdd:COG4136 166 AA 167
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1082-1323 |
1.48e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFY---DVTGGALRMDGQDIKNISLYHLRT 1158
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1159 QMALVGQEP-RLFVG-TIRENVCLGLKD--VPLEK----INQALELANanrflgnLPDGIDTEvgerGGQLSGGQKQRIA 1230
Cdd:PRK13640 85 KVGIVFQNPdNQFVGaTVGDDVAFGLENraVPRPEmikiVRDVLADVG-------MLDYIDSE----PANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1231 IARALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMql 1308
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF-- 231
|
250
....*....|....*
gi 1678196980 1309 kgKYFELIKKQDLAI 1323
Cdd:PRK13640 232 --SKVEMLKEIGLDI 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
421-640 |
1.63e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 421 NVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDG--VDVRDLNLEWLRNVVGIV 498
Cdd:PRK13639 6 DLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEP--ILFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTL 570
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 571 IRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIA-HRLSTI-READKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1113-1306 |
1.89e-24 |
|
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: 106.73 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1113 VALVGPSGSGKST---CIGMLERFYdvtGGALRMDGQDI----KNISLYHLRTQMALVGQEPRLFVG-TIRENVCLGLK- 1183
Cdd:TIGR02142 26 TAIFGRSGSGKTTlirLIAGLTRPD---EGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHlSVRGNLRYGMKr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1184 -DVPLEKINQA--LELANANRFLGNLPdgidtevgergGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQ 1260
Cdd:TIGR02142 103 aRPSERRISFErvIELLGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678196980 1261 EALDRARE--GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELM 1306
Cdd:TIGR02142 172 PYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1109-1301 |
2.38e-24 |
|
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: 103.97 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLyHLRTQMALV--GQEPRLFVG-TIRENVCLG---- 1181
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIArtFQNPRLFPElTVLENVLVAahar 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1182 --------LKDVPLEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSAL-D 1252
Cdd:COG0411 108 lgrgllaaLLRLPRARREEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLnP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1253 SESERAVQ--EALdRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGT 1301
Cdd:COG0411 186 EETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
417-642 |
3.51e-24 |
|
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: 103.24 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEP-EQGSVQI-----DGVDVRDLnlew 490
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLfgerrGGEDVWEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 lRNVVGIV---QQEPILFNDTIHNNLL---------FGNPDAT-RETMIRVCKMANAHDFIkkmpkgyDTQIGdggvQLS 557
Cdd:COG1119 77 -RKRIGLVspaLQLRFPRDETVLDVVLsgffdsiglYREPTDEqRERARELLELLGLAHLA-------DRPFG----TLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 558 GGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLSTIREA-DKIVFFEKGVIVEA 634
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
....*...
gi 1678196980 635 GNHEELVN 642
Cdd:COG1119 225 GPKEEVLT 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
410-642 |
3.63e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.58 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 410 IEKVVGKVTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPE-----QGSVQIDGVDV- 483
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 484 -RDLNLEWLRNVVGIVQQEPILFNDTIHNNLLFG------NPDATRETMIR-VCKMANAHDFIKKmpkgydtQIGDGGVQ 555
Cdd:PRK14258 78 eRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVEsALKDADLWDEIKH-------KIHKSALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 556 LSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNAS--KGRTTIMIAHRLSTI-READKIVFFEK---- 628
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVsRLSDFTAFFKGnenr 230
|
250
....*....|....*
gi 1678196980 629 -GVIVEAGNHEELVN 642
Cdd:PRK14258 231 iGQLVEFGLTKKIFN 245
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1085-1300 |
4.05e-24 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 101.89 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPqrpHQPVMKQLQWTALRGQTvALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNiSLYHLRTQMALVG 1164
Cdd:cd03264 4 ENLTKRYG---KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEPRLFVG-TIRENV--CLGLKDVP----LEKINQALELANANrflgnlpdgidTEVGERGGQLSGGQKQRIAIARALVR 1237
Cdd:cd03264 79 QEFGVYPNfTVREFLdyIAWLKGIPskevKARVDEVLELVNLG-----------DRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1238 DPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNS-DLIVYIDDGRVQESG 1300
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1082-1305 |
4.53e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.29 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYpQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:PRK13648 8 IVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEP-RLFVGTI-RENVCLGLKD--VPLEK----INQALELANanrflgnLPDGIDTEvgerGGQLSGGQKQRIAIAR 1233
Cdd:PRK13648 87 IVFQNPdNQFVGSIvKYDVAFGLENhaVPYDEmhrrVSEALKQVD-------MLERADYE----PNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDRAREGR--TCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
417-640 |
6.28e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYP--TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVR----DLNLEW 490
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 LRNVVGIVQQ--EPILFNDTIHNNLLFG--NPDATRETmirvcKMANAHDFIKKMpkGYDTQIGDGG-VQLSGGQKQRVA 565
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDE-----AKEKALKWLKKV--GLSEDLISKSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQS-ESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1097-1305 |
6.30e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.52 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKST---CIGMLE-------RFYDVTGGALRMDGQDIKNISlyHLRTQMALVGQE 1166
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEqpeagtiRVGDITIDTARSLSQQKGLIR--QLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1167 PRLFVG-TIRENVCLGLKDVPLEKINQALELANAnrflgnlpdgIDTEVGERGGQ------LSGGQKQRIAIARALVRDP 1239
Cdd:PRK11264 94 FNLFPHrTVLENIIEGPVIVKGEPKEEATARARE----------LLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1240 KILLLDEATSALDSEserAVQEALDR----AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK11264 164 EVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
96-313 |
6.85e-24 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 103.48 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 96 GLITSVISGVSQPVLAIISGRMTNVllvIDPLSKEFKTKTMENVY--------IFLGLGIFVSINDFCQYMCFQRVCSRM 167
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDA---VTNHSGSGGEEALRALNqavlillgVVLIGSIATFLRSWLFTLAGERVVARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 168 mtvmRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIP 247
Cdd:cd18780 78 ----RKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 248 VSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNS----GKKHAI 313
Cdd:cd18780 154 PLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINEsyllGKKLAR 223
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
96-372 |
7.13e-24 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 103.33 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 96 GLITSVISGVSQPVLAIISGRMTNVLLVidplskeFKTKTMENVYIFLGLGIFV--SINDFCQYMCFQRVCSRMMTVMRN 173
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALG-------GGDTASLNQIALLLLGLFLlqAVFSFFRIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 174 RYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICM 253
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 254 TLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIwggfwsgfFGGIFFFWLMAF 333
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLAL--------KRARIRALFSSF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1678196980 334 MG-------CGIL-YGGYLLKVGIIkSPGDVF-IIVVAMLLGAYFLGL 372
Cdd:cd18576 226 IIfllfgaiVAVLwYGGRLVLAGEL-TAGDLVaFLLYTLFIAGSIGSL 272
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
417-635 |
9.98e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.52 E-value: 9.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYP--TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDV----RDLNLEW 490
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 LRNVVGIVQQ--EPILFNDTIHNNLLFG-------NPDATRETMIRVCKMANAHDFIKKMPkgydtqigdggVQLSGGQK 561
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqnfgvsQEEAEALAREKLALVGISESLFEKNP-----------FELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 562 QRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK-GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
420-658 |
1.15e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTrkeAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDG--------VDVRDLNLewL 491
Cdd:PRK11124 6 NGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQE----PILfndTIHNNLLfgnpdatrETMIRVCKMANAH---------------DFIKKMPkgydtqigdg 552
Cdd:PRK11124 81 RRNVGMVFQQynlwPHL---TVQQNLI--------EAPCRVLGLSKDQalaraekllerlrlkPYADRFP---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 553 gVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD----AQSESVVQSAlnnASKGRTTIMIAHRLSTIRE-ADKIVFFE 627
Cdd:PRK11124 140 -LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIREL---AETGITQVIVTHEVEVARKtASRVVYME 215
|
250 260 270
....*....|....*....|....*....|.
gi 1678196980 628 KGVIVEAGNHEelvnlggrYFDLVKAQAFKQ 658
Cdd:PRK11124 216 NGHIVEQGDAS--------CFTQPQTEAFKN 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
417-635 |
1.17e-23 |
|
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: 100.52 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRY-PTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNvV 495
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 GIVQQEPILFND-TIHNNLL-FG-----NPDATRETMIRVCKMANAHDFIKKMPKGydtqigdggvqLSGGQKQRVAIAR 568
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyFAglyglKGDELTARLEELADRLGMEELLDRRVGG-----------FSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 569 TLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAG 635
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
418-665 |
1.27e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.70 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwlRNVVgi 497
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--RGVV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VQQEPILFNDTIHNNLLFG-----NPDATRET----MIRVCKMANA-HDFIkkmpkgydtqigdggVQLSGGQKQRVAIA 567
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGlqlagVEKMQRLEiahqMLKKVGLEGAeKRYI---------------WQLSGGQRQRVGIA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHrlsTIREAdkiVFFEKGVIVEAGNHEELV---- 641
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH---DIEEA---VFMATELVLLSPGPGRVVerlp 214
|
250 260
....*....|....*....|....*
gi 1678196980 642 -NLGGRYFDLVKAQAFKQDPDEIAL 665
Cdd:PRK11248 215 lNFARRFVAGESSRSIKSDPQFIAM 239
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1082-1307 |
1.28e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.81 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPqrpHQPVMKQLQwtALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDiknislyHLRTQMA 1161
Cdd:PRK10771 2 LKLTDITWLYH---HLPMRFDLT--VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-------HTTTPPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 -----LVGQEPRLFVG-TIRENVCLGL---------KDVPLEKINQALELANanrFLGNLPdgidtevgergGQLSGGQK 1226
Cdd:PRK10771 70 rrpvsMLFQENNLFSHlTVAQNIGLGLnpglklnaaQREKLHAIARQMGIED---LLARLP-----------GQLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1227 QRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGR--TCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHK 1303
Cdd:PRK10771 136 QRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTD 215
|
....
gi 1678196980 1304 ELMQ 1307
Cdd:PRK10771 216 ELLS 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1082-1300 |
1.82e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMA 1161
Cdd:PRK13647 5 IEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEP--RLFVGTIRENVCLGLKDVPL------EKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIAR 1233
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLdkdeveRRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESG 1300
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1076-1305 |
1.86e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 101.27 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1076 PEIRGNilfeNVKFSYPQrphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTG-----GALRMDGQDI-- 1148
Cdd:PRK14258 6 PAIKVN----NLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIye 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1149 KNISLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDV---PLEKINQALELANANrflGNLPDGIDTEVGERGGQLSGGQ 1225
Cdd:PRK14258 79 RRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrPKLEIDDIVESALKD---ADLWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1226 KQRIAIARALVRDPKILLLDEATSALDSESERAVQEALD--RAREGRTCITIAHRLSSIQN-SDLIVYIDD-----GRVQ 1297
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLV 235
|
....*...
gi 1678196980 1298 ESGTHKEL 1305
Cdd:PRK14258 236 EFGLTKKI 243
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1082-1314 |
1.98e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.29 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCI-GMLERFYDVTGGALRmdgqdiknislyhLRTQM 1160
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVV-------------IRGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPRLFVGTIRENVCLGLKDVPlEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPK 1240
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDP-ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1241 ILLLDEATSALDSESERAV-QEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQlKGKYFE 1314
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NGPLFQ 834
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1095-1289 |
2.25e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1095 PHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGqdiknislyhlRTQMALVGQ---EPRLFV 1171
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1172 GTIRENVCLGL--KDVPLEKINQALELAnANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATS 1249
Cdd:NF040873 72 LTVRDLVAMGRwaRRGLWRRLTRDDRAA-VDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1678196980 1250 ALDSESERAVQEALDR-AREGRTCITIAHRLSSIQNSDLIV 1289
Cdd:NF040873 149 GLDAESRERIIALLAEeHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
433-642 |
2.57e-23 |
|
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: 100.20 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlEWLRNVVGIVQ--QEPILFND-TI 509
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 510 HNNLLFGNPDATRETMIRVCKMANAHDFIKK---------MPKGYDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLD 580
Cdd:cd03219 93 LENVMVAAQARTGSGLLLARARREEREARERaeellervgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 581 EATSAL-DAQSESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKG-VIVEaGNHEELVN 642
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGrVIAE-GTPDEVRN 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1065-1296 |
3.36e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.52 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1065 PQTGDLKSGTKpeirgnILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMD 1144
Cdd:PRK11247 2 MNTARLNQGTP------LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1145 gqdikNISLYHLRTQMALVGQEPRLFV-GTIRENVCLGLKDVPLEKINQALELAnanrflgnlpdGIDTEVGERGGQLSG 1223
Cdd:PRK11247 73 -----TAPLAEAREDTRLMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAV-----------GLADRANEWPAALSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 1224 GQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLS-SIQNSDLIVYIDDGRV 1296
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
431-640 |
3.47e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.37 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 431 EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYE--PE---QGSVQIDGVDVRDLNLEWLRNVVGIVQQEP-IL 504
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 505 FNDTIHNNLLFGNP-----DATRETMIRV---CKMANAHDFIKKmpkgydtQIGDGGVQLSGGQKQRVAIARTLIRDPKV 576
Cdd:PRK14247 95 PNLSIFENVALGLKlnrlvKSKKELQERVrwaLEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNASKGRTTIMIAH-RLSTIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
136-368 |
4.12e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 101.08 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 136 MENVYIFLGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLG 215
Cdd:cd18572 36 YRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 216 VLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQE 295
Cdd:cd18572 116 VFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 296 EMVAKYEKQLNS----GKKHAIwggfwSGFFGGIFFFWLMAFMGCGIL-YGGYLLKVGIIkSPGDV--FIIVVAMLLGAY 368
Cdd:cd18572 196 REARRYERALDKalklSVRQAL-----AYAGYVAVNTLLQNGTQVLVLfYGGHLVLSGRM-SAGQLvtFMLYQQQLGEAF 269
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
417-635 |
8.69e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.19 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRK--EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDV----RDLNLEW 490
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 LRNVVGIVQQEP--ILFNDTIHNNLLFG--NPDATRETMIRVCK-----MANAHDFIKKMPkgydtqigdggVQLSGGQK 561
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGpqNFGIPKEKAEKIAAeklemVGLADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 562 QRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK-GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
433-642 |
9.10e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.81 E-value: 9.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLE---WLRNVVGIVQQ--------- 500
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQnpygslnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 501 --------EPILfndtIHNNLlfgnPDATREtmirvckmANAHDFIKKM---PKGYDTQIGdggvQLSGGQKQRVAIART 569
Cdd:PRK11308 109 kkvgqileEPLL----INTSL----SAAERR--------EKALAMMAKVglrPEHYDRYPH----MFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 570 LIRDPKVLLLDEATSALDAqseSVVQSALN-----NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDV---SVQAQVLNlmmdlQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1088-1300 |
9.28e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 98.21 E-value: 9.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1088 KFSYPQRPHQPVmKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIkNISLYHLRTQMALV---- 1163
Cdd:cd03266 10 RFRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVsdst 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPRLfvgTIRENVCL--GLKDVPLEKINQALELAnANRFlgnlpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03266 88 GLYDRL---TARENLEYfaGLYGLKGDELTARLEEL-ADRL------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1242 LLLDEATSALDSESERAVQEALDRAREGRTCITIA-HRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1110-1305 |
9.37e-23 |
|
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: 98.57 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYhlRTQMALVGQEPRLFVG-TIRENVCLGLKDVPL- 1187
Cdd:cd03296 28 GELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHmTVFDNVAFGLRVKPRs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1188 ---------EKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERA 1258
Cdd:cd03296 106 erppeaeirAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1259 VQEALDRARE--GRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:cd03296 175 LRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
438-640 |
9.91e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 9.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 438 LNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlEWLRNVVGIVQQEPILFNDTIHNNLLFG- 516
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPINMMFQSYALFPHMTVEQNIAFGl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 517 --NPDATRETMIRVCKM---ANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSE 591
Cdd:PRK11607 117 kqDKLPKAEIASRVNEMlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 592 SVVQSALNNASK--GRTTIMIAH-RLSTIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK11607 186 DRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1085-1305 |
1.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVG 1164
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEP-RLFVG-TIRENVCLGLKD--VPLE----KINQALELANANRFLGNLPdgidtevgergGQLSGGQKQRIAIARALV 1236
Cdd:PRK13642 88 QNPdNQFVGaTVEDDVAFGMENqgIPREemikRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1237 RDPKILLLDEATSALD----SESERAVQEALDRARegRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
435-629 |
1.37e-22 |
|
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: 97.92 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwlRNVVgiVQQEPILFNDTIHNNLL 514
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVV--FQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 515 FG----NPDAT---RETMIRvckmanAHDFIKKMPKGYDTQIGdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:TIGR01184 77 LAvdrvLPDLSkseRRAIVE------EHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678196980 588 AQSESVVQSALNNASK--GRTTIMIAHrlsTIREA----DKIVFFEKG 629
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTH---DVDEAlllsDRVVMLTNG 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1099-1306 |
1.80e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.50 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1099 VMKQLQWTALRGQTVALVGPSGSGKST---CIGMLERfydVTGGALRMDGQDIKNI-------------SLYHLRTQMAL 1162
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1163 VGQEPRLFVG-TIRENVclglkdvpLEKINQALELANAN------RFLGNLpdGIDTEV-GERGGQLSGGQKQRIAIARA 1234
Cdd:PRK10619 97 VFQHFNLWSHmTVLENV--------MEAPIQVLGLSKQEareravKYLAKV--GIDERAqGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1235 LVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELM 1306
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1082-1301 |
2.25e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS-LYHLRTQM 1160
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPRL-FVG-TIRENVCLGLKDV---PLE---KINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIA 1232
Cdd:PRK13644 80 GIVFQNPETqFVGrTVEEDLAFGPENLclpPIEirkRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESERAVQEALDRA-REGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGT 1301
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
416-635 |
2.76e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 96.96 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 416 KVTFENVhFRYPT--RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPE---QGSVQIDGVDV-RDLnle 489
Cdd:cd03234 3 VLPWWDV-GLKAKnwNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRkPDQ--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 490 WLRNVVGIVQQEPILFNDTIHNNLLFG--------NPDATRETMIRVCKMANAHDfikkmpkgydTQIGDGGVQ-LSGGQ 560
Cdd:cd03234 79 FQKCVAYVRQDDILLPGLTVRETLTYTailrlprkSSDAIRKKRVEDVLLRDLAL----------TRIGGNLVKgISGGE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 561 KQRVAIARTLIRDPKVLLLDEATSALDAQSE-SVVQSALNNASKGRTTIMIAH--RLSTIREADKIVFFEKGVIVEAG 635
Cdd:cd03234 149 RRRVSIAVQLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1110-1305 |
3.20e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.77 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIkniSLYHLRT-QMALVGQEPRLFVG-TIRENVCLGLKDVPL 1187
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDrKVGFVFQHYALFRHmTVFDNIAFGLTVLPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1188 ----------EKINQALELAN----ANRFlgnlPdgidtevgergGQLSGGQKQRIAIARALVRDPKILLLDEATSALDS 1253
Cdd:PRK10851 105 rerpnaaaikAKVTQLLEMVQlahlADRY----P-----------AQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1254 ESERAVQEALDRARE--GRTCITIAH-RLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK10851 170 QVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
435-640 |
3.47e-22 |
|
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: 96.28 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwLRNVVGIVQQEPILFND-TIHNNL 513
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 514 -----LFGNPDATRETMIR-VCKMANAHDFIKKMPKGYdtqigdggvqlSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:cd03265 95 yiharLYGVPGAERRERIDeLLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 588 AQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:cd03265 164 PQTRAHVWEYIEklKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1109-1307 |
3.73e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEP----RLfvgTIRENVCLG--- 1181
Cdd:COG4604 26 KGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENhinsRL---TVRELVAFGrfp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1182 -----LKDVPLEKINQALELAN----ANRFLgnlpdgiDtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:COG4604 103 yskgrLTAEDREIIDEAIAYLDledlADRYL-------D--------ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1253 SESERAVQEALDR-ARE-GRTCITIAHRLssiqN-----SDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:COG4604 168 MKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
439-642 |
4.15e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 439 NLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEwlRNVVGIVQQEPILFND-TIHNNLLFG- 516
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 517 NP-----DATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDaqse 591
Cdd:PRK10771 97 NPglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD---- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 592 svvqSALNN----------ASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK10771 162 ----PALRQemltlvsqvcQERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
420-642 |
4.41e-22 |
|
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: 96.59 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPtrkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWL-RNVVGIV 498
Cdd:COG0410 7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPILFND-TIHNNLLFG-----NPDATRETMIRVCKManahdF--IKKMpkgydtqIGDGGVQLSGGQKQRVAIARTL 570
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGayarrDRAEVRADLERVYEL-----FprLKER-------RRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 571 IRDPKVLLLDEATSALdaqSESVVQ------SALNnaSKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEeifeiiRRLN--REGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1049-1307 |
5.14e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 103.71 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1049 GAKSAAGQMFNLINRQPQTGDLKSGTKPEIRGNILFENVKFSYPqrphqpvmkqlqwtalRGQTVALVGPSGSGKSTCIG 1128
Cdd:PTZ00243 641 GGTGGGHEATPTSERSAKTPKMKTDDFFELEPKVLLRDVSVSVP----------------RGKLTVVLGATGSGKSTLLQ 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1129 MLERFYDVTGGalrmdgqdikniSLYHLRTqMALVGQEPRLFVGTIRENVcLGLKDVPLEKINQALELANANRFLGNLPD 1208
Cdd:PTZ00243 705 SLLSQFEISEG------------RVWAERS-IAYVPQQAWIMNATVRGNI-LFFDEEDAARLADAVRVSQLEADLAQLGG 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1209 GIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSE-SERAVQEALDRAREGRTCITIAHRLSSIQNSDL 1287
Cdd:PTZ00243 771 GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADY 850
|
250 260
....*....|....*....|
gi 1678196980 1288 IVYIDDGRVQESGTHKELMQ 1307
Cdd:PTZ00243 851 VVALGDGRVEFSGSSADFMR 870
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1099-1307 |
5.92e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1099 VMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYhlRTQMALVGQEPRLFVG-TIREN 1177
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1178 VCLGLK--DVPLEKINQ----ALELAN----ANRFlgnlpdgIDtevgerggQLSGGQKQRIAIARALVRDPKILLLDEA 1247
Cdd:PRK11432 99 VGYGLKmlGVPKEERKQrvkeALELVDlagfEDRY-------VD--------QISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1248 TSALDSESERAVQEALdRAREGRTCIT---IAHRLS-SIQNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK11432 164 LSNLDANLRRSMREKI-RELQQQFNITslyVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1096-1300 |
7.82e-22 |
|
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: 94.98 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1096 HQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNisLYHLRTQMALVGQEPRLFVG-TI 1174
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1175 RENVCLG--LKDVPLEKINQALELAnanrflgnlpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:cd03268 90 RENLRLLarLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1253 SESERAVQEAL-DRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:cd03268 159 PDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1081-1313 |
8.36e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.85 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1081 NILFENVKFSYPQrphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ--------DIKNIS 1152
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1153 LyhLRTQMALVGQE----PRLfvgTIRENV------CLGL-KDVPLEKINQ---ALELAN-ANRFlgnlPDgidtevger 1217
Cdd:COG4161 79 L--LRQKVGMVFQQynlwPHL---TVMENLieapckVLGLsKEQAREKAMKllaRLRLTDkADRF----PL--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1218 ggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSE-SERAVQEALDRAREGRTCITIAHRLS-SIQNSDLIVYIDDGR 1295
Cdd:COG4161 141 --HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEfARKVASQVVYMEKGR 218
|
250
....*....|....*...
gi 1678196980 1296 VQESGTHKELMQLKGKYF 1313
Cdd:COG4161 219 IIEQGDASHFTQPQTEAF 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
416-642 |
9.42e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.19 E-value: 9.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 416 KVTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVD---VRDLN----- 487
Cdd:PRK10619 5 KLNVIDLHKRY---GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlVRDKDgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 488 -----LEWLRNVVGIVQQEpilFNDTIHNNLLfgnpDATRETMIRVCKMANA---HDFIKKMPK-GYD-TQIGDGGVQLS 557
Cdd:PRK10619 82 adknqLRLLRTRLTMVFQH---FNLWSHMTVL----ENVMEAPIQVLGLSKQearERAVKYLAKvGIDeRAQGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 558 GGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
....*..
gi 1678196980 636 NHEELVN 642
Cdd:PRK10619 235 APEQLFG 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1097-1299 |
1.05e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.17 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRE 1176
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1177 NVCLglkdvPLEKINQALE----LANANRFlgNLPDGIdteVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PRK10247 100 NLIF-----PWQIRNQQPDpaifLDDLERF--ALPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1253 SESERAVQEALDR-ARE-GRTCITIAHRLSSIQNSDLIVYIDD--GRVQES 1299
Cdd:PRK10247 170 ESNKHNVNEIIHRyVREqNIAVLWVTHDKDEINHADKVITLQPhaGEMQEA 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
438-640 |
1.09e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 98.26 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 438 LNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRD----LNLEWLRNVVGIVQQEPILFND-TIHNN 512
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFG----NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDA 588
Cdd:TIGR02142 96 LRYGmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 589 QSESVVQSALNN--ASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEEL 640
Cdd:TIGR02142 165 PRKYEILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
426-640 |
1.17e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 426 YPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEP--I 503
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 504 LFNDTIHNNLLFG------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVL 577
Cdd:PRK13652 91 IFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 578 LLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
435-629 |
1.94e-21 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 94.32 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSvgLLTRLYEPE--QGSVQIDGVDVRDLNLEWL----RNVVGIVQQEPILFNDT 508
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 509 IHNNLLFGNP-DATR-ETMIRVCKMANAHDFikkMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:cd03290 95 VEENITFGSPfNKQRyKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678196980 587 DAQ-SESVVQSALNN--ASKGRTTIMIAHRLSTIREADKIVFFEKG 629
Cdd:cd03290 172 DIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
433-640 |
2.05e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRnvVGIVQQEPILFND-TIHN 511
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 512 NLLFG----------NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDE 581
Cdd:PRK10851 94 NIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 582 ATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
439-642 |
2.10e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.18 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 439 NLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV-----VGIVQQEPILFNDTIHNNL 513
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkiAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 514 LFGNPDA------TRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:PRK10070 128 AFGMELAginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 588 AQSESVVQSALN--NASKGRTTIMIAHRL-STIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK10070 197 PLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1085-1289 |
2.17e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.31 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQ-RPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlyhlrTQMALV 1163
Cdd:COG4525 7 RHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQE----PRLfvgTIRENVCLGLKdvpLEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDP 1239
Cdd:COG4525 82 FQKdallPWL---NVLDNVAFGLR---LRGVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1240 KILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHrlsSIQN-----SDLIV 1289
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH---SVEEalflaTRLVV 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
420-633 |
2.21e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.52 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPT------RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRN 493
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQqepILFNDTIhnnllfG--NPDAT-----RETM------------IRVCKMANAHDF----IKKMPKgydtqig 550
Cdd:PRK10419 87 FRRDIQ---MVFQDSI------SavNPRKTvreiiREPLrhllsldkaerlARASEMLRAVDLddsvLDKRPP------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 551 dggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDA--QSESVVQSALNNASKGRTTIMIAHRLSTI-READKIVFFE 627
Cdd:PRK10419 151 ----QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlQAGVIRLLKKLQQQFGTACLFITHDLRLVeRFCQRVMVMD 226
|
....*.
gi 1678196980 628 KGVIVE 633
Cdd:PRK10419 227 NGQIVE 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
430-635 |
2.38e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.82 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 430 KEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWlrNVVGIVQQEPILF-NDT 508
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 509 IHNNL-----LFGNPDATRETMIRVCKMANAHDfiKKMpKGYdtqigdggvqlSGGQKQRVAIARTLIRDPKVLLLDEAT 583
Cdd:cd03268 89 ARENLrllarLLGIRKKRIDEVLDVVGLKDSAK--KKV-KGF-----------SLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 584 SALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:cd03268 155 NGLDPDGIKELRELILSlRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1109-1305 |
2.50e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDiknislYHLRTQM-------ALVGQEPRLFVG-TIRENVCL 1180
Cdd:COG1129 29 PGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP------VRFRSPRdaqaagiAIIHQELNLVPNlSVAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 GLKDVPLEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSAL-DSESER-- 1257
Cdd:COG1129 103 GREPRRGGLIDWRAMRRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLtEREVERlf 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678196980 1258 AVQEALdrAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:COG1129 181 RIIRRL--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
395-639 |
2.97e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 395 DRVPKID--PYSRHGKKIekvvgkVTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPE 472
Cdd:COG0488 298 DKTVEIRfpPPERLGKKV------LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 473 QGSVQIdGVDVRdlnlewlrnvVGIVQQEPILF--NDTIHNNLLFGNPDATRETmirvckmanAHDFIKKM---PKGYDT 547
Cdd:COG0488 369 SGTVKL-GETVK----------IGYFDQHQEELdpDKTVLDELRDGAPGGTEQE---------VRGYLGRFlfsGDDAFK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 548 QIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNAsKGrTTIMIAH-R--LSTIreADKIV 624
Cdd:COG0488 429 PVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--ATRIL 500
|
250
....*....|....*.
gi 1678196980 625 FFEKGVIVE-AGNHEE 639
Cdd:COG0488 501 EFEDGGVREyPGGYDD 516
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
439-640 |
3.52e-21 |
|
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: 96.71 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 439 NLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGV----DVRDLNLE-WLRNVvGIVQQEPILFND-TIHNN 512
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPpHRRRI-GYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFG----NPDATRETMIRVCKMANAHDFIKKMPkgydtqigdggVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDA 588
Cdd:COG4148 98 LLYGrkraPRAERRISFDEVVELLGIGHLLDRRP-----------ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 589 QSesvvqsalnnaskgRTTIM-----IAHRLST------------IREADKIVFFEKGVIVEAGNHEEL 640
Cdd:COG4148 167 AR--------------KAEILpylerLRDELDIpilyvshsldevARLADHVVLLEQGRVVASGPLAEV 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1109-1306 |
4.00e-21 |
|
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: 93.89 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKST---CI-GMLerfyDVTGGALRMDGQDIKNISLYHL-RTQMALVGQEPRLFVG-TIRENVCLGL 1182
Cdd:COG0410 28 EGEIVALLGRNGAGKTTllkAIsGLL----PPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEENLLLGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 KDVP-LEKINQALELANAnRFlgnlPdgidtEVGER----GGQLSGGQKQRIAIARALVRDPKILLLDEATSALdseSER 1257
Cdd:COG0410 104 YARRdRAEVRADLERVYE-LF----P-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1258 AVQE---ALDR-AREGRT----------CITIAHRlssiqnsdliVYI-DDGRVQESGTHKELM 1306
Cdd:COG0410 171 IVEEifeIIRRlNREGVTillveqnarfALEIADR----------AYVlERGRIVLEGTAAELL 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
417-635 |
6.05e-21 |
|
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: 92.73 E-value: 6.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlewlRNVVG 496
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFND-TIHNNLLF-----G-NPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIART 569
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYlaqlkGlKKEEARRRIDEWLERLELSEYANKRVE-----------ELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
420-635 |
7.10e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 93.64 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIV- 498
Cdd:COG4559 5 ENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPILFNDTIHNNLLFG----------NPDATRETMIRVckmaNAHDFIKKMpkgYDTqigdggvqLSGGQKQRVAIAR 568
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGraphgssaaqDRQIVREALALV----GLAHLAGRS---YQT--------LSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 569 TLI-------RDPKVLLLDEATSALD-AQSESVVQSALNNASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAG 635
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDlAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQG 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
435-639 |
7.42e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTsvgLLTRL--YEPEQGSVQIDGVDVRDLNLE-------WLRnvvgivQQEPILF 505
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAelarhraYLS------QQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 506 NDTIHNNLLFGNPDATRETMIRVCKMANAHDFiKKMPKgYDTQIGdggvQLSGGQKQRVAIARTLIR-------DPKVLL 578
Cdd:COG4138 83 AMPVFQYLALHQPAGASSEAVEQLLAQLAEAL-GLEDK-LSRPLT----QLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 579 LDEATSALD-AQsesvvQSALNN-----ASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEE 639
Cdd:COG4138 157 LDEPMNSLDvAQ-----QAALDRllrelCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
91-312 |
8.06e-21 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 94.38 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIGLITSVISGVSQPVLA--IISGRMTNVLLVIDPLskefktktMENVYIFLGLGIFVSINDFCQYMCFQRVCSRMM 168
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIkrAIDDYIVPGQGDLQGL--------LLLALLYLGLLLLSFLLQYLQTYLLQKLGQRII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 169 TVMRNRYISSILRQNAGWFDKNLSGTITTRL-NDnMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIP 247
Cdd:cd18544 74 YDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVtND-TEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 248 VSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKqLNSGKKHA 312
Cdd:cd18544 153 LLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDE-INQEYRKA 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
415-624 |
8.41e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.34 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTRKEakVLNGLNLTVEPGTSVALVGHSGCGKSTsvgLLtR----LYEPEQGSVQI-DGVDVrdlnle 489
Cdd:COG4178 361 GALALEDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKST---LL-RaiagLWPYGSGRIARpAGARV------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 490 wLrnvvgIVQQEPILFNDTIHNNLLFGNP--DATRETMIRVCKMANAHDFIKKMpkgyDTQiGDGGVQLSGGQKQRVAIA 567
Cdd:COG4178 429 -L-----FLPQRPYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLAERL----DEE-ADWDQVLSLGEQQRLAFA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIV 624
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1082-1318 |
8.46e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 99.67 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCI-GMLerfydvtGGALRMDGQDIKnislyhLRTQM 1160
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIsAML-------GELSHAETSSVV------IRGSV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEPRLFVGTIRENVCLGlKDVPLEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPK 1240
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1241 ILLLDEATSALDSESERAV-QEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMqlkgKYFELIKK 1318
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS----KSGSLFKK 835
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
123-313 |
8.82e-21 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 94.50 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 123 VID-----PLSKEFKTKTMENVYIFLgLGIFV--SINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTI 195
Cdd:cd18573 22 LIDvaskeSGDIEIFGLSLKTFALAL-LGVFVvgAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 196 TTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAG 275
Cdd:cd18573 101 VSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADAT 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678196980 276 AIAEECLMGVRTIQAFNGQEEMVAKYEKQLNS----GKKHAI 313
Cdd:cd18573 181 KVAEERLSNIRTVRAFAAERKEVERYAKKVDEvfdlAKKEAL 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1109-1296 |
9.19e-21 |
|
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: 90.57 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRtqmalvgqepRLFVGTIRenvclglkdvple 1188
Cdd:cd03216 25 RGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR----------RAGIAMVY------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1189 kinqalelananrflgnlpdgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR-AR 1267
Cdd:cd03216 82 -------------------------------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRlRA 130
|
170 180 190
....*....|....*....|....*....|
gi 1678196980 1268 EGRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:cd03216 131 QGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1086-1321 |
9.78e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1086 NVKFSYPQrpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIK--NISLYHLRTQMALV 1163
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEP--RLFVGTIRENVC-----LGLKDVPLEK-INQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARAL 1235
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAfgplnLGLSKEEVEKrVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1236 VRDPKILLLDEATSALDSESERAVQEAL-DRAREGRTCITIAHRLSSIQ-NSDLIVYIDDGRVQESGTHKELMQLKgkyf 1313
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI---- 228
|
....*...
gi 1678196980 1314 ELIKKQDL 1321
Cdd:PRK13639 229 ETIRKANL 236
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1094-1298 |
1.10e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 93.33 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1094 RPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNI---SLYHLRTQMALVGQE---- 1166
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDspsa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1167 --PRLfvgTIRENVCLGLKDvpLEKINQALELANANRFLGNLpdGIDTEVGER-GGQLSGGQKQRIAIARALVRDPKILL 1243
Cdd:TIGR02769 101 vnPRM---TVRQIIGEPLRH--LTSLDESEQKARIAELLDMV--GLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1244 LDEATSALDSESERAVQEALD--RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQE 1298
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1082-1302 |
1.20e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrpHQpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ--------DIKNISL 1153
Cdd:PRK11124 3 IQLNGINCFYGA--HQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1154 yhLRTQMALVGQE----PRLfvgTIRENV------CLGLKDVplEKINQALELANANRFlgnlpdgidTEVGERGG-QLS 1222
Cdd:PRK11124 80 --LRRNVGMVFQQynlwPHL---TVQQNLieapcrVLGLSKD--QALARAEKLLERLRL---------KPYADRFPlHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1223 GGQKQRIAIARALVRDPKILLLDEATSALDSE-SERAVQEALDRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
..
gi 1678196980 1301 TH 1302
Cdd:PRK11124 224 DA 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1082-1306 |
1.28e-20 |
|
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: 92.84 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERF-YDVTGGALRMDGQDIKNISLYHLRTQM 1160
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQE--PRLFVG-TIRENVC------LGL-KDVPLEKINQALELananrfLGNLpdGIDTEVGERGGQLSGGQKQRIA 1230
Cdd:COG1119 81 GLVSPAlqLRFPRDeTVLDVVLsgffdsIGLyREPTDEQRERAREL------LELL--GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1231 IARALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTC-ITIAHRLssiqnSDLIVYID------DGRVQESGTH 1302
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTlVLVTHHV-----EEIPPGIThvlllkDGRVVAAGPK 227
|
....
gi 1678196980 1303 KELM 1306
Cdd:COG1119 228 EEVL 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1098-1277 |
1.29e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 92.11 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1098 PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ----DIKNIS----LYHLRTQMALVGQ---- 1165
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASpreiLALRRRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1166 EPRlfVGTIrenvclglkDV---PL----EKINQALELANA--NRFlgNLPdgidtevgERGGQL-----SGGQKQRIAI 1231
Cdd:COG4778 105 IPR--VSAL---------DVvaePLlergVDREEARARAREllARL--NLP--------ERLWDLppatfSGGEQQRVNI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678196980 1232 ARALVRDPKILLLDEATSALDSESERAVQEALDRA-REGRTCITIAH 1277
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFH 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1085-1304 |
1.54e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPHQ-PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNI---SLYHLRTQ- 1159
Cdd:PRK10535 8 KDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVG-TIRENVclglkDVP--LEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALV 1236
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNV-----EVPavYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1237 RDPKILLLDEATSALDSESERAVQEALDRARE-GRTCITIAHRLSSIQNSDLIVYIDDGR-VQESGTHKE 1304
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEiVRNPPAQEK 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1093-1307 |
1.59e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1093 QRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRL-FV 1171
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1172 GTIRENVCLGLKDVPLEK------INQALELAN----ANRFlgnLPdgidtevgerggQLSGGQKQRIAIARALVR---- 1237
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRaeddalVAAALAQVDlahlAGRD---YP------------QLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1238 --DPKILLLDEATSALD-SESERAVQEALDRARE-GRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK13548 156 dgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
419-612 |
1.61e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 419 FENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvDVRdlnlewlrnvVGIV 498
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPILFND-TIHNNLLFGNPDAtRETMIRVC----KMANAHDFIKKMPK---------GY------------------- 545
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAEL-RALEAELEeleaKLAEPDEDLERLAElqeefealgGWeaearaeeilsglgfpeed 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 546 -DTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAqsESVV--QSALNNaSKGrTTIMIAH 612
Cdd:COG0488 146 lDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--ESIEwlEEFLKN-YPG-TVLVVSH 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1114-1305 |
1.89e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.42 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ------DIKNISLYHLRTQMALVGQEPRLFVG-TIRENVCLGLKDVP 1186
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHlSIYDNIAYPLKSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 LEKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRA 1266
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 1267 REGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK14246 200 KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
417-640 |
2.34e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.71 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVhfrYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLnlEWLRNVVG 496
Cdd:PRK11000 4 VTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILF-NDTIHNNLLFGNPDA---TRETMIRVCKMAN----AHdFIKKMPKGydtqigdggvqLSGGQKQRVAIAR 568
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFGLKLAgakKEEINQRVNQVAEvlqlAH-LLDRKPKA-----------LSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 569 TLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAH-RLSTIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1110-1304 |
2.38e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI--KNISLYHLRTQMALVGQEP--RLFVGTIRENVCLGLKDV 1185
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1186 PLE------KINQALELAnanrflgnlpdGIDTEVGERGG--QLSGGQKQRIAIARALVRDPKILLLDEATSALDSeseR 1257
Cdd:PRK13637 113 GLSeeeienRVKRAMNIV-----------GLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP---K 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1258 AVQEALDRARE-----GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKE 1304
Cdd:PRK13637 179 GRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
421-640 |
2.93e-20 |
|
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: 96.29 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 421 NVHFRYPTRkEAKVLNGLNLTVEPGTSVALVGHSGCGKSTS----VGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNV-- 494
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 --VGIVQQEPI-----LFndTI----------HNNLlfgNPDATRETMI----RVcKMANAHDFIKKMPKgydtqigdgg 553
Cdd:COG4172 92 nrIAMIFQEPMtslnpLH--TIgkqiaevlrlHRGL---SGAAARARALelleRV-GIPDPERRLDAYPH---------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 554 vQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDA--QSE-----SVVQSALNNAskgrtTIMIAHRLSTIRE-ADKIVF 625
Cdd:COG4172 156 -QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvQAQildllKDLQRELGMA-----LLLITHDLGVVRRfADRVAV 229
|
250
....*....|....*
gi 1678196980 626 FEKGVIVEAGNHEEL 640
Cdd:COG4172 230 MRQGEIVEQGPTAEL 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1082-1296 |
3.29e-20 |
|
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: 89.92 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPHQ---PVMKQLQWTALRGQTVALVGPSGSGKSTCIGML--ERFYDVTGGALRMDGqdiKNISLYHL 1156
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1157 RTQMALVGQE----PRLfvgTIRENVclglkdvplekinqalelananRFLGNLpdgidtevgeRGgqLSGGQKQRIAIA 1232
Cdd:cd03213 81 RKIIGYVPQDdilhPTL---TVRETL----------------------MFAAKL----------RG--LSGGERKRVSIA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSS--IQNSDLIVYIDDGRV 1296
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1082-1300 |
3.37e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.58 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSY-PQRPHQPV-MKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIK----NISLYH 1155
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVGQ--EPRLFVGTIRENVCLGLKDVPL---EKINQALElananrFLGNLpdGIDTEVGERGG-QLSGGQKQRI 1229
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFsedEAKEKALK------WLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1230 AIARALVRDPKILLLDEATSALDSESERAVQEA-LDRAREGRTCITIAHRLssiqnSDLIVYIDDGRVQESG 1300
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNM-----DDVAEYADDVLVLEHG 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1097-1300 |
3.91e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.52 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRL-FVGTIR 1175
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCLG----------LKDVPLEKINQALELANANRFlgnlpdgIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLD 1245
Cdd:PRK09536 96 QVVEMGrtphrsrfdtWTETDRAAVERAMERTGVAQF-------ADRPVTS----LSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1246 EATSALDSESE-RAVQEALDRAREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESG 1300
Cdd:PRK09536 165 EPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
429-641 |
4.11e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 96.27 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 429 RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPE---QGSVQIDGvdvRDLNLEWLRNVVGIVQQEPILF 505
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 506 ND-TIHNNLLF------GNPDATRETMIRVckmanaHDFIKKMP--KGYDTQIGDGGVQ--LSGGQKQRVAIARTLIRDP 574
Cdd:TIGR00955 112 PTlTVREHLMFqahlrmPRRVTKKEKRERV------DEVLQALGlrKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 575 KVLLLDEATSALDAQS-ESVVQSALNNASKGRTTIMIAHRLST--IREADKIVFFEKGVIVEAGNHEELV 641
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1109-1294 |
4.31e-20 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 90.47 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCI-GMLERFYDVTGGAL---RMDGQDIKNISLYHLRTQMALVGQEPRLFVGTIRENVCLGlkd 1184
Cdd:cd03290 26 TGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFG--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1185 VPLEK--INQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSE-SERAVQE 1261
Cdd:cd03290 103 SPFNKqrYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQE 182
|
170 180 190
....*....|....*....|....*....|....*
gi 1678196980 1262 ALDR--AREGRTCITIAHRLSSIQNSDLIVYIDDG 1294
Cdd:cd03290 183 GILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
425-624 |
4.99e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 425 RYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvdvrdlnlewLRNVVGIVQQE--- 501
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSevp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 502 ---PILFNDTI------HNNLLFGNPDATRETMIRVCKMANAHDFIKKmpkgydtQIGDggvqLSGGQKQRVAIARTLIR 572
Cdd:NF040873 68 dslPLTVRDLVamgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNAS-KGRTTIMIAHRLSTIREADKIV 624
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCV 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
434-640 |
5.15e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 93.25 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWlRNVVgIVQQEPILF-NDTIHNN 512
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDIC-MVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 L-----LFGNPDATRETmiRVCKMANAHDFIkkmpkGYDTQIGDggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:PRK11432 99 VgyglkMLGVPKEERKQ--RVKEALELVDLA-----GFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 588 AQ-----SESV--VQSALNnaskgRTTIMIAHRLStirEA----DKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK11432 169 ANlrrsmREKIreLQQQFN-----ITSLYVTHDQS---EAfavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
431-642 |
5.31e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.46 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 431 EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDL------------------------ 486
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 487 NLEWLRNVVGIVQQ--EPILFNDTIHNNLLFG------NPDATRETMIRVCKMAN-AHDFIKKMPkgydtqigdggVQLS 557
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvSKEEAKKRAAKYIELVGlDESYLQRSP-----------FELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 558 GGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK-GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDG 247
|
....*..
gi 1678196980 636 NHEELVN 642
Cdd:PRK13651 248 DTYDILS 254
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
90-304 |
5.58e-20 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 91.72 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 90 YILLLIGLITSVISGVSQPVLA------IISGRMTNVLLVIdplskefktktmenVYIFLGLGIFVSINDFCQYMCFQRV 163
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIrriidsVIGGGLRELLWLL--------------ALLILGVALLRGVFRYLQGYLAEKA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 164 CSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMML 243
Cdd:cd18542 67 SQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 244 GLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQ 304
Cdd:cd18542 147 AIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKE 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
420-642 |
6.41e-20 |
|
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: 90.29 E-value: 6.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNL-EWLRNVVGIV 498
Cdd:cd03218 4 ENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPILFND-TIHNNLL-----FGNPDATRETMIRvckmANAHDF-IKKMPKGYdtqigdgGVQLSGGQKQRVAIARTLI 571
Cdd:cd03218 81 PQEASIFRKlTVEENILavleiRGLSKKEREEKLE----ELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALNN-ASKG----------RTTIMIAHRLSTIREadkivffekGVIVEAGNHEEL 640
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGigvlitdhnvRETLSITDRAYIIYE---------GKVLAEGTPEEI 220
|
..
gi 1678196980 641 VN 642
Cdd:cd03218 221 AA 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1100-1294 |
8.61e-20 |
|
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: 89.83 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1100 MKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI-----------KNISLYhlrtqmalvgqePR 1168
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdrmvvfQNYSLL------------PW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1169 LfvgTIRENVCLGLKDV-PLEKINQALELANANRFLGNLPDGIDtevgERGGQLSGGQKQRIAIARALVRDPKILLLDEA 1247
Cdd:TIGR01184 69 L---TVRENIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1248 TSALDSESERAVQEALDRARE--GRTCITIAHRL-SSIQNSDLIVYIDDG 1294
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1094-1298 |
9.98e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.52 E-value: 9.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1094 RPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlyhlRTQMA-------LVGQE 1166
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN----RAQRKafrrdiqMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1167 ------PRLFVGTI-RENV--CLGLKDVplEKINQALELANANrflgNLPDGIdteVGERGGQLSGGQKQRIAIARALVR 1237
Cdd:PRK10419 98 sisavnPRKTVREIiREPLrhLLSLDKA--ERLARASEMLRAV----DLDDSV---LDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1238 DPKILLLDEATSALDseseRAVQ-EALD-----RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQE 1298
Cdd:PRK10419 169 EPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
141-307 |
1.13e-19 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 91.01 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 141 IFLGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRG 220
Cdd:cd18575 41 LLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 221 ISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAK 300
Cdd:cd18575 121 LLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQR 200
|
....*..
gi 1678196980 301 YEKQLNS 307
Cdd:cd18575 201 FATAVEA 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1109-1305 |
1.21e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.56 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS---LYHLRTQMALVGQE------PRLFVGTIRENvc 1179
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNpygslnPRKKVGQILEE-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 lglkdvPLEkINQALELAN-ANRFLGNLPD-GIDTEVGERGGQL-SGGQKQRIAIARALVRDPKILLLDEATSALDSeSE 1256
Cdd:PRK11308 118 ------PLL-INTSLSAAErREKALAMMAKvGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1257 RA--------VQEALdrareGRTCITIAHRLS---SIQNSDLIVYIddGRVQESGTHKEL 1305
Cdd:PRK11308 190 QAqvlnlmmdLQQEL-----GLSYVFISHDLSvveHIADEVMVMYL--GRCVEKGTKEQI 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
420-632 |
1.38e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.79 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKEA-KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWL----RNV 494
Cdd:PRK10535 8 KDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 495 VG-IVQQEPILFNDTIHNNLLFGNPDATRETMIRvckMANAHDFIKKMpkGYDTQIGDGGVQLSGGQKQRVAIARTLIRD 573
Cdd:PRK10535 88 FGfIFQRYHLLSHLTAAQNVEVPAVYAGLERKQR---LLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 574 PKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIREADKIVFFEKGVIV 632
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1082-1307 |
1.40e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQ-RPHQ-PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI----KNISLYH 1155
Cdd:PRK13649 3 INLQNVSYTYQAgTPFEgRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVGQ--EPRLFVGTIRENVCLGLKDVPLEKInQALELANANRFLGnlpdGIDTEVGERGG-QLSGGQKQRIAIA 1232
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQE-EAEALAREKLALV----GISESLFEKNPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESERAVQEALDRARE-GRTCITIAHRLSSIQNSDLIVYI-DDGRVQESGTHKELMQ 1307
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVlEKGKLVLSGKPKDIFQ 234
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
761-1054 |
1.46e-19 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 91.18 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 761 MLIGLSAALIRGLDLPTFALLFAWVFEGFEFVPYGGKMMHRLA--------------MSVIAHCAAGLGIWFFQT--LST 824
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGlnssagpfekleeeMTLYAYYYLIIGAIVLITayIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 825 VMFAIVSENLGVRFRVAAFRNLLYQDAAYFdnPAHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFINC 904
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 905 WQVAILGTALIFLLGfIMAGLAFKI--SIVAAEHMENDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELR 982
Cdd:cd18558 159 WKLTLVILAISPVLG-LSAVVWAKIlsGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 983 KSVYEAVNYCISQNFMYYMSCFCFALAIRIINQGDQTVDKTFRCLMAMMLCCEGIIMSAQFFPQFVGAKSAA 1054
Cdd:cd18558 238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAA 309
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
434-629 |
1.47e-19 |
|
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: 89.03 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQID----GVDV-----RDLnLEWLRNVVGIVQQ---- 500
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaspREI-LALRRRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 501 -----------EPI----------------LFNdtiHNNL---LFGNPDATretmirvckmanahdFikkmpkgydtqig 550
Cdd:COG4778 105 iprvsaldvvaEPLlergvdreeararareLLA---RLNLperLWDLPPAT---------------F------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 551 dggvqlSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNA-SKGRTTIMIAHRLSTI-READKIVFFEK 628
Cdd:COG4778 154 ------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVReAVADRVVDVTP 227
|
.
gi 1678196980 629 G 629
Cdd:COG4778 228 F 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-640 |
1.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQ-----GSVQIDGVDV--RDLNLEWLRNVVGIVQQEPILF- 505
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 506 NDTIHNNLLFG--------NPDATRETMIRVCKMANAHDFIKKMPKGYDTQigdggvqLSGGQKQRVAIARTLIRDPKVL 577
Cdd:PRK14267 99 HLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 578 LLDEATSALDAQSESVVQSALNNASKGRTTIMIAHR-LSTIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1110-1307 |
1.81e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLFVG-TIRENVCLG------- 1181
Cdd:PRK11231 28 GKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRELVAYGrspwlsl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1182 ---LKDVPLEKINQALELAnanrflgnlpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD----SE 1254
Cdd:PRK11231 108 wgrLSAEDNARVNQAMEQT-----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 1255 SERAVQEaldRAREGRTCITIAHRLSsiQNS---DLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK11231 177 LMRLMRE---LNTQGKTVVTVLHDLN--QASrycDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1114-1307 |
1.96e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGMLERFYDVTG-----GALRMDGQDIKN--ISLYHLRTQMALVGQEPRLFVG-TIRENVCLGLKDV 1185
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFPHlTIYDNVAIGVKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1186 PL--------EKINQALELANanrflgnLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESER 1257
Cdd:PRK14267 114 GLvkskkeldERVEWALKKAA-------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1258 AVQEALDRAREGRTCITIAHR-LSSIQNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK14267 187 KIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
415-640 |
2.30e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.07 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTFENVHFRYPTRK--EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDV-----RDLN 487
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 488 LEWLRNVVGIVQQEP--ILFNDTIHNNLLFG--NPDATRETMIRvcKMANAHDFIKkMPKGYdtqIGDGGVQLSGGQKQR 563
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLKLVQ-LPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 564 VAIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1082-1318 |
2.46e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.76 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSY---PQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS-LYHLR 1157
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1158 TQMALVGQEP-RLFVGTI-RENVCLGLKD--VPLEKI----NQALELANANRFLGNLPDgidtevgerggQLSGGQKQRI 1229
Cdd:PRK13633 85 NKAGMVFQNPdNQIVATIvEEDVAFGPENlgIPPEEIrervDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1230 AIARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMq 1307
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIF- 232
|
250
....*....|.
gi 1678196980 1308 lkgKYFELIKK 1318
Cdd:PRK13633 233 ---KEVEMMKK 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
420-632 |
2.62e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVH--FRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlEWLR-NVVG 496
Cdd:COG1101 5 KNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRaKYIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPIL---FNDTIHNNLL------------FGNPDATRETMirvckmanaHDFIKKMPKGY----DTQIGdggvQLS 557
Cdd:COG1101 84 RVFQDPMMgtaPSMTIEENLAlayrrgkrrglrRGLTKKRRELF---------RELLATLGLGLenrlDTKVG----LLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 558 GGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLS-TIREADKIVFFEKGVIV 632
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
420-640 |
2.90e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDG--VDVRDLNLEWLRNVVGI 497
Cdd:PRK13636 9 EELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VQQEP--ILFNDTIHNNLLFG------NPDATRETMIRVCKMAN-AHdfIKKMPKGYdtqigdggvqLSGGQKQRVAIAR 568
Cdd:PRK13636 87 VFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRTGiEH--LKDKPTHC----------LSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 569 TLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGR-TTIMIA-HRLSTIR-EADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
420-639 |
3.02e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRyptRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QepilfndtiHNNLLF----------------GNPDATRETMIRVCKMANAHDFikkmpKGYDTQigdggvQLSGGQKQR 563
Cdd:PRK13548 83 Q---------HSSLSFpftveevvamgraphgLSRAEDDALVAAALAQVDLAHL-----AGRDYP------QLSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 564 VAIARTLIR------DPKVLLLDEATSALD-AQSESVVQSALNNASK-GRTTIMIAHRLS-TIREADKIVFFEKGVIVEA 634
Cdd:PRK13548 143 VQLARVLAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVAD 222
|
....*
gi 1678196980 635 GNHEE 639
Cdd:PRK13548 223 GTPAE 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1085-1307 |
4.19e-19 |
|
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: 87.98 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHlRTQMAL-- 1162
Cdd:cd03218 4 ENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1163 VGQEPRLFVG-TIRENVCLGL------KDVPLEKINQALELANANRFLGNLpdgidtevgerGGQLSGGQKQRIAIARAL 1235
Cdd:cd03218 80 LPQEASIFRKlTVEENILAVLeirglsKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1236 VRDPKILLLDEATSALD----SESERAVQEALDR----------AREgrtCITIAHRlssiqnsdliVYI-DDGRVQESG 1300
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDpiavQDIQKIIKILKDRgigvlitdhnVRE---TLSITDR----------AYIiYEGKVLAEG 215
|
....*..
gi 1678196980 1301 THKELMQ 1307
Cdd:cd03218 216 TPEEIAA 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1114-1305 |
5.87e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGMLERFYD-VTG----GALRMDGQDIKNI-SLYHLRTQMALVGQEPRLFVGTIRENVCLGLKDVPL 1187
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDkVSGyrysGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1188 EKINQALELANANRFLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAR 1267
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190
....*....|....*....|....*....|....*....
gi 1678196980 1268 EGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK14271 211 DRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
417-623 |
6.44e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.09 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDlNLEWLRNVVG 496
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFND-TIHNNLL-----FGNPDAT-RETMIRVCKMAnahdfikKMPKGYDTQIGDggvqLSGGQKQRVAIART 569
Cdd:PRK13537 84 VVPQFDNLDPDfTVRENLLvfgryFGLSAAAaRALVPPLLEFA-------KLENKADAKVGE----LSGGMKRRLTLARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAH----------RLSTIREADKI 623
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHfmeeaerlcdRLCVIEEGRKI 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1082-1305 |
6.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQ-RPHQPV-MKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI----KNISLYH 1155
Cdd:PRK13646 3 IRFDNVSYTYQKgTPYEHQaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVGQ--EPRLFVGTIRENVCLGLKD--VPLEKINqalelANANRFLGNLpdGIDTEVGERGG-QLSGGQKQRIA 1230
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVK-----NYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1231 IARALVRDPKILLLDEATSALDSESERAVQEALDRAR--EGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1109-1279 |
1.02e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.53 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGAlRMDGQDI---KNISLYH-----LRTQMALVGQEPRLFVGTIRENVCL 1180
Cdd:PRK14243 35 KNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgKNLYAPDvdpveVRRRIGMVFQKPNPFPKSIYDNIAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 GLK------DVPlEKINQALELANanrflgnLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSE 1254
Cdd:PRK14243 114 GARingykgDMD-ELVERSLRQAA-------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPI 185
|
170 180
....*....|....*....|....*
gi 1678196980 1255 SERAVQEALDRAREGRTCITIAHRL 1279
Cdd:PRK14243 186 STLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
417-631 |
1.02e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.43 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGV---DVRDlnlewlrN 493
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaEARE-------D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPILFNDTIHNNL---LFGN-PDATRETMIRVckmanahdfikkmpkGYDTQIGDGGVQLSGGQKQRVAIART 569
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVglgLKGQwRDAALQALAAV---------------GLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLS-TIREADKIVFFEKGVI 631
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1109-1305 |
1.23e-18 |
|
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: 86.27 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLyHLRTQMALVGQEPRLFVG-TIRENVCL-----GL 1182
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDElTGWENLYIharlyGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 K-DVPLEKINQALElananrFLGnLPDGIDTEVGerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQE 1261
Cdd:cd03265 104 PgAERRERIDELLD------FVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678196980 1262 ALDR--AREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:cd03265 173 YIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
420-640 |
1.44e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.04 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWL-RNVVGIV 498
Cdd:TIGR03410 4 SNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPILFND-TIHNNLLFG---NPDATRE------TMIRVCKmanahDFIKKmpKGydtqiGDggvqLSGGQKQRVAIAR 568
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTGlaaLPRRSRKipdeiyELFPVLK-----EMLGR--RG-----GD----LSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 569 TLIRDPKVLLLDEATSALDAqseSVVQ---SALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQP---SIIKdigRVIRrlRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1084-1323 |
2.24e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQdiknislyhlrTQMALV 1163
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPRLFVG-TIRENVCLGLKDV-----PLEKINQALEL------------------------ANANRFLGNLpdGIDTE 1213
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraleaELEELEAKLAEpdedlerlaelqeefealggweaeARAEEILSGL--GFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1214 VGERG-GQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALdRAREGrTCITIAH-R--LSSIQNSdlIV 1289
Cdd:COG0488 145 DLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL-KNYPG-TVLVVSHdRyfLDRVATR--IL 220
|
250 260 270
....*....|....*....|....*....|....*.
gi 1678196980 1290 YIDDGRVQEsgthkelmqLKGKY--FELIKKQDLAI 1323
Cdd:COG0488 221 ELDRGKLTL---------YPGNYsaYLEQRAERLEQ 247
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
424-640 |
2.45e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 424 FRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSV--QIDGVDVRDLNLEWLRNVVGIVQQE 501
Cdd:PRK13638 9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwQGKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 502 P---ILFNDtIHNNLLF-----GNPDAtrETMIRV---CKMANAHDFiKKMPkgydtqigdggVQ-LSGGQKQRVAIART 569
Cdd:PRK13638 86 PeqqIFYTD-IDSDIAFslrnlGVPEA--EITRRVdeaLTLVDAQHF-RHQP-----------IQcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
432-643 |
3.47e-18 |
|
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: 86.45 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 432 AKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVdvrdlnlewlrnvVGIVQQEPILFNDTIHN 511
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 512 NLLFG-NPDATR-ETMIRVCKManaHDFIKKMPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQ 589
Cdd:cd03291 117 NIIFGvSYDEYRyKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 590 SE-SVVQSALNNASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHEELVNL 643
Cdd:cd03291 194 TEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1091-1277 |
3.77e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1091 YPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlyhlrTQMALVGQEPRLF 1170
Cdd:PRK11248 8 YADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1171 V-GTIRENVCLGLKdvpLEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATS 1249
Cdd:PRK11248 83 PwRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|
gi 1678196980 1250 ALDSESERAVQEALDR--AREGRTCITIAH 1277
Cdd:PRK11248 158 ALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
430-640 |
3.85e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 430 KEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ---QEPI--- 503
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQmifQDPLasl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 504 ----LFNDTIHNNLLFGNPDATRET--------MIRVCKMANahdFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLI 571
Cdd:PRK15079 112 nprmTIGEIIAEPLRTYHPKLSRQEvkdrvkamMLKVGLLPN---LINRYPH-----------EFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1080-1320 |
4.39e-18 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 86.06 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYPQRPHQpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDvTGGALRMDGQDIKNISLYHLRTQ 1159
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MALVGQEPRLFVGTIRENV----CLglKDVPLEKINQALELANAnrfLGNLPDGIDTEVGERGGQLSGGQKQRIAIARAL 1235
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdpygKW--SDEEIWKVAEEVGLKSV---IEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1236 VRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKYFEL 1315
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQA 233
|
....*
gi 1678196980 1316 IKKQD 1320
Cdd:cd03289 234 ISPSD 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
417-642 |
4.69e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.13 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG 496
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEpilfND-----TIHNNLLFG---------NPDATR--ETMIRVCKMAN-AHDFIKkmpkgydtqigdggvQLSGG 559
Cdd:COG4604 79 ILRQE----NHinsrlTVRELVAFGrfpyskgrlTAEDREiiDEAIAYLDLEDlADRYLD---------------ELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 560 QKQRVAIARTLIRDPKVLLLDEATSALD-AQSesvVQ--SALNNAS--KGRTTIMIAHRLS-TIREADKIVFFEKGVIVE 633
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHS---VQmmKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVA 216
|
....*....
gi 1678196980 634 AGNHEELVN 642
Cdd:COG4604 217 QGTPEEIIT 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1110-1306 |
4.83e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.17 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLR----TQMALVGQEPRLFVG-TIRENVCLG--L 1182
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTVLDNTAFGmeL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 KDVPL----EKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERA 1258
Cdd:PRK10070 134 AGINAeerrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1259 VQEALDR--AREGRTCITIAHRL-SSIQNSDLIVYIDDGRVQESGTHKELM 1306
Cdd:PRK10070 203 MQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-640 |
4.98e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.48 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 439 NLTVE-PGTSV-ALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGV------DVRDLNLEWLRNVVGIVQQEPILF-NDTI 509
Cdd:PRK14246 28 DITIKiPNNSIfGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFpHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 510 HNNLLF-----GNPDA------TRETMIRVCKMANAHDfikkmpkgydtQIGDGGVQLSGGQKQRVAIARTLIRDPKVLL 578
Cdd:PRK14246 108 YDNIAYplkshGIKEKreikkiVEECLRKVGLWKEVYD-----------RLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 579 LDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1081-1252 |
5.29e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.21 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1081 NILFENVKFSYPQRphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGM---LERfydVTGGALRMDGQ----------D 1147
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLER---ITSGEIWIGGRvvnelepadrD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1148 I----KNISLY-HLrtqmalvgqeprlfvgTIRENVCLGLKD--VPLEKINQalELANANRFLgnlpdgidtEVGE---- 1216
Cdd:PRK11650 78 IamvfQNYALYpHM----------------SVRENMAYGLKIrgMPKAEIEE--RVAEAARIL---------ELEPlldr 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678196980 1217 RGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PRK11650 131 KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1082-1307 |
5.65e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSY-PQRP-HQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI----KNISLYH 1155
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVGQ--EPRLFVGTIRENVCLGLKD--VP----LEKINQALELAnanrflgnlpdGIDTEVGERGG-QLSGGQK 1226
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSeedaKQKAREMIELV-----------GLPEELLARSPfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1227 QRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHK 1303
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....
gi 1678196980 1304 ELMQ 1307
Cdd:PRK13634 232 EIFA 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1110-1295 |
5.67e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.83 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVT--GGALRMDGQDI----------KNISLYHlrTQMALVgqePRLFVGtirEN 1177
Cdd:PRK13549 31 GEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELqasnirdterAGIAIIH--QELALV---KELSVL---EN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1178 VCLGLKDVPLEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALdSESER 1257
Cdd:PRK13549 103 IFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TESET 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1678196980 1258 AVQEAL--DRAREGRTCITIAHRLSSIQN-SDLIVYIDDGR 1295
Cdd:PRK13549 180 AVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1099-1305 |
8.13e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 84.11 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1099 VMKQLQWTALRGQTVALVGPSGSGKST----CIGMLerfyDVTGGALRMDGQDIKNISLYHL-RTQMALV--GQE--PRL 1169
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDITKLPPHERaRAGIAYVpqGREifPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1170 fvgTIRENVCLGL-------KDVPLEkinqALEL-----ANANRflgnlpdgidtevgeRGGQLSGGQKQRIAIARALVR 1237
Cdd:TIGR03410 91 ---TVEENLLTGLaalprrsRKIPDE----IYELfpvlkEMLGR---------------RGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1238 DPKILLLDEATSALD----SESERAVQEAldRAREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQpsiiKDIGRVIRRL--RAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1094-1306 |
8.58e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.89 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1094 RPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlYHLRTQ---MalVGQE---- 1166
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD-YKYRCKhirM--IFQDpnts 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1167 --PRLFVGTIRenvclglkDVPL------------EKINQALELananrfLGNLPD----GIDTevgerggqLSGGQKQR 1228
Cdd:COG4167 100 lnPRLNIGQIL--------EEPLrlntdltaeereERIFATLRL------VGLLPEhanfYPHM--------LSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1229 IAIARALVRDPKILLLDEATSALDSeSERA--------VQEaldraREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQES 1299
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDM-SVRSqiinlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231
|
....*..
gi 1678196980 1300 GTHKELM 1306
Cdd:COG4167 232 GKTAEVF 238
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
433-633 |
8.71e-18 |
|
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: 84.71 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlEWLRNVVGIVQ--QEPILFND-TI 509
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFPElTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 510 HNNLLFGNPDATRETMIRVCK------------MANAHDFIKKMpkGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVL 577
Cdd:COG0411 97 LENVLVAAHARLGRGLLAALLrlprarreereaRERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 578 LLDEATSALDAQ-SESVVQ--SALnNASKGRTTIMIAHRLSTIRE-ADKIVFFEKG-VIVE 633
Cdd:COG0411 175 LLDEPAAGLNPEeTEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
428-641 |
9.67e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 428 TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPIL-FN 506
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 507 DTIHNNLLFG-NPDATR-----ETMIRVCKMAnahdfikkMPKGYDTQIGDGGV-QLSGGQKQRVAIARTLIRDPKVLLL 579
Cdd:PRK09536 92 FDVRQVVEMGrTPHRSRfdtwtETDRAAVERA--------MERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 580 DEATSALDAQSE-SVVQSALNNASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEELV 641
Cdd:PRK09536 164 DEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1083-1305 |
1.17e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1083 LFENVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMAL 1162
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1163 VGQEP--RLFVGTIRENVCLGLKDVPLEKINQALELANANRFLGNlpdgidTEVGERG-GQLSGGQKQRIAIARALVRDP 1239
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGL------EELRDRVpHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1240 KILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1093-1252 |
1.25e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.91 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1093 QRPHQPVMKQLQWTALRGQTVALVGPSGSGKST----CIGMLERFYDVTGgALRMDGQDIKNISLyHLRtQMALVGQEPR 1168
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFSASG-EVLLNGRRLTALPA-EQR-RIGILFQDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1169 LF----VGtirENVCLGL-KDVPLE----KINQALELAN----ANRFlgnlPDgidtevgerggQLSGGQKQRIAIARAL 1235
Cdd:COG4136 87 LFphlsVG---ENLAFALpPTIGRAqrraRVEQALEEAGlagfADRD----PA-----------TLSGGQRARVALLRAL 148
|
170
....*....|....*..
gi 1678196980 1236 VRDPKILLLDEATSALD 1252
Cdd:COG4136 149 LAEPRALLLDEPFSKLD 165
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
435-624 |
1.68e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN-LEWLRNVVGIVQQEPILFND-TIHNN 512
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFGNPDaTRETMIRvckMANAHDFIKKMPKGY------DTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:COG3845 101 IVLGLEP-TKGGRLD---RKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 587 DAQ-SESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIV 624
Cdd:COG3845 173 TPQeADELFEILRRLAAEGKSIIFITHKLREVMAiADRVT 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
448-652 |
1.87e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 448 VALVGHSGCGKSTSVGLLTRLYE-----PEQGSVQIDGVDVRDLNLE--WLRNVVGIVQQEPILFNDTIHNNLLFG---- 516
Cdd:PRK14243 39 TAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSIYDNIAYGarin 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 517 ----NPDATRETMIRvckMANAHDFIKKmpkgydtQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSES 592
Cdd:PRK14243 119 gykgDMDELVERSLR---QAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 593 VVQSALNNASKGRTTIMIAHRL-STIREADKIVFFekgviveagnHEELVNLGGRYFDLVK 652
Cdd:PRK14243 189 RIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFF----------NVELTEGGGRYGYLVE 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1110-1305 |
1.90e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMalVGQE----PRLfvgTIRENVCLGLKDV 1185
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM--VFQSyalyPHL---SVAENMSFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1186 PLEK--INQALELANANRFLGNLPDgidtevgERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESEraVQEAL 1263
Cdd:PRK11000 104 GAKKeeINQRVNQVAEVLQLAHLLD-------RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678196980 1264 DRA----REGRTCITIAH-RLSSIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK11000 175 EISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
91-581 |
2.05e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.55 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIGLITSVISGVSQP-VLAIISGRMTNVLLVIDPLskefktktmenVYIFLGLGIFvsindfcqYMCFQRVCSRMMT 169
Cdd:COG4615 13 WLLLLALLLGLLSGLANAgLIALINQALNATGAALARL-----------LLLFAGLLVL--------LLLSRLASQLLLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 170 V--------MRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDkLGVLIRGISMVIASvvisLIY----EWR 237
Cdd:COG4615 74 RlgqhavarLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGC----LAYlawlSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 238 LALMMLGLIPVSTICMTLLSRFLEKStgeeLEKVGEA--------GAIAE---ECLMGVRTIQAFNGQEemvakYEKQLN 306
Cdd:COG4615 149 LFLLTLVLLGLGVAGYRLLVRRARRH----LRRAREAedrlfkhfRALLEgfkELKLNRRRRRAFFDED-----LQPTAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 307 SGKKHAIWGGFWSGFFGGIFFFWLMAFMGCgILYGgyLLKVGIIkSPGDVFIIVVAMLLgayflgLISPHLMV------L 380
Cdd:COG4615 220 RYRDLRIRADTIFALANNWGNLLFFALIGL-ILFL--LPALGWA-DPAVLSGFVLVLLF------LRGPLSQLvgalptL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 381 LNARVAAASIYKTIDRVPKIDPYSRHGKKIEKVVG--KVTFENVHFRYPTRKEAK--VLNGLNLTVEPGTSVALVGHSGC 456
Cdd:COG4615 290 SRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 457 GKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDTIHnnlLFGNPDATRetmirvckmanAHD 536
Cdd:COG4615 370 GKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLLG---LDGEADPAR-----------ARE 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1678196980 537 FIKKMPKGYDTQIGDGG---VQLSGGQKQRVAIARTLIRDPKVLLLDE 581
Cdd:COG4615 436 LLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
417-617 |
2.15e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN---LEWLRN 493
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVG-IVQQEPILFNDTIHNNLLFgnP----DATRETMIRvcKMANAHDFIKKMPKGYDTQIgdggvQLSGGQKQRVAIAR 568
Cdd:PRK10908 80 QIGmIFQDHHLLMDRTVYDNVAI--PliiaGASGDDIRR--RVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 569 TLIRDPKVLLLDEATSALD-AQSESVVQSALNNASKGRTTIMIAHRLSTI 617
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1110-1307 |
2.57e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTcIGML----ERfYDVTGGALRMDGQD-----------------------IKNISLYH-LRTQMA 1161
Cdd:COG0396 26 GEVHAIMGPNGSGKST-LAKVlmghPK-YEVTSGSILLDGEDilelspderaragiflafqypveIPGVSVSNfLRTALN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEP---RLFVGTIRENvclgLKDVpleKINQALelanANRFLGnlpdgidteVGerggqLSGGQKQRIAIARALVRD 1238
Cdd:COG0396 104 ARRGEElsaREFLKLLKEK----MKEL---GLDEDF----LDRYVN---------EG-----FSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALDRAR-EGRTCITIAH--RLSSIQNSDLIVYIDDGRVQESGThKELMQ 1307
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELAL 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
433-689 |
3.27e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.78 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLL--TRLYEPEQGSV---------------------------------Q 477
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvgepcpvcggtlepeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 478 IDGVDVRDLNLEWLRNVVGIVQQEPILF--NDTIHNNLLFGNPDATRETMIRVCKmanAHDFIKKMPKGYdtQIGDGGVQ 555
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGR---AVDLIEMVQLSH--RITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 556 LSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIV 632
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWLENGEIK 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 633 EAGNHEELVNlggRYFDLVKaqafkqdpdeiALEKEEEdqfDEFDKPTVFNRKVSVR 689
Cdd:TIGR03269 249 EEGTPDEVVA---VFMEGVS-----------EVEKECE---VEVGEPIIKVRNVSKR 288
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1060-1260 |
4.40e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1060 LINRQPQtGD---LKSGTKPEIRgnilFENVKFSYPQRP--------HQPVMKQLQWTALRGQTVALVGPSGSGKSTCIG 1128
Cdd:PRK15134 256 LLNSEPS-GDpvpLPEPASPLLD----VEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1129 MLERFYDvTGGALRMDGQDIKNIS---LYHLRTQMALVGQEP------RLFVGTIRENvclGLKdVPLEKINQALELANA 1199
Cdd:PRK15134 331 ALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPnsslnpRLNVLQIIEE---GLR-VHQPTLSAAQREQQV 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1200 NRFLGNLpdGIDTEVGER-GGQLSGGQKQRIAIARALVRDPKILLLDEATSALDseseRAVQ 1260
Cdd:PRK15134 406 IAVMEEV--GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQ 461
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
433-660 |
4.70e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN-------LEWLRNVV----GIVQQE 501
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsrqlarrLALLPQHHltpeGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 502 PILFNDTIHNNLlFGNPDATRETMIRvckmanahdfiKKMPKGYDTQIGDGGV-QLSGGQKQRVAIARTLIRDPKVLLLD 580
Cdd:PRK11231 96 LVAYGRSPWLSL-WGRLSAEDNARVN-----------QAMEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 581 EATSALDA--QSE--SVVQSaLNNasKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEELVN--LGGRYFDlVKA 653
Cdd:PRK11231 164 EPTTYLDInhQVElmRLMRE-LNT--QGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTpgLLRTVFD-VEA 239
|
....*..
gi 1678196980 654 QAFkQDP 660
Cdd:PRK11231 240 EIH-PEP 245
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
420-638 |
5.03e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.04 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRyPTRKEakVLNGLNLTVEPGTSVALVGHSGCGKSTsvglLTRL------YEPEQGSVQIDGVDVRDL------- 486
Cdd:COG0396 4 KNLHVS-VEGKE--ILKGVNLTIKPGEVHAIMGPNGSGKST----LAKVlmghpkYEVTSGSILLDGEDILELspderar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 487 -----------------NLEWLRNVVGIVQQEPI---LFNDTIhnnllfgnpdatRETMIRVcKMANahDFIKKmpkgyd 546
Cdd:COG0396 77 agiflafqypveipgvsVSNFLRTALNARRGEELsarEFLKLL------------KEKMKEL-GLDE--DFLDR------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 547 tQIGDGgvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAH--RLSTIREADKI 623
Cdd:COG0396 136 -YVNEG---FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFV 211
|
250
....*....|....*
gi 1678196980 624 VFFEKGVIVEAGNHE 638
Cdd:COG0396 212 HVLVDGRIVKSGGKE 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
423-632 |
5.80e-17 |
|
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: 81.61 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 423 HFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQ-- 500
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQkt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 501 ---------EPILFNDTIHNNllfgNPDATRETMIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLI 571
Cdd:cd03267 105 qlwwdlpviDSFYLLAAIYDL----PPARFKKRLDELSELLDLEELLDTPVR-----------QLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 572 RDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTI-READKIVFFEKGVIV 632
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKeyNRERGTTVLLTSHYMKDIeALARRVLVIDKGRLL 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1109-1246 |
5.82e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCigmlerFYDVTG------GALRMDGQDIKNISLyHLRTQMALvG---QEPRLFVG-TIRENV 1178
Cdd:COG1137 28 QGEIVGLLGPNGAGKTTT------FYMIVGlvkpdsGRIFLDGEDITHLPM-HKRARLGI-GylpQEASIFRKlTVEDNI 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1179 --CLGLKDVPLEKINQALElananRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDE 1246
Cdd:COG1137 100 laVLELRKLSKKEREERLE-----ELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
761-1020 |
5.93e-17 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 82.98 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 761 MLIGLSAALIRGLDLPTFALLFAWVFEGFEfvpyGGKMMHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIVSENLGVRFRV 840
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI----PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 841 AAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFINCWQVAILGTALIFLLGF 920
Cdd:cd07346 77 DLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 921 IMAGLAFKISIVAAEHME-NDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKRKRTELRKSVYEAVNYCISQNFMY 999
Cdd:cd07346 155 ILRYFRRRIRKASREVREsLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260
....*....|....*....|.
gi 1678196980 1000 YMSCFCFALAIRIINQGDQTV 1020
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTI 255
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1099-1305 |
6.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1099 VMKQLQWTALRGQTVALVGPSGSGKSTCI----GML---------ERFY-----DVTGGALRMDGQDIKNISlyHLRTQM 1160
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLIkskygtiqvGDIYigdkkNNHELITNPYSKKIKNFK--ELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1161 ALVGQEP--RLFVGTIRENVCLGLKDVPLEKiNQALELANanRFLGNLpdGIDTEVGERGG-QLSGGQKQRIAIARALVR 1237
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFGPVALGVKK-SEAKKLAK--FYLNKM--GLDDSYLERSPfGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1238 DPKILLLDEATSALDSESERA-VQEALDRAREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
428-642 |
6.93e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 428 TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSV----GLLTRLYEPEQ------GSVQIDGVDVRDLNLEwlRNVVGI 497
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGShiellgRTVQREGRLARDIRKS--RANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 498 VQQEPILFND-TIHNNLLFGNPDATR--ETMIRVCKMANAHDFIKKMPKGYDTQIGDGGVQ-LSGGQKQRVAIARTLIRD 573
Cdd:PRK09984 91 IFQQFNLVNRlSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVStLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 574 PKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDN 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
417-629 |
7.41e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.64 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVdvrdlnlewlrnvvg 496
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 ivqqepilfndtihnnllfgnpdatretmIRVCKMAnahdfikkmpkgydtqigdggvQLSGGQKQRVAIARTLIRDPKV 576
Cdd:cd03221 63 -----------------------------VKIGYFE----------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNasKGRTTIMIAH-R--LSTIreADKIVFFEKG 629
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1082-1307 |
7.58e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.93 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlYHLRTQMA 1161
Cdd:PRK13537 8 IDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRL---FvgTIRENVCL-----GLKDVPL-EKINQALELANanrflgnLPDGIDTEVGErggqLSGGQKQRIAIA 1232
Cdd:PRK13537 84 VVPQFDNLdpdF--TVRENLLVfgryfGLSAAAArALVPPLLEFAK-------LENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESERAVQEALDR--AReGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
420-581 |
7.65e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTS----VGLLTrlyePEQGSVQIDGVDVRDLNLeWLRNVV 495
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLPM-HKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 GI--VQQEPILFND-TIHNNLL-----FGNPDATREtmirvcKMANA--HDF----IKKMPkgydtqigdgGVQLSGGQK 561
Cdd:COG1137 79 GIgyLPQEASIFRKlTVEDNILavlelRKLSKKERE------ERLEEllEEFgithLRKSK----------AYSLSGGER 142
|
170 180
....*....|....*....|
gi 1678196980 562 QRVAIARTLIRDPKVLLLDE 581
Cdd:COG1137 143 RRVEIARALATNPKFILLDE 162
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1085-1307 |
7.71e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVG 1164
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QE-PRLFVGTIRENVCLG----------LKDVPLEKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIAR 1233
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESE---RAVQEALDRAReGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQvdvLALVHRLSQER-GLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1096-1301 |
1.12e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1096 HQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISL---YHLRTQ-MALVGQEPRLFV 1171
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1172 G-TIRENVCLGL---KDVPLEKINQALELANANrflgnlpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEA 1247
Cdd:PRK11629 101 DfTALENVAMPLligKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 1248 TSALDSESERAVQEALDR--AREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGT 1301
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
434-638 |
1.20e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDlNLEWLRNVVGIVQQepilFND-----T 508
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FDNldlefT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 509 IHNNLL-----FGNPDATRETMIrvckmANAHDFIKKMPKGyDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEAT 583
Cdd:PRK13536 131 VRENLLvfgryFGMSTREIEAVI-----PSLLEFARLESKA-DARVSD----LSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 584 SALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTI-READKIVFFEKGV-IVEAGNHE 638
Cdd:PRK13536 201 TGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRkIAEGRPHA 258
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1082-1307 |
1.47e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYpqRPHQPVMKQ----LQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS----L 1153
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASRalfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1154 YHLRTQMALVGQEP--RLFVGTIRENVCLGLKDVPLEKiNQALELANANRFLGnlpdGIDTEVGERGG-QLSGGQKQRIA 1230
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMV----GLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1231 IARALVRDPKILLLDEATSALDSESERAVQEALDRARE-GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
93-303 |
1.50e-16 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 81.68 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQPVLAIISGRMTNVLLVIDPLSKEFKTKTMenVYIFLGLGIFVSINDFCQY---MCFQRVCSRMMT 169
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGL--LRILLLLLGLYLLSALFSYlqnRLMARVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 170 VMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVS 249
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 250 TICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEK 303
Cdd:cd18547 159 LLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDE 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
429-612 |
1.90e-16 |
|
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: 79.46 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 429 RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDT 508
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 509 IHNNLLFGNPDATRETmirvCKMANAhdfikkmpkgydtQIGDGGV------QLSGGQKQRVAIARTLIRDPKVLLLDEA 582
Cdd:cd03231 90 VLENLRFWHADHSDEQ----VEEALA-------------RVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 1678196980 583 TSALDAQSESVVQSAL-NNASKGRTTIMIAH 612
Cdd:cd03231 153 TTALDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
417-655 |
2.00e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAK-------------------VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQ 477
Cdd:COG1134 5 IEVENVSKSYRLYHEPSrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 478 IDGvdvrdlNLEWLRNV-VGIVQQ----EPILFNDTIHnnllfG-NPDATRETMIRVCKMANAHDFIkKMP-KGYdtqig 550
Cdd:COG1134 85 VNG------RVSALLELgAGFHPEltgrENIYLNGRLL-----GlSRKEIDEKFDEIVEFAELGDFI-DQPvKTY----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 551 dggvqlSGGQKQRVAIARTLIRDPKVLLLDEATSALDA--QSESvvQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFF 626
Cdd:COG1134 148 ------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafQKKC--LARIRElRESGRTVIFVSHSMGAVRRlCDRAIWL 219
|
250 260
....*....|....*....|....*....
gi 1678196980 627 EKGVIVEAGNHEELVNlggRYFDLVKAQA 655
Cdd:COG1134 220 EKGRLVMDGDPEEVIA---AYEALLAGRE 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
434-612 |
2.34e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.82 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEW---LR-NVVGIVQQEPILFN--D 507
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFVFQSFMLIPtlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 508 TIHN----NLLFGNPDA-TRETMIRVCKMANAHDFIKKMPkgydtqigdggVQLSGGQKQRVAIARTLIRDPKVLLLDEA 582
Cdd:PRK10584 105 ALENvelpALLRGESSRqSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|..
gi 1678196980 583 TSALDAQSESVVQSALN--NASKGRTTIMIAH 612
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFslNREHGTTLILVTH 205
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
423-640 |
2.89e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.27 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 423 HFRYPT----RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIV 498
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQEPilfNDTIHNNLLFG---------NPDAT---RETMI-----RVCKMANAHDFIKKMpkgydtqigdggvqLSGGQK 561
Cdd:COG4167 93 FQDP---NTSLNPRLNIGqileeplrlNTDLTaeeREERIfatlrLVGLLPEHANFYPHM--------------LSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 562 QRVAIARTLIRDPKVLLLDEATSALDAQsesvVQSALNN------ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEA 634
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMS----VRSQIINlmlelqEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231
|
....*.
gi 1678196980 635 GNHEEL 640
Cdd:COG4167 232 GKTAEV 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
420-642 |
2.91e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRYPTRK--------EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYePEQGSVQIDGVDVRDLNLEWL 491
Cdd:PRK15134 279 EQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 ---RNVVGIVQQEPilfndtihNNLLfgNPDATRETMI----RV-CKMANAHD----FIKKMPK-GYDTQIGDG-GVQLS 557
Cdd:PRK15134 358 lpvRHRIQVVFQDP--------NSSL--NPRLNVLQIIeeglRVhQPTLSAAQreqqVIAVMEEvGLDPETRHRyPAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 558 GGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGR--TTIMIAHRLSTIRE-ADKIVFFEKGVIVEA 634
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQ 507
|
....*...
gi 1678196980 635 GNHEELVN 642
Cdd:PRK15134 508 GDCERVFA 515
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
417-613 |
3.45e-16 |
|
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: 77.58 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvdvrdlnlewlRNVVG 496
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILfndtihnnllfgnPDAT-RETMIRVCKMAnahdfikkmpkgydtqigdggvqLSGGQKQRVAIARTLIRDPK 575
Cdd:cd03223 68 FLPQRPYL-------------PLGTlREQLIYPWDDV-----------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678196980 576 VLLLDEATSALDAQSESVVQSALNnaSKGRTTIMIAHR 613
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1109-1295 |
4.31e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYH-LRTQMALVGQE----PRLfvgTIRENVCLGLK 1183
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TVAENLYLGQL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1184 DVPLEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDS-ESER--AVQ 1260
Cdd:PRK11288 106 PHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQlfRVI 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678196980 1261 EALdRArEGRTCITIAHRLSSI-QNSDLIVYIDDGR 1295
Cdd:PRK11288 184 REL-RA-EGRVILYVSHRMEEIfALCDAITVFKDGR 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-640 |
4.34e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEP-----EQGSVQIDGVDV---RDLnLEWLRNVvGIVQQEPILF 505
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LEFRRRV-GMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 506 NDTIHNNLLFGnpdatretmIRVCKMANAHDFiKKMPKGYDTQIG----------DGGVQLSGGQKQRVAIARTLIRDPK 575
Cdd:PRK14271 114 PMSIMDNVLAG---------VRAHKLVPRKEF-RGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 576 VLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1109-1305 |
5.17e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.81 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKS----TCIGMLERFYDVTGGALRMDGQDIKNISLYHLRT----QMALVGQEPR-----LF-VGT- 1173
Cdd:COG4172 35 AGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMtslnpLHtIGKq 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1174 IRENVCL--GLKDVPLEKinQALEL------ANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLD 1245
Cdd:COG4172 115 IAEVLRLhrGLSGAAARA--RALELlervgiPDPERRLDAYPH-----------QLSGGQRQRVMIAMALANEPDLLIAD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1246 EATSALDSeserAVQ-EALD-----RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:COG4172 182 EPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1093-1306 |
5.17e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.83 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1093 QRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIkNISLYHLRTQ-MALVGQE----- 1166
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQrIRMIFQDpstsl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1167 -PRLFVGTIRenvclglkDVPL------------EKINQALelananRFLGNLPDgidtEVGERGGQLSGGQKQRIAIAR 1233
Cdd:PRK15112 101 nPRQRISQIL--------DFPLrlntdlepeqreKQIIETL------RQVGLLPD----HASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 1234 ALVRDPKILLLDEATSALD-SESERAVQEALD-RAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELM 1306
Cdd:PRK15112 163 ALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
434-640 |
5.77e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNlEWLRNVVGI--VQQEPILF-NDTIH 510
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 511 NNLLFGNPdATRETMIRVckmanaHDFIKKMPKGYDTQIGDGGVQLSggQKQRVAIARTLIRDPKVLLLDEATSALD-AQ 589
Cdd:PRK15439 105 ENILFGLP-KRQASMQKM------KQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTpAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 590 SESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
407-641 |
5.81e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 407 GKKIEKVvgkvtfENVHFRYPT--RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQ------- 477
Cdd:TIGR03269 276 GEPIIKV------RNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 478 IDGVDVRDLNLEWLRNVVGIVQQEPILF-NDTIHNNLL----FGNPD--ATRETMIrVCKMAN-----AHDFIKKMPKgy 545
Cdd:TIGR03269 350 VDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNLTeaigLELPDelARMKAVI-TLKMVGfdeekAEEILDKYPD-- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 546 dtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADK 622
Cdd:TIGR03269 427 ---------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDR 497
|
250
....*....|....*....
gi 1678196980 623 IVFFEKGVIVEAGNHEELV 641
Cdd:TIGR03269 498 AALMRDGKIVKIGDPEEIV 516
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1078-1276 |
7.11e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1078 IRGN-ILFENVKFsypqrphqpvmkqlqwTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIkniSLYHL 1156
Cdd:PRK13539 11 VRGGrVLFSGLSF----------------TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1157 RTQMALVGQ----EPRLfvgTIRENV-----CLGLKDVPLEKINQALELANanrfLGNLPdgidtevgerGGQLSGGQKQ 1227
Cdd:PRK13539 72 AEACHYLGHrnamKPAL---TVAENLefwaaFLGGEELDIAAALEAVGLAP----LAHLP----------FGYLSAGQKR 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678196980 1228 RIAIARALVRDPKILLLDEATSALDSESERAVQEALdRAREGRTCITIA 1276
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1098-1309 |
7.17e-16 |
|
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: 83.42 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1098 PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQdiknislyhlrtqMALVGQEPRLFVGTIREN 1177
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1178 VCLGLK--DVPLEKINQALELANAnrfLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSES 1255
Cdd:TIGR01271 507 IIFGLSydEYRYTSVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1256 ERAVQEA-LDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLK 1309
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
418-642 |
7.21e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 418 TFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLE-WLRNVVG 496
Cdd:PRK10575 13 ALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILFNDTI-----------HNNL-LFGNPDATR--ETMIRVCKMANAHDFIKkmpkgydtqigdggvQLSGGQKQ 562
Cdd:PRK10575 90 LPQQLPAAEGMTVrelvaigrypwHGALgRFGAADREKveEAISLVGLKPLAHRLVD---------------SLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 563 RVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNAS--KGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEE 639
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAE 234
|
...
gi 1678196980 640 LVN 642
Cdd:PRK10575 235 LMR 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1109-1305 |
9.64e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.49 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlYHLRTQMALVG--QEPRLFVG-TIRENVCL----- 1180
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFREmTVIENLLVaqhqq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 -------GLKDVP---------LEKINQALE----LANANRFLGNlpdgidtevgerggqLSGGQKQRIAIARALVRDPK 1240
Cdd:PRK11300 109 lktglfsGLLKTPafrraeseaLDRAATWLErvglLEHANRQAGN---------------LAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1241 ILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
438-652 |
1.08e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.14 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 438 LNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVrDLNLEWLRNVVGIVQQEPILFND-TIHNNLLFG 516
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 517 NPDATR---ETMIRVCKMANahdfikkmPKGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESV 593
Cdd:TIGR01257 1028 AQLKGRsweEAQLEMEAMLE--------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 594 VQSALNNASKGRTTIMIAHRLStirEA----DKIVFFEKGVIVEAGNHEELVNL--GGRYFDLVK 652
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIISQGRLYCSGTPLFLKNCfgTGFYLTLVR 1161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
417-640 |
1.29e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.00 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvdvRDLNLEwLRNVVG 496
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPE-DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEPILF-NDTIHNNLLF-------GNPDATRET---MIRVCKMANAHDFIKKmpkgydtqigdggvqLSGGQKQRVA 565
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlarlkglSKAEAKRRAdewLERLGLGDRANKKVEE---------------LSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 566 IARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEEL 640
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
417-635 |
1.30e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.57 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPT-------------------RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQ 477
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 478 IDGvDVR---DLNLEWLRNVVGIvqqEPILFNDTIHNNllfgNPDATRETMIRVCKMANAHDFIKKMPKGYdtqigdggv 554
Cdd:cd03220 81 VRG-RVSsllGLGGGFNPELTGR---ENIYLNGRLLGL----SRKEIDEKIDEIIEFSELGDFIDLPVKTY--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 qlSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIV 632
Cdd:cd03220 144 --SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
...
gi 1678196980 633 EAG 635
Cdd:cd03220 222 FDG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1076-1298 |
1.38e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1076 PEIRGNILF--ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLerfydvtGGALRMDGQDIKnisl 1153
Cdd:COG0488 308 PERLGKKVLelEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL-------AGELEPDSGTVK---- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1154 YHLRTQMALVGQEPRLFVG--TIRENVCLGLKDVPLEKINQALElananRFLGNlPDGIDTEVGErggqLSGGQKQRIAI 1231
Cdd:COG0488 374 LGETVKIGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLG-----RFLFS-GDDAFKPVGV----LSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1232 ARALVRDPKILLLDEATSALDSESERAVQEALDrAREGrTCITIAH-R--LSSIQNSdlIVYIDDGRVQE 1298
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRVATR--ILEFEDGGVRE 509
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
420-635 |
1.55e-15 |
|
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: 76.41 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFRyptRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTsvgLLTRL-----YEPEQGSVQIDGVDVRDLNL-EWLRN 493
Cdd:cd03217 4 KDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITDLPPeERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 494 VVGIVQQEPILFndtihnnllfgnpdatreTMIRVckmanaHDFIKKMPKGydtqigdggvqLSGGQKQRVAIARTLIRD 573
Cdd:cd03217 78 GIFLAFQYPPEI------------------PGVKN------ADFLRYVNEG-----------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 574 PKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAH--RLSTIREADKIVFFEKGVIVEAG 635
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1097-1318 |
1.57e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.75 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNiSLYHLRTQMALVGQEPRLFVG-TIR 1175
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCL--GLKDVPLEKINQALElananrflGNLPD-GIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:TIGR01257 1022 EHILFyaQLKGRSWEEAQLEME--------AMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 1253 SESERAVQEALDRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQL--KGKYFELIKK 1318
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNCfgTGFYLTLVRK 1162
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
416-588 |
1.82e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.50 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 416 KVTFENVHFRYPTRKEakVLNGLNLTVEPGTSVALVGHSGCGKSTsvglLTR----LYEPEQGSVQIDGVDVRDLnlewl 491
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKST----LLRmvagLERITSGEIWIGGRVVNEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 rnvvgivqqEP------ILFND-------TIHNNLLFG-----NPDATRETMIR-VCKMANAHDFIKKMPKgydtqigdg 552
Cdd:PRK11650 72 ---------EPadrdiaMVFQNyalyphmSVRENMAYGlkirgMPKAEIEERVAeAARILELEPLLDRKPR--------- 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678196980 553 gvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDA 588
Cdd:PRK11650 134 --ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1098-1300 |
1.85e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1098 PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNIS--LYHlrtQMA--LVGQEPRLFVG- 1172
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpaKAH---QLGiyLVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1173 TIRENVCLGL--KDVPLEKINQALELANANrflgnlpdgIDTEVgeRGGQLSGGQKQRIAIARALVRDPKILLLDEATSA 1250
Cdd:PRK15439 102 SVKENILFGLpkRQASMQKMKQLLAALGCQ---------LDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1251 LD-SESERAVQEALDRAREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESG 1300
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1110-1308 |
1.99e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.25 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGML--------ERFYDVTGGALRMDGQDIKNISLYhlrtqmalvGQEPRLFVG--TIRENVC 1179
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALafrspkgvKGSGSVLLNGMPIDAKEMRAISAY---------VQQDDLFIPtlTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 L---------GLKDVPLEKINQALELANanrflgnLPDGIDTEVGERGGQ--LSGGQKQRIAIARALVRDPKILLLDEAT 1248
Cdd:TIGR00955 122 FqahlrmprrVTKKEKRERVDEVLQALG-------LRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1249 SALDSESERAVQEALDR-AREGRTCITIAHRLSS--IQNSDLIVYIDDGRVQESGTHKELMQL 1308
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1110-1307 |
2.05e-15 |
|
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: 76.41 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERF--YDVTGGALRMDGQDIKNISLYH-LRTQMALVGQEPRLFVGtirenvclglkdvp 1186
Cdd:cd03217 26 GEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPG-------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 lekinqaleLANANrFLGNLPDGidtevgerggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRA 1266
Cdd:cd03217 92 ---------VKNAD-FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678196980 1267 R-EGRTCITIAH--RLSSIQNSDLIVYIDDGRVQESGThKELMQ 1307
Cdd:cd03217 151 ReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELAL 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1084-1296 |
2.63e-15 |
|
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: 76.17 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYpqRPHQpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKnislYHLRTQMALV 1163
Cdd:cd03269 3 VENVTKRF--GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPRLFVG-TIREN-VCLG-LKDVPLEKInqaleLANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPK 1240
Cdd:cd03269 76 PEERGLYPKmKVIDQlVYLAqLKGLKKEEA-----RRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1241 ILLLDEATSALDSESERAVQEAL-DRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
122-367 |
2.68e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 78.12 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 122 LVIDPLSKEFKTKTMENVYIFLGLGIFVSinDFCQYM---CFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTR 198
Cdd:cd18784 21 QVIDGIVIEKSQDKFSRAIIIMGLLAIAS--SVAAGIrggLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 199 LNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIA 278
Cdd:cd18784 99 LTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 279 EECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAIWGGFWSGFFGGIFFFWLMAFMGCGILYGGYLLKVGIIKSPGDVFI 358
Cdd:cd18784 179 EETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISF 258
|
....*....
gi 1678196980 359 IVVAMLLGA 367
Cdd:cd18784 259 ILYQLELGS 267
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
438-639 |
3.50e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 438 LNLTVEPGTSVALVGHSGCGKSTsvgLLTRL--YEPEQGSVQIDGVDVRDLNLEWLRNVVG-IVQQEPILFNDTIHNNLL 514
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 515 FGNPDATRETMIR-----VCKMANAHDFIKKMpkgydtqIGdggvQLSGGQKQRVAIA-------RTLIRDPKVLLLDEA 582
Cdd:PRK03695 92 LHQPDKTRTEAVAsalneVAEALGLDDKLGRS-------VN----QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 583 TSALD-AQsesvvQSALNN-----ASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEE 639
Cdd:PRK03695 161 MNSLDvAQ-----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1096-1305 |
4.20e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1096 HQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGML----------ERFYDVTGGALRMDGQDIKNISlyHLRTQMALVGQ 1165
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLARDIR--KSRANTGYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1166 EPRLFVG-TIRENVCLG-LKDVPLEKIN-QALELANANRFLGNLpdgidTEVG------ERGGQLSGGQKQRIAIARALV 1236
Cdd:PRK09984 94 QFNLVNRlSVLENVLIGaLGSTPFWRTCfSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1237 RDPKILLLDEATSALDSESERAVQEALD--RAREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1109-1322 |
4.81e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.46 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ-----DIKNI-------SLYhlrtqmalvgqePRLfvgTIRE 1176
Cdd:COG4152 26 KGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpeDRRRIgylpeerGLY------------PKM---KVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1177 N-VCLG-LKDVPLEKINQALE--LAnanRFlgNLPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:COG4152 91 QlVYLArLKGLSKAEAKRRADewLE---RL--GLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1253 SESERAVQEAL-DRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL-MQLKGKYFELIKKQDLA 1322
Cdd:COG4152 162 PVNVELLKDVIrELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIrRQFGRNTLRLEADGDAG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1110-1300 |
5.11e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.77 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCI----GMLERFYdVTGGALRMDGQDIKnislyhlRTQM----ALVGQEPRLFVG-TIREN--- 1177
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLdaisGRVEGGG-TTSGQILFNGQPRK-------PDQFqkcvAYVRQDDILLPGlTVRETlty 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1178 -VCLGLKDVPLEKINQALELANANRFLGNLPDGidtevGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESE 1256
Cdd:cd03234 105 tAILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678196980 1257 RAVQEALDR-AREGRTCITIAH--RLSSIQNSDLIVYIDDGRVQESG 1300
Cdd:cd03234 180 LNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1106-1307 |
5.39e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1106 TALRGQTVALVGPSGSGKSTCI----GMLErfydvTGGALRMDGQDIKNISLYHLRTQMA-LVGQEPRLFVGTIRENVCL 1180
Cdd:COG4138 18 QVNAGELIHLIGPNGAGKSTLLarmaGLLP-----GQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 GLKD-VPLEKINQAL-ELANAnrfLGnLPDGIDTEVgergGQLSGGQKQRIAIARALVR-------DPKILLLDEATSAL 1251
Cdd:COG4138 93 HQPAgASSEAVEQLLaQLAEA---LG-LEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1252 DSeserAVQEALDR-----AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:COG4138 165 DV----AQQAALDRllrelCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
434-641 |
5.53e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.56 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFND-TIHNN 512
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFG----NPDATR---ETMIRVCKMANAHDFIKKMPKGYDTqigdggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSA 585
Cdd:PRK10253 102 VARGryphQPLFTRwrkEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 586 LDAQSESVVQSALN--NASKGRTTIMIAHRLS-TIREADKIVFFEKGVIVEAGNHEELV 641
Cdd:PRK10253 174 LDISHQIDLLELLSelNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1086-1309 |
6.37e-15 |
|
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: 76.82 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1086 NVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQdiknislyhlrtqMALVGQ 1165
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1166 EPRLFVGTIRENVCLGLK--DVPLEKINQALELANAnrfLGNLPDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILL 1243
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSydEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1244 LDEATSALDSESERAVQEA-LDRAREGRTCITIAHRLSSIQNSDLIVYIDDGRVQESGTHKELMQLK 1309
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
429-637 |
7.13e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.38 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 429 RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDvrdlnLEWLRNVVGIvqqEPILFNDT 508
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPD-----NQFGREASLI---DAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 509 IhnnllfgnPDATRetMIRVCKMANAHDFIKKmpkgYDtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDA 588
Cdd:COG2401 112 F--------KDAVE--LLNAVGLSDAVLWLRR----FK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 589 QSESVVQSALNNASK--GRTTIMIAHRlSTIREA---DKIVFFEKGVIVEAGNH 637
Cdd:COG2401 170 QTAKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPEEKRR 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
434-642 |
7.24e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKS-TSVGLLTRLYEPE----QGSVQIDGVDVRDLNLEWLRNVVG----IVQQEPIL 504
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 505 FNDTIHN---------NLLFG-NPDATRETMIRVCKMANahdfIKKMPKgydtQIGDGGVQLSGGQKQRVAIARTLIRDP 574
Cdd:PRK15134 104 SLNPLHTlekqlyevlSLHRGmRREAARGEILNCLDRVG----IRQAAK----RLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1110-1322 |
1.29e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.51 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHlRTQM-ALVGQEPRLfvGT-----IRENVCL--- 1180
Cdd:COG1101 32 GDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKYiGRVFQDPMM--GTapsmtIEENLALayr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 -----GLKdvplekinQALELANANRF------LGN-LPDGIDTEVGerggQLSGGQKQRIAIARALVRDPKILLLDEAT 1248
Cdd:COG1101 109 rgkrrGLR--------RGLTKKRRELFrellatLGLgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1249 SALDSESERAVQEALDR--AREGRTCITIAHRLS-SIQNSDLIVYIDDGRV--QESGTHKELMQLKG--KYFELIKKQDL 1321
Cdd:COG1101 177 AALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRIilDVSGEEKKKLTVEDllELFEEIRGEEL 256
|
.
gi 1678196980 1322 A 1322
Cdd:COG1101 257 A 257
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1110-1305 |
1.68e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKST----CIGMLErfydVTGGALRMDGQDIKNISLYHLRT-----QM----ALVGQEPRLFVG-TIR 1175
Cdd:PRK15079 47 GETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMKDDEWRAvrsdiQMifqdPLASLNPRMTIGeIIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCLGLKDVPLEKINQalELANANRFLGNLPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSES 1255
Cdd:PRK15079 123 EPLRTYHPKLSRQEVKD--RVKAMMLKVGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1256 ERAVQEAL-DRARE-GRTCITIAHRLSSIQN-SD--LIVYIddGRVQESGTHKEL 1305
Cdd:PRK15079 197 QAQVVNLLqQLQREmGLSLIFIAHDLAVVKHiSDrvLVMYL--GHAVELGTYDEV 249
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1095-1307 |
1.70e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1095 PHQPVMKQLQWTALRGQTVALVGPSGSGKS-TC---IGMLERFYDVTGGALRMDGQDIkniSLYHLR-TQMALVGQEPR- 1168
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCaaaLGILPAGVRQTAGRVLLDGKPV---APCALRgRKIATIMQNPRs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1169 LF--VGTIRENV---CLGL-KDVPLEKINQALE---LANANRFLGNLPdgidtevgergGQLSGGQKQRIAIARALVRDP 1239
Cdd:PRK10418 91 AFnpLHTMHTHAretCLALgKPADDATLTAALEavgLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1240 KILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
423-667 |
1.76e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.28 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 423 HFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVvGIV---- 498
Cdd:COG4586 26 GLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 499 QQepiLFND--TIHNNLLFGN----PDAT-RETMIRVCKMANAHDFIKKMpkgydtqigdggV-QLSGGQKQRVAIARTL 570
Cdd:COG4586 105 SQ---LWWDlpAIDSFRLLKAiyriPDAEyKKRLDELVELLDLGELLDTP------------VrQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 571 IRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVNLGGRY 647
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
250 260
....*....|....*....|
gi 1678196980 648 fDLVKAQaFKQDPDEIALEK 667
Cdd:COG4586 250 -KTIVLE-LAEPVPPLELPR 267
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1081-1321 |
1.84e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1081 NIL-FENVKFSYPQRPHqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ--DIKNISLYHLR 1157
Cdd:PRK13636 4 YILkVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1158 TQMALVGQEP--RLFVGTIRENVCLGLKD--VPLEKINQALELANANRFLGNLPDgidtevgERGGQLSGGQKQRIAIAR 1233
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGAVNlkLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1234 ALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQ-NSDLIVYIDDGRVQESGTHKELMQLKg 1310
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK- 233
|
250
....*....|.
gi 1678196980 1311 kyfELIKKQDL 1321
Cdd:PRK13636 234 ---EMLRKVNL 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1109-1296 |
2.04e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ--DIKNislyhlrTQMAL------VGQEPRLF-VGTIRENVC 1179
Cdd:COG3845 30 PGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-------PRDAIalgigmVHQHFMLVpNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 LGLKDVPLEKINqaleLANANRFLGNLPD--GIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSAL-DSESE 1256
Cdd:COG3845 103 LGLEPTKGGRLD----RKAARARIRELSEryGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEAD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678196980 1257 RaVQEALDR-AREGRTCITIAHRLSSI-QNSDLIVYIDDGRV 1296
Cdd:COG3845 179 E-LFEILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1056-1307 |
2.65e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1056 QMFNLINRQPQTGDLKSGTKPEIRGnilFENVKFSYpqrphqpvmkqlqWTalrGQTVALVGPSGSGKSTCIGMLERFYD 1135
Cdd:PRK10261 315 QVRNLVTRFPLRSGLLNRVTREVHA---VEKVSFDL-------------WP---GETLSLVGESGSGKSTTGRALLRLVE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1136 VTGGALRMDGQDIKNIS---LYHLRTQMALVGQEP------RLFVG-TIREnvclglkdvPLeKINQALELANANRFLGN 1205
Cdd:PRK10261 376 SQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldpRQTVGdSIME---------PL-RVHGLLPGKAAAARVAW 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1206 LPD--GIDTEVGER-GGQLSGGQKQRIAIARALVRDPKILLLDEATSALD-SESERAVQEALDRARE-GRTCITIAHRLS 1280
Cdd:PRK10261 446 LLErvGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINLLLDLQRDfGIAYLFISHDMA 525
|
250 260
....*....|....*....|....*...
gi 1678196980 1281 SIQN-SDLIVYIDDGRVQESGTHKELMQ 1307
Cdd:PRK10261 526 VVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1061-1277 |
2.86e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1061 INRQPQTG----DLKSGTKPEIRgnILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLerfydv 1136
Cdd:PRK13536 19 IERKHQGIseakASIPGSMSTVA--IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMI------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1137 tggaLRMDGQDIKNISLYHL---------RTQMALVGQEPRL---FvgTIRENVCL-----GLKDVPLEK-INQALELAN 1198
Cdd:PRK13536 88 ----LGMTSPDAGKITVLGVpvpararlaRARIGVVPQFDNLdleF--TVRENLLVfgryfGMSTREIEAvIPSLLEFAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1199 anrflgnLPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALdRA--REGRTCITIA 1276
Cdd:PRK13536 162 -------LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL-RSllARGKTILLTT 229
|
.
gi 1678196980 1277 H 1277
Cdd:PRK13536 230 H 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1080-1321 |
3.50e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.66 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYPQR-PHQpvMKQLQWTALR---GQTVALVGPSGSGKSTCI----GML--ERFYDVTGG-ALRMDGQDI 1148
Cdd:PRK13645 5 KDIILDNVSYTYAKKtPFE--FKALNNTSLTfkkNKVTCVIGTTGSGKSTMIqltnGLIisETGQTIVGDyAIPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1149 KNISlyHLRTQMALVGQEP--RLFVGTIRENVCLGL------KDVPLEKINQALELANanrflgnLPDgidtEVGERGG- 1219
Cdd:PRK13645 83 KEVK--RLRKEIGLVFQFPeyQLFQETIEKDIAFGPvnlgenKQEAYKKVPELLKLVQ-------LPE----DYVKRSPf 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1220 QLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR--AREGRTCITIAHRLSSI-QNSDLIVYIDDGRV 1296
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
250 260
....*....|....*....|....*
gi 1678196980 1297 QEsgthkelmqlKGKYFELIKKQDL 1321
Cdd:PRK13645 230 IS----------IGSPFEIFSNQEL 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1097-1305 |
4.25e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ--DIKNISLYHLRTQMALVGQEP--RLFVG 1172
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1173 TIRENVCLGLKD--VPLEKI----NQALELANANRFLgnlpdgidtevgERGGQ-LSGGQKQRIAIARALVRDPKILLLD 1245
Cdd:PRK13638 94 DIDSDIAFSLRNlgVPEAEItrrvDEALTLVDAQHFR------------HQPIQcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1246 EATSALDSESERAVQEALDR-AREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
429-612 |
4.33e-14 |
|
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: 72.39 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 429 RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFNDT 508
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 509 IHNNLLFGNPDATRETMirvckmaNAHDFIKKMP-KGY-DTQIGdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQR-------TIEDALAAVGlTGFeDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*..
gi 1678196980 587 DAQSESVVQSAL-NNASKGRTTIMIAH 612
Cdd:TIGR01189 159 DKAGVALLAGLLrAHLARGGIVLLTTH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
435-642 |
4.93e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEW-LRNVVGIVQQEPILFND-TIHNN 512
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 LLFGnpdatRETMIRVCKMaNAHDFiKKMPK-------------GYDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLL 579
Cdd:PRK09700 101 LYIG-----RHLTKKVCGV-NIIDW-REMRVraammllrvglkvDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 580 DEATSAL-DAQSESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK09700 170 DEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1109-1298 |
5.36e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNI---SLYHLRTQ-MALVGQEPRLfVGTI--RENVCLgl 1182
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhVGFVFQSFML-IPTLnaLENVEL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 kdvP--LEKINQALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSES-ERAV 1259
Cdd:PRK10584 112 ---PalLRGESSRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 1260 QEALDRARE-GRTCITIAHRLSSIQNSDLIVYIDDGRVQE 1298
Cdd:PRK10584 187 DLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
433-641 |
6.46e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNL-EWLRNVVGIVQQEPILFND-TIH 510
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQELHLVPEmTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 511 NNLLFGN-PDA----TRETMIRVCKMANAHDFIKKMPkgyDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSA 585
Cdd:PRK11288 98 ENLYLGQlPHKggivNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 586 LDAQsESVVQSALNNA--SKGRTTIMIAHRLSTI-READKIVFFEKGVIVE-----AG-NHEELV 641
Cdd:PRK11288 171 LSAR-EIEQLFRVIRElrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmAQvDRDQLV 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
421-640 |
6.83e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 421 NVHFRYPTRKEAKVLNgLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDG----------VDVRDLNLEW 490
Cdd:PRK10261 19 NIAFMQEQQKIAAVRN-LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 LRNVVG----IVQQEPIL-----------FNDTIHNNLLFGNPDATRET--MIRVCKMANAHDFIKKMPKgydtqigdgg 553
Cdd:PRK10261 98 MRHVRGadmaMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAkrMLDQVRIPEAQTILSRYPH---------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 554 vQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD----AQSESVVQSALNNASKGrtTIMIAHRLSTIRE-ADKIVFFEK 628
Cdd:PRK10261 168 -QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|..
gi 1678196980 629 GVIVEAGNHEEL 640
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
433-623 |
7.19e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.98 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYePE---QGSVQIDG--VDVRDLNLEWLRNVVgIVQQE----PI 503
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevCRFKDIRDSEALGIV-IIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 504 LfndTIHNNLLFGNPDATR------ETMIRvckmanAHDFIKKM-----PkgyDTQIGDGGVqlsgGQKQRVAIARTLIR 572
Cdd:NF040905 93 L---SIAENIFLGNERAKRgvidwnETNRR------ARELLAKVgldesP---DTLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 573 DPKVLLLDEATSAL-DAQSESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKI 623
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
380-633 |
8.18e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 8.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 380 LLNARVAAASIyKTIDRVP-----KIDPYSRHGKKIEkvvgkvtFENVHFRYPTRKEAkvLNGLNLTVEPGTSVALVGHS 454
Cdd:PRK10522 289 LLSAQVAFNKL-NKLALAPykaefPRPQAFPDWQTLE-------LRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGN 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 455 GCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQEPILFnDTIHNNLLFGNPDATRETMIRVCKMANA 534
Cdd:PRK10522 359 GSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-DQLLGPEGKPANPALVEKWLERLKMAHK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 535 HDFIkkmpkgyDTQIGDggVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNA--SKGRTTIMIAH 612
Cdd:PRK10522 438 LELE-------DGRISN--LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISH 508
|
250 260
....*....|....*....|.
gi 1678196980 613 RLSTIREADKIVFFEKGVIVE 633
Cdd:PRK10522 509 DDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
93-304 |
8.55e-14 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 73.60 E-value: 8.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQPVLAIISGRMtnvllvIDPLSKEFKTKT--MENVYIFLGLGIFVSINDFCQYMCFQRVCSRMMTV 170
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRA------IDALTAGTLTASqlLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 171 MRNRYISSILRQNAGWFDKNLSGTITTRL-NDnMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVS 249
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARAtND-LNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 250 TICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQ 304
Cdd:cd18541 154 ALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKL 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1098-1300 |
8.73e-14 |
|
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: 72.37 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1098 PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRtQMALV-GQEPRLFVG-TIR 1175
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfGQKTQLWWDlPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCL-----GLKDVP----LEKINQALELAnanRFLgnlpdgiDTEVgeRggQLSGGQKQRIAIARALVRDPKILLLDE 1246
Cdd:cd03267 114 DSFYLlaaiyDLPPARfkkrLDELSELLDLE---ELL-------DTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1247 ATSALDSESERAVQEALDRAREGR--TCITIAHRLSSIQN-SDLIVYIDDGRVQESG 1300
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1082-1292 |
9.73e-14 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 75.94 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQrpHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGqdiknislyhlRTQMA 1161
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVGTIRENVCL----------GLKDVPLEKINQALELananrflgnlpdgidTEVGERGG----------QL 1221
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDKDLEQILDNVQL---------------THILEREGgwsavqdwmdVL 583
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1222 SGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAreGRTCITIAHRLSSIQNSDLIVYID 1292
Cdd:TIGR00954 584 SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
407-635 |
9.80e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 407 GKKIEKVVGKVTfenvhfRYPTR--------KEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQI 478
Cdd:PRK10261 310 GEPILQVRNLVT------RFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 479 DGVDVRDLN---LEWLRNVVGIVQQEPILFNDTIH------------NNLLFGNPDATR--ETMIRVcKMANAHDFikKM 541
Cdd:PRK10261 384 NGQRIDTLSpgkLQALRRDIQFIFQDPYASLDPRQtvgdsimeplrvHGLLPGKAAAARvaWLLERV-GLLPEHAW--RY 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 542 PKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTI-R 618
Cdd:PRK10261 461 PH-----------EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeR 529
|
250
....*....|....*..
gi 1678196980 619 EADKIVFFEKGVIVEAG 635
Cdd:PRK10261 530 ISHRVAVMYLGQIVEIG 546
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
433-639 |
1.43e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVE---PGTSV-ALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDG---VDV-RDLNLEWLRNVVGIVQQEPIL 504
Cdd:PRK11144 8 QQLGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 505 F-NDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKMPkgydtqigdggVQLSGGQKQRVAIARTLIRDPKVLLLDEAT 583
Cdd:PRK11144 88 FpHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 584 SALDAQSESVVQSALNNASKGRTTIMI--AHRLSTI-READKIVFFEKGVIVEAGNHEE 639
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILyvSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
433-623 |
2.05e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYePE---QGSVQIDGVDVRDLNL-EWLRNVVGIVQQEPILFND- 507
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 508 TIHNNLLFGNpDATRETMIRVCKM-ANAHDFIKKMPKGYD--TQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATS 584
Cdd:PRK13549 98 SVLENIFLGN-EITPGGIMDYDAMyLRAQKLLAQLKLDINpaTPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1678196980 585 ALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKI 623
Cdd:PRK13549 173 SLTESETAVLLDIIRDlKAHGIACIYISHKLNEVKAiSDTI 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1094-1307 |
3.86e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1094 RPHQPVMKQLQWTALRGQTVALVGPSGSGKST---------CIGMLERFYDVTGGaLRMDGQDIKNISLYHLRTQMALVG 1164
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTllkalagdlTGGGAPRGARVTGD-VTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEPR-LFVGTIRENVCLG----------LKDVPLEKINQALELANAnrflgnlpdgiDTEVGERGGQLSGGQKQRIAIAR 1233
Cdd:PRK13547 90 QAAQpAFAFSAREIVLLGrypharragaLTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1234 AL---------VRDPKILLLDEATSALD-SESERAVQEALDRAREGRT-CITIAHRLS-SIQNSDLIVYIDDGRVQESGT 1301
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
....*.
gi 1678196980 1302 HKELMQ 1307
Cdd:PRK13547 239 PADVLT 244
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
814-1054 |
3.93e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 71.44 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 814 LGIWFFQTLSTVM----FAIVSENLGVRFRVAAFRNLLYQDAAYFDnpAHAPGSLITRLAADPPCVKAVVDGRMMQVVYA 889
Cdd:cd18557 43 LAIYLLQSVFTFVryylFNIAGERIVARLRRDLFSSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 890 TAAVIACVTIGFINCWQVAILgtALIFLLGFIMAGLAFKISIVAAEHMEND---DAGKIAIEIIENVKTIQLLTRTRRFL 966
Cdd:cd18557 121 ILQVIGGLIILFILSWKLTLV--LLLVIPLLLIASKIYGRYIRKLSKEVQDalaKAGQVAEESLSNIRTVRSFSAEEKEI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 967 NSYENESKKRKRTELRKSVYEAVNYCISqNFMYYMSCFC-FALAIRIINQGDQTVDKtfrcLMAMMLCCEGIIMSAQ--- 1042
Cdd:cd18557 199 RRYSEALDRSYRLARKKALANALFQGIT-SLLIYLSLLLvLWYGGYLVLSGQLTVGE----LTSFILYTIMVASSVGgls 273
|
250
....*....|...
gi 1678196980 1043 -FFPQFVGAKSAA 1054
Cdd:cd18557 274 sLLADIMKALGAS 286
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
417-629 |
4.58e-13 |
|
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: 69.19 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAK-VLNGLNLTVEPGTSVALVGHSGCGKSTsvgLLTRLYEPE-----QGSVQIDGvdvRDLNLEW 490
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILING---RPLDKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 LRnVVGIVQQEPILFndtihnnllfgnPDAT-RETMIRVCKManahdfikkmpKGydtqigdggvqLSGGQKQRVAIART 569
Cdd:cd03232 78 QR-STGYVEQQDVHS------------PNLTvREALRFSALL-----------RG-----------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 570 LIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLS--TIREADKIVFFEKG 629
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
433-629 |
5.03e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVrdlNLEWLRNV----VGIVQQE-PILFND 507
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV---TFNGPKSSqeagIGIIHQElNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 508 TIHNNLLFGNPDATRETMIRVCKM-ANAHDFIKKMPKGYDTQIGDGgvQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:PRK10762 95 TIAENIFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFSSDKLVG--ELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1678196980 587 -DAQSESVVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKG 629
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1065-1252 |
6.95e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1065 PQTGDLKSGTKPEIRG-NILFENvkfsypQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRM 1143
Cdd:PRK10261 2 PHSDELDARDVLAVENlNIAFMQ------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1144 DGQDI--KNISLYHLRTQ------------MALVGQEPRLF---VGTIRENVCLGLKdvplekINQAL----ELANANRF 1202
Cdd:PRK10261 76 DKMLLrrRSRQVIELSEQsaaqmrhvrgadMAMIFQEPMTSlnpVFTVGEQIAESIR------LHQGAsreeAMVEAKRM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1203 LG--NLPDGiDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PRK10261 150 LDqvRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
434-615 |
8.48e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 434 VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDL---NLEWLRN-VVGIVQQEPILFND-T 508
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 509 IHNN----LLFG--NPDATRETmirvckmanAHDFIKKMpkGYDTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEA 582
Cdd:PRK11629 104 ALENvampLLIGkkKPAEINSR---------ALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1678196980 583 TSALDAQSESVVQSALN--NASKGRTTIMIAHRLS 615
Cdd:PRK11629 173 TGNLDARNADSIFQLLGelNRLQGTAFLVVTHDLQ 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
417-590 |
9.44e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.44 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYP-TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKST---SVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLR 492
Cdd:cd03233 4 LSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 493 NVVGIVQQEpilfndtIHNNLLfgnpdATRETMIRVCKMaNAHDFIKKmpkgydtqigdggvqLSGGQKQRVAIARTLIR 572
Cdd:cd03233 84 EIIYVSEED-------VHFPTL-----TVRETLDFALRC-KGNEFVRG---------------ISGGERKRVSIAEALVS 135
|
170
....*....|....*...
gi 1678196980 573 DPKVLLLDEATSALDAQS 590
Cdd:cd03233 136 RASVLCWDNSTRGLDSST 153
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
424-627 |
1.06e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.36 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 424 FRYPTRKeaKVLNGLNLTVEPGT-----SVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVD---------------V 483
Cdd:cd03237 1 YTYPTMK--KTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvsykpqyikadyegtV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 484 RDLnlewLRNVVGIVQQEPiLFNDTIHNNLlfgnpdatretmirvckmanahdfikKMPKGYDTQIGDggvqLSGGQKQR 563
Cdd:cd03237 79 RDL----LSSITKDFYTHP-YFKTEIAKPL--------------------------QIEQILDREVPE----LSGGELQR 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 564 VAIARTLIRDPKVLLLDEATSALDAQSESVVQSALN----NASKgrTTIMIAHRLSTIRE-ADKIVFFE 627
Cdd:cd03237 124 VAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfaeNNEK--TAFVVEHDIIMIDYlADRLIVFE 190
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1114-1300 |
1.18e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGML------ERFYDVTGGALRMDGQdiKNISLYHLRTQMALVGQEPRLFVG-TIRENVCLGLKDVP 1186
Cdd:PRK11144 28 AIFGRSGAGKTSLINAIsgltrpQKGRIVLNGRVLFDAE--KGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 LEKINQALELANANRFLGNLPdgidtevgergGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR- 1265
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERl 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678196980 1266 AREGRTCIT-IAHRLSSI-QNSDLIVYIDDGRVQESG 1300
Cdd:PRK11144 175 AREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
428-594 |
1.27e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 428 TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWL------RNVVgivqqE 501
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAM-----K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 502 PILfndTIHNNLLF-GNPDATRETMIR--VCKMANAHdfIKKMPKGYdtqigdggvqLSGGQKQRVAIARTLIRDPKVLL 578
Cdd:PRK13539 86 PAL---TVAENLEFwAAFLGGEELDIAaaLEAVGLAP--LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|....*.
gi 1678196980 579 LDEATSALDAQSESVV 594
Cdd:PRK13539 151 LDEPTAALDAAAVALF 166
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
432-627 |
2.01e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 67.07 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 432 AKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN-LEWL----------RNVVGIVQQ 500
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIragiayvpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 501 EPILFNDTIhnnllfgnpdatretmirvckmanahdfikkmpkgydtqigdgGVQLSGGQKQRVAIARTLIRDPKVLLLD 580
Cdd:cd03215 93 LSVAENIAL-------------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 581 EATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKI-VFFE 627
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRIlVMYE 179
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1109-1251 |
2.61e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYH-LRTQMALVGQEPRLFVG-TIRENVCLGLKDVP 1186
Cdd:PRK11614 30 QGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEENLAMGGFFAE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1187 LEKINQALElananRFLGNLPDGIDTEVgERGGQLSGGQKQRIAIARALVRDPKILLLDEATSAL 1251
Cdd:PRK11614 110 RDQFQERIK-----WVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
429-612 |
2.69e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 429 RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDL------NLEWLRNVVGIvqqEP 502
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 503 ILfndTIHNNLLF---GNPDATRETMIRVCkmanahdfikkmpkgydTQIGDGGV------QLSGGQKQRVAIARTLIRD 573
Cdd:PRK13538 88 EL---TALENLRFyqrLHGPGDDEALWEAL-----------------AQVGLAGFedvpvrQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 574 PKVLLLDEATSALDAQSESVVQSAL-NNASKGRTTIMIAH 612
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLaQHAEQGGMVILTTH 187
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
399-616 |
2.88e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 399 KIDPYSRHGKKIEKVVGKVTFENVHFRypTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLT-RLYEPE-QGSV 476
Cdd:PLN03211 50 KFENMKNKGSNIKRILGHKPKISDETR--QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 477 QIDGvdvRDLNLEWLRNVvGIVQQEPILF-NDTIHNNLLFGNPDATRETMIRVCKMANAHDFIKKM--PKGYDTQIGDGG 553
Cdd:PLN03211 128 LANN---RKPTKQILKRT-GFVTQDDILYpHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNSF 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 554 VQ-LSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSE-SVVQSALNNASKGRTTIMIAHRLST 616
Cdd:PLN03211 204 IRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1110-1305 |
4.35e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCI-----------GMLERFY-----------------DVTGGALRMdgQDIKNISlyHLRTQMA 1161
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFkdeknkkktkekekvleKLVIQKTRF--KKIKKIK--EIRRRVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQ--EPRLFVGTIRENVCLGLKDVPLEKiNQALELANanRFLGNLpdGIDTEVGERGG-QLSGGQKQRIAIARALVRD 1238
Cdd:PRK13651 109 VVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAA--KYIELV--GLDESYLQRSPfELSGGQKRRVALAGILAME 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALDRA-REGRTCITIAHRLSSI-QNSDLIVYIDDGR-VQESGTHKEL 1305
Cdd:PRK13651 184 PDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIFFKDGKiIKDGDTYDIL 253
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
411-629 |
4.65e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 411 EKVVGKVTFE--NVHFRYPTRKEAKV-LNGLNLTVEPGTSVALVGHSGCGKSTsvgLLTRLYEPEQGSVQIDG---VDVR 484
Cdd:TIGR00956 752 EKESGEDIFHwrNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGdrlVNGR 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 485 DLNLEWLRNvVGIVQQEPI-LFNDTIHNNLLFGN--------PDATR----ETMIRVCKMANAHDFIkkmpkgydtqIGD 551
Cdd:TIGR00956 829 PLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAylrqpksvSKSEKmeyvEEVIKLLEMESYADAV----------VGV 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 552 GGVQLSGGQKQRVAIARTLIRDPKVLL-LDEATSALDAQSE-SVVQSALNNASKGRTTIMIAHRLSTI--READKIVFFE 627
Cdd:TIGR00956 898 PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAwSICKLMRKLADHGQAILCTIHQPSAIlfEEFDRLLLLQ 977
|
..
gi 1678196980 628 KG 629
Cdd:TIGR00956 978 KG 979
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1110-1300 |
4.83e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHL---------RTQMALVGQEPRlfvGTIRENVCL 1180
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPR---DGLRMQVSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 GlkdvplEKINQALeLANANRFLGNL--------------PDGIDtevgERGGQLSGGQKQRIAIARALVRDPKILLLDE 1246
Cdd:PRK11701 109 G------GNIGERL-MAVGARHYGDIratagdwlerveidAARID----DLPTTFSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1247 ATSALDSeserAVQ-EALDRARE-----GRTCITIAH-----RLSsiqnSDLIVYIDDGRVQESG 1300
Cdd:PRK11701 178 PTGGLDV----SVQaRLLDLLRGlvrelGLAVVIVTHdlavaRLL----AHRLLVMKQGRVVESG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1110-1295 |
4.95e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFY--DVTGGALRMDGQDIKNISLYHL-RTQMALVGQEPRLFVG-TIRENVCLGLK-D 1184
Cdd:TIGR02633 27 GECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVAENIFLGNEiT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1185 VPLEKINQALELANANRFLGNLPDGIDTeVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSAL-DSESERAVQEAL 1263
Cdd:TIGR02633 107 LPGGRMAYNAMYLRAKNLLRELQLDADN-VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEKETEILLDIIR 185
|
170 180 190
....*....|....*....|....*....|...
gi 1678196980 1264 DRAREGRTCITIAHRLSSIQN-SDLIVYIDDGR 1295
Cdd:TIGR02633 186 DLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1093-1263 |
6.32e-12 |
|
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: 65.98 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1093 QRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRtQMALVGQEPRL-FV 1171
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-GLLYLGHAPGIkTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1172 GTIRENVCLGLKDVPLEKINQALELANANRFlGNLPdgidtevgerGGQLSGGQKQRIAIARALVRDPKILLLDEATSAL 1251
Cdd:cd03231 88 LSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|..
gi 1678196980 1252 DSESERAVQEAL 1263
Cdd:cd03231 157 DKAGVARFAEAM 168
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1109-1300 |
6.49e-12 |
|
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: 66.79 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYhlrtqmalVGQEPRLfvgTIRENV-----CLGLK 1183
Cdd:cd03220 47 RGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG--------GGFNPEL---TGRENIylngrLLGLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1184 -DVPLEKINQALELAnanrflgNLPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSE-SERAVQE 1261
Cdd:cd03220 116 rKEIDEKIDEIIEFS-------ELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 1262 ALDRAREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESG 1300
Cdd:cd03220 185 LRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
141-306 |
6.61e-12 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 67.86 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 141 IFLGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDnMERIQDGVGDKLGVLIRG 220
Cdd:cd18570 47 GLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 221 ISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAK 300
Cdd:cd18570 126 LLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKK 205
|
....*.
gi 1678196980 301 YEKQLN 306
Cdd:cd18570 206 IEKKFS 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1098-1282 |
7.63e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 7.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1098 PVMKQLQWTALR---GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIK----------NISLYHlrtqmalvg 1164
Cdd:PRK10762 15 PGVKALSGAALNvypGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeaGIGIIH--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QE----PRLfvgTIRENVCLGLKDV-PLEKINQALELANANRFLG--NLPDGIDTEVGErggqLSGGQKQRIAIARALVR 1237
Cdd:PRK10762 86 QElnliPQL---TIAENIFLGREFVnRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGEQQMVEIAKVLSF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678196980 1238 DPKILLLDEATSAL-DSESE---RAVQEALDrarEGRTCITIAHRLSSI 1282
Cdd:PRK10762 159 ESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEI 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1077-1305 |
7.88e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1077 EIRGnilfenVKFSypqRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLerfydvtGGALR-------MDGQDIK 1149
Cdd:PRK11831 9 DMRG------VSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI-------GGQIApdhgeilFDGENIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1150 NIS---LYHLRTQMALVGQEPRLFVG-TIRENVCLglkdvPLEKINQALELANANRFLGNLpdgidTEVGERGG------ 1219
Cdd:PRK11831 73 AMSrsrLYTVRKRMSMLFQSGALFTDmNVFDNVAY-----PLREHTQLPAPLLHSTVMMKL-----EAVGLRGAaklmps 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1220 QLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:PRK11831 143 ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKI 222
|
....*....
gi 1678196980 1297 QESGTHKEL 1305
Cdd:PRK11831 223 VAHGSAQAL 231
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
143-304 |
8.37e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 67.92 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 143 LGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDgvgdklgVLIRGIS 222
Cdd:cd18564 61 VGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD-------LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 223 MVIASVVISLIY-------EWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQE 295
Cdd:cd18564 134 PLLTNLLTLVGMlgvmfwlDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREE 213
|
....*....
gi 1678196980 296 EMVAKYEKQ 304
Cdd:cd18564 214 HEERRFARE 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1082-1277 |
8.79e-12 |
|
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: 64.01 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTcigmLerfydvtggaLRMDGQDIKNISlyhlrtqma 1161
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKST----L----------LKLIAGELEPDE--------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 lvgqeprlfvGTIRENVCLGLKDVPlekinqalelananrflgnlpdgidtevgerggQLSGGQKQRIAIARALVRDPKI 1241
Cdd:cd03221 55 ----------GIVTWGSTVKIGYFE---------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678196980 1242 LLLDEATSALDSESERAVQEALdrAREGRTCITIAH 1277
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL--KEYPGTVILVSH 125
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
417-586 |
8.91e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDlnleW-----L 491
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD----WqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 492 RNVVGIVQQEPILFND-TIHNNLLFGNPDATRETMIRvcKMANAHDFikkMPKGYDTQIGDGGVqLSGGQKQRVAIARTL 570
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170
....*....|....*.
gi 1678196980 571 IRDPKVLLLDEATSAL 586
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1093-1305 |
9.16e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1093 QRPHQPVMKQLQWTALRGQTVALVGPSGSGKS-TCIGMLERF------YdvTGGALRMDGQDIKNIS---LYHLR-TQMA 1161
Cdd:PRK15134 18 QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpsppvvY--PSGDIRFHGESLLHASeqtLRGVRgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1162 LVGQEPRLFVG---TIRENV--CLGL-----KDVPLEKINQALE---LANANRFLGNLPDgidtevgerggQLSGGQKQR 1228
Cdd:PRK15134 96 MIFQEPMVSLNplhTLEKQLyeVLSLhrgmrREAARGEILNCLDrvgIRQAAKRLTDYPH-----------QLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1229 IAIARALVRDPKILLLDEATSALDSeserAVQ-EALDRARE-----GRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGT 1301
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDV----SVQaQILQLLRElqqelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNR 240
|
....
gi 1678196980 1302 HKEL 1305
Cdd:PRK15134 241 AATL 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1109-1320 |
1.09e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.26 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGqdikNISlyhlrtqmAL----VGQEPRLfvgTIRENV-----C 1179
Cdd:COG1134 51 RGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVS--------ALlelgAGFHPEL---TGRENIylngrL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 LGL-KDVPLEKINQALELANanrfLGnlpDGIDTEVgergGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSE-SER 1257
Cdd:COG1134 116 LGLsRKEIDEKFDEIVEFAE----LG---DFIDQPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1258 AVQEALDRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQLkgkYFELIKKQD 1320
Cdd:COG1134 185 CLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA---YEALLAGRE 245
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
436-640 |
1.19e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 436 NGLNLTVEPGTSVALVGHSGCGKSTSV----GLLTRLYEPEqGSVQIDGVDVRDLN---LEWLRnvvgiVQQEPILFND- 507
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAfalmGLLAANGRIG-GSATFNGREILNLPekeLNKLR-----AEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 508 ------------------TIHNNLlfGNPDATRET--MIRVCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIA 567
Cdd:PRK09473 107 mtslnpymrvgeqlmevlMLHKGM--SKAEAFEESvrMLDAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTT--IMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1109-1297 |
1.23e-11 |
|
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: 63.93 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTG-GALRMDGQDIKNISLYHLRtqmalvgqeprlfvgtirenvclglkdvpl 1187
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1188 ekinqalelananrflgnlpdgiDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALD--- 1264
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678196980 1265 ----RAREGRTCITIAHRLSSIQnSDLIVYIDDGRVQ 1297
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLG-PALLRRRFDRRIV 143
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
421-635 |
1.41e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 421 NVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLT-RLYEPE-------QGSVQIDGVDVRDLN---LE 489
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDaprLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 490 WLRNVvgIVQQEPILFNDTIHNNLLFGN-PDATR--ETMIRV-----CKMANAhdfikkmpkGYDTQIGDGGVQLSGGQK 561
Cdd:PRK13547 83 RLRAV--LPQAAQPAFAFSAREIVLLGRyPHARRagALTHRDgeiawQALALA---------GATALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 562 QRVAIARTL---------IRDPKVLLLDEATSALD-AQSESVVQSALNNASKGRTTIM-IAHRLS-TIREADKIVFFEKG 629
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLGVLaIVHDPNlAARHADRIAMLADG 231
|
....*.
gi 1678196980 630 VIVEAG 635
Cdd:PRK13547 232 AIVAHG 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
430-590 |
1.65e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 430 KEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNL-EWLRNVVGIVQQEPILFND- 507
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 508 TIHNNLLfgnpdATRETMIRVCKMANAHDFIKKMPKGYDTQIGDG-GVQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:PRK10895 94 SVYDNLM-----AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
....
gi 1678196980 587 DAQS 590
Cdd:PRK10895 169 DPIS 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1099-1317 |
2.39e-11 |
|
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: 67.91 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1099 VMKQLQWTALRGQTVALVGPSGSGKSTCIGML-----------ERFYDVT---------------------GGALRMDGQ 1146
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgRIIYHVAlcekcgyverpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1147 DIKNIS---LYHLRTQMALVGQepRLFV----GTIRENVCLGLKDVPL---EKINQALELANAnrflgnlpdgidTEVGE 1216
Cdd:TIGR03269 95 DFWNLSdklRRRIRKRIAIMLQ--RTFAlygdDTVLDNVLEALEEIGYegkEAVGRAVDLIEM------------VQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1217 R----GGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRA--REGRTCITIAHRLSSIQN-SDLIV 1289
Cdd:TIGR03269 161 RithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAI 240
|
250 260
....*....|....*....|....*...
gi 1678196980 1290 YIDDGRVQESGTHKELMQlkgKYFELIK 1317
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA---VFMEGVS 265
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
433-629 |
2.66e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.54 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYePE---QGSVQIDGVDVRDLNL-EWLRNVVGIVQQEPILFND- 507
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 508 TIHNNLLFGN------PDATRETMIRVCKMANAHDFIKKMPKGYDTQigdggvQLSGGQKQRVAIARTLIRDPKVLLLDE 581
Cdd:TIGR02633 94 SVAENIFLGNeitlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVG------DYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 582 ATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKG 629
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1109-1296 |
3.26e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKS----TCIGMLERfydvTGGALRMDGQDIKNISLYH-LRTQMALVgQEPR----LFVG-TIRENV 1178
Cdd:COG1129 277 AGEILGIAGLVGAGRTelarALFGADPA----DSGEIRLDGKPVRIRSPRDaIRAGIAYV-PEDRkgegLVLDlSIRENI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1179 CLGLkdvpLEK------INQALELANANRFLGNL---PDGIDTEVGerggQLSGGQKQRIAIARALVRDPKILLLDEATS 1249
Cdd:COG1129 352 TLAS----LDRlsrgglLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1250 ALDSESERAVQEALDR-AREGRTCITIahrlSS-----IQNSDLIVYIDDGRV 1296
Cdd:COG1129 424 GIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
162-306 |
3.73e-11 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 65.64 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 162 RVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVgdKLGVL--IRGISMVIASvVISLIY-EWRL 238
Cdd:cd18574 68 VVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSF--KQCVSqgLRSVTQTVGC-VVSLYLiSPKL 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 239 ALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLN 306
Cdd:cd18574 145 TLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVE 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
417-638 |
4.06e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHfryptrkeaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRdlnlEWLR-NVV 495
Cdd:PRK15056 14 VTWRNGH---------TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQkNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 GIVQQE-------PILFNDTI------HNNLLFGNPDATRETMIRVCKMANAHDFIKKmpkgydtQIGdggvQLSGGQKQ 562
Cdd:PRK15056 81 AYVPQSeevdwsfPVLVEDVVmmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHR-------QIG----ELSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 563 RVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIREADKIVFFEKGVIVEAGNHE 638
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1110-1316 |
5.52e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLE---RFYDVTGGALRMDGQDIKNIslyhlRTQMALVGQEPRLFVG-TIREN-VCLGLKD 1184
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgriQGNNFTGTILANNRKPTKQI-----LKRTGFVTQDDILYPHlTVRETlVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1185 VP--LEKINQALELANANRFLGnLPDGIDTEVGE---RGgqLSGGQKQRIAIARALVRDPKILLLDEATSALDSESE-RA 1258
Cdd:PLN03211 169 LPksLTKQEKILVAESVISELG-LTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRL 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1259 VQEALDRAREGRTCITIAHRLSS--IQNSDLIVYIDDGRVQESGTHKELMqlkgKYFELI 1316
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAM----AYFESV 301
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1093-1276 |
6.15e-11 |
|
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: 63.15 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1093 QRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIkNISLYHLRTQMALVGQEPrlfvg 1172
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLGHLP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1173 tirenvclGLKdvplekinQALELANANRFLGNLPDGID-------TEVGERG------GQLSGGQKQRIAIARALVRDP 1239
Cdd:TIGR01189 83 --------GLK--------PELSALENLHFWAAIHGGAQrtiedalAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRR 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678196980 1240 KILLLDEATSALDSESERAVQEALdRAREGRTCITIA 1276
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLL-RAHLARGGIVLL 182
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1110-1296 |
6.36e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI---KNISLYHLRTQMALVGQEPRLFVG-TIRENVCLGL--- 1182
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHHLLMDrTVYDNVAIPLiia 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1183 ----KDVPlEKINQALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSE-SER 1257
Cdd:PRK10908 108 gasgDDIR-RRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAlSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 1258 AVQEALDRAREGRTCITIAHRLSSIQNSDL-IVYIDDGRV 1296
Cdd:PRK10908 176 ILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
437-640 |
6.71e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 437 GLNLTVEPGTSVALVGHSGCGKS-TSVGLLTRL---YEPEQGSVQIDGVDVRDLNLEWlRNVVGIVQQEPILFN--DTIH 510
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRG-RKIATIMQNPRSAFNplHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 511 NN-----LLFGNPdATRETMIRVCK---MANAHDFIKKMPkgydtqigdggVQLSGGQKQRVAIARTLIRDPKVLLLDEA 582
Cdd:PRK10418 100 THaretcLALGKP-ADDATLTAALEavgLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 583 TSALDAQSESVVQSALNN--ASKGRTTIMIAHRLSTI-READKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK10418 168 TTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1085-1299 |
1.02e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1085 ENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLY-HLRTQMALV 1163
Cdd:PRK10895 7 KNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPRLF-----------VGTIRENVClglKDVPLEKINQALELANANRFLGNLpdgidtevgerGGQLSGGQKQRIAIA 1232
Cdd:PRK10895 84 PQEASIFrrlsvydnlmaVLQIRDDLS---AEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESeravqealdraregrtCITIAHRLSSIQNSDLIVYIDDGRVQES 1299
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPIS----------------VIDIKRIIEHLRDSGLGVLITDHNVRET 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
424-641 |
1.10e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 424 FRYPT----RKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQ 499
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 500 QEP------------ILFNDTIHNNLLfgNPDATRETMIRVCKMANA-HDFIKKMPKgydtqigdggvQLSGGQKQRVAI 566
Cdd:PRK15112 94 QDPstslnprqrisqILDFPLRLNTDL--EPEQREKQIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 567 ARTLIRDPKVLLLDEATSALDAQSES-VVQSALNNASK-GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELV 641
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSqLINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1110-1306 |
1.17e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLfVG--TIRENVCLG-LKDVP 1186
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGdiTVQELVARGrYPHQP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 L---------EKINQALELAnanrflgnlpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESER 1257
Cdd:PRK10253 112 LftrwrkedeEAVTKAMQAT-----------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1258 AVQEAL-DRARE-GRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKELM 1306
Cdd:PRK10253 181 DLLELLsELNREkGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1109-1296 |
1.51e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 61.68 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKS----TCIGMLErfydVTGGALRMDGQDIKNISLYHLRTQ-MALVGQEPR---LFVG-TIRENVC 1179
Cdd:cd03215 25 AGEIVGIAGLVGNGQTelaeALFGLRP----PASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSVAENIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 LGLkdvplekinqalelananrflgnlpdgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAV 1259
Cdd:cd03215 101 LSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678196980 1260 QEALDR-AREGRTCITIahrlSS-----IQNSDLIVYIDDGRV 1296
Cdd:cd03215 144 YRLIRElADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1090-1261 |
1.72e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1090 SYPqrPHQPVMKQLQWTALRGQTVALVGPSGSGKSTcigmLERFY-----DVTGGALRMDGqdIKnislyhlrtqmalVG 1164
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMagvdkDFNGEARPQPG--IK-------------VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 ---QEPRL-FVGTIRENVCLGLKDVP-----------------------------LEKINQALELANANRFLG------N 1205
Cdd:TIGR03719 72 ylpQEPQLdPTKTVRENVEEGVAEIKdaldrfneisakyaepdadfdklaaeqaeLQEIIDAADAWDLDSQLEiamdalR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1206 LPDGiDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSES----ERAVQE 1261
Cdd:TIGR03719 152 CPPW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
420-627 |
2.12e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFR--------YPTRKEA------------KVLNGLNLTVEPGT-----SVALVGHSGCGKSTSVGLLTRLYEPEQG 474
Cdd:COG1245 316 ENVRIRdepiefevHAPRREKeeetlveypdltKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 475 SVQID--------------GVDVRDLnlewLRNVvgivqqepilfndtihnnllfgNPDATRETMIRvckmanaHDFIKK 540
Cdd:COG1245 396 EVDEDlkisykpqyispdyDGTVEEF----LRSA----------------------NTDDFGSSYYK-------TEIIKP 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 541 M--PKGYDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLST 616
Cdd:COG1245 443 LglEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaENRGKTAMVVDHDIYL 518
|
250
....*....|..
gi 1678196980 617 IRE-ADKIVFFE 627
Cdd:COG1245 519 IDYiSDRLMVFE 530
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1110-1294 |
2.16e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.49 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGML-ERFYD-VTGGALRMDGQDIKNislyHLRTQMALVGQEPRLFVG-TIREnvclglkdvp 1186
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDK----NFQRSTGYVEQQDVHSPNlTVRE---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 lekinqalelanANRFLGNLpdgidtevgeRGgqLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR- 1265
Cdd:cd03232 99 ------------ALRFSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKl 154
|
170 180 190
....*....|....*....|....*....|.
gi 1678196980 1266 AREGRTCITIAHRLSS--IQNSDLIVYIDDG 1294
Cdd:cd03232 155 ADSGQAILCTIHQPSAsiFEKFDRLLLLKRG 185
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
91-304 |
2.33e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 63.27 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIgLITSVIsGVSQPVL-------AIISGRMTNV-LLVIdplskefktktmenvyIFLGLGIFVSINDFCQYMCFQR 162
Cdd:cd18550 4 VLLLI-LLSALL-GLLPPLLlreiiddALPQGDLGLLvLLAL----------------GMVAVAVASALLGVVQTYLSAR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 163 VCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMM 242
Cdd:cd18550 66 IGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 243 LGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECL--MGVRTIQAFNGQEEMVAKYEKQ 304
Cdd:cd18550 146 LVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARR 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1098-1318 |
2.33e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1098 PVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERF--YDVTGGALRMDGQDIKNISLyHLRTQMA--LVGQEP------ 1167
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEP-EERAHLGifLAFQYPieipgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1168 ------RLFVGTIRENvcLGLKDV-PL---EKINQALELANAN-RFLG-NLPDGidtevgerggqLSGGQKQRIAIARAL 1235
Cdd:CHL00131 100 snadflRLAYNSKRKF--QGLPELdPLeflEIINEKLKLVGMDpSFLSrNVNEG-----------FSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1236 VRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAH--RLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGKY 1312
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEKKG 246
|
....*.
gi 1678196980 1313 FELIKK 1318
Cdd:CHL00131 247 YDWLKQ 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1109-1305 |
3.04e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTC----IGMLERFYDVTGGALRMDGQDIKNISLYHLR----TQMALVGQEPRLFVgtireNVC- 1179
Cdd:PRK11022 32 QGEVVGIVGESGSGKSVSslaiMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSL-----NPCy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1180 -LGLKDVPLEKINQ----------ALELANanrfLGNLPDGIdTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEAT 1248
Cdd:PRK11022 107 tVGFQIMEAIKVHQggnkktrrqrAIDLLN----QVGIPDPA-SRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1249 SALDSESERAVQEALD--RAREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK11022 182 TALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1084-1305 |
3.25e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPHQpvMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLRTQMALV 1163
Cdd:PRK10522 325 LRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1164 GQEPRLF---VGTIRENVCLGLKDVPLEKINQALELANANRFLGNLpdgidtevgerggQLSGGQKQRIAIARALVRDPK 1240
Cdd:PRK10522 403 FTDFHLFdqlLGPEGKPANPALVEKWLERLKMAHKLELEDGRISNL-------------KLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1241 ILLLDEATSALDSESERAV-QEALDRARE-GRTCITIAHRLSSIQNSDLIVYIDDGRVQE-SGTHKEL 1305
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
414-612 |
3.45e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 414 VGKVtfenvhfrYPTRKEakVLNGLNLTVEPGTSVALVGHSGCGKST----------------------SVGLLTRlyEP 471
Cdd:TIGR03719 10 VSKV--------VPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTllrimagvdkdfngearpqpgiKVGYLPQ--EP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 472 eqgsvQID-GVDVRDLNLEWLRNVVGIVQQepilFNDTihnNLLFGNPDATRETMIRvcKMA---------NAHDFIKKM 541
Cdd:TIGR03719 78 -----QLDpTKTVRENVEEGVAEIKDALDR----FNEI---SAKYAEPDADFDKLAA--EQAelqeiidaaDAWDLDSQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 542 ---------PKGyDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNaSKGrTTIMIAH 612
Cdd:TIGR03719 144 eiamdalrcPPW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
439-635 |
3.51e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 439 NLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNL--------------EWlrnvvGIVQQEP-- 502
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrrllrtEW-----GFVHQHPrd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 503 -----ILFNDTIHNNLL------FGNpdatretmIRvckmANAHDFIKKMPKGYDtQIGDGGVQLSGGQKQRVAIARTLI 571
Cdd:PRK11701 101 glrmqVSAGGNIGERLMavgarhYGD--------IR----ATAGDWLERVEIDAA-RIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 572 RDPKVLLLDEATSALDAQsesvVQSALNNASKGRTT------IMIAHRLSTIRE-ADKIVFFEKGVIVEAG 635
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
123-306 |
3.85e-10 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 62.36 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 123 VIDPLSKEFKTKTMENVYIFLGLGIFVS-INDFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLND 201
Cdd:cd18590 22 VIDILGGEYQHNAFTSAIGLMCLFSLGSsLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 202 NMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEEC 281
Cdd:cd18590 102 DTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREA 181
|
170 180
....*....|....*....|....*
gi 1678196980 282 LMGVRTIQAFNGQEEMVAKYEKQLN 306
Cdd:cd18590 182 VSSIRTVRSFKAEEEEACRYSEALE 206
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1110-1305 |
3.93e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKS----TCIGMLERfYDVTGGALRMDGQDIKNIS---LYHLRT-QMALVGQEPR------LFVGTIR 1175
Cdd:PRK09473 42 GETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPMtslnpyMRVGEQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVC-----LGLKDVPLEKIN--QALELANANRFLGNLPDgidtevgerggQLSGGQKQRIAIARALVRDPKILLLDEAT 1248
Cdd:PRK09473 121 MEVLmlhkgMSKAEAFEESVRmlDAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1249 SALDSESERAVQEAL-DRAREGRTC-ITIAHRL---SSIQNSDLIVYIddGRVQESGTHKEL 1305
Cdd:PRK09473 190 TALDVTVQAQIMTLLnELKREFNTAiIMITHDLgvvAGICDKVLVMYA--GRTMEYGNARDV 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
426-593 |
4.27e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 426 YPTRKeaKVLNGLNLTVEPGTSVALVGHSGCGKSTsvglLTRLyepeqgsvqIDGVDvRDLNLE-WLRN--VVGIVQQEP 502
Cdd:PRK11819 16 VPPKK--QILKDISLSFFPGAKIGVLGLNGAGKST----LLRI---------MAGVD-KEFEGEaRPAPgiKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 503 IL-----------------------FNDTihnNLLFGNPDA-TRETMIRVCKM------ANAHDFikkmpkgyDTQI--- 549
Cdd:PRK11819 80 QLdpektvrenveegvaevkaaldrFNEI---YAAYAEPDAdFDALAAEQGELqeiidaADAWDL--------DSQLeia 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 550 --------GDGGV-QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAqsESV 593
Cdd:PRK11819 149 mdalrcppWDAKVtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--ESV 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1110-1298 |
4.37e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLerfydvTGGALRMDGQDIKNISLYHLRTQMALVGQEPRLfvGTIRENVCL----GLKDV 1185
Cdd:COG2401 56 GEIVLIVGASGSGKSTLLRLL------AGALKGTPVAGCVDVPDNQFGREASLIDAIGRK--GDFKDAVELlnavGLSDA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1186 PLekinqalelananrFLgnlpdgidtevgERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR 1265
Cdd:COG2401 128 VL--------------WL------------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1678196980 1266 A--REGRTCITIAHR---LSSIQnSDLIVYID-DGRVQE 1298
Cdd:COG2401 182 LarRAGITLVVATHHydvIDDLQ-PDLLIFVGyGGVPEE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
409-632 |
5.39e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 409 KIEKVVGKVTFENVHFRYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN- 487
Cdd:COG3845 248 KAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSp 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 488 LEWLRNVVGIVQQEPI---LFND-TIHNNLLFG---NPDATRETMIRVCKM-ANAHDFIKKM---PKGYDTQIGdggvQL 556
Cdd:COG3845 328 RERRRLGVAYIPEDRLgrgLVPDmSVAENLILGryrRPPFSRGGFLDRKAIrAFAEELIEEFdvrTPGPDTPAR----SL 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 557 SGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNA-SKGRTTIMIAHRLSTIRE-ADKI-VFFEkGVIV 632
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrDAGAAVLLISEDLDEILAlSDRIaVMYE-GRIV 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
420-627 |
7.15e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 420 ENVHFR--------YPTRKEA------------KVLNGLNLTVEPGTS-----VALVGHSGCGKSTSVGLLTRLYEPEQG 474
Cdd:PRK13409 315 ENMRIRpepiefeeRPPRDESeretlveypdltKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 475 SVQIDgVDV--------RDLNL---EWLRNVvgivqqepilfNDTIHNNLLFgnpdatretmirvckmanaHDFIKKM-- 541
Cdd:PRK13409 395 EVDPE-LKIsykpqyikPDYDGtveDLLRSI-----------TDDLGSSYYK-------------------SEIIKPLql 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 542 PKGYDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN--ASKGRTTIMIAHRLSTIRE 619
Cdd:PRK13409 444 ERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaEEREATALVVDHDIYMIDY 519
|
....*....
gi 1678196980 620 -ADKIVFFE 627
Cdd:PRK13409 520 iSDRLMVFE 528
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
91-303 |
1.11e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 60.94 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIGLITSVISGVSQPVL---AI---ISGRMTNVLLVIdplskefktktmenVYIFLGLGIFvsindfcqYMCFQRVC 164
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLikiAIdeyIPNGDLSGLLII--------------ALLFLALNLV--------NWVASRLR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 165 SRMMTV--------MRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEW 236
Cdd:cd18545 61 IYLMAKvgqrilydLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 237 RLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEK 303
Cdd:cd18545 141 RLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDE 207
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
433-640 |
1.20e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.30 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTS----VGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVG----IVQQEP-- 502
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSslaiMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 503 -----------ILFNDTIHNNllfGNPDATRETMIRVCKMANAHDFIKKM---PKgydtqigdggvQLSGGQKQRVAIAR 568
Cdd:PRK11022 101 slnpcytvgfqIMEAIKVHQG---GNKKTRRQRAIDLLNQVGIPDPASRLdvyPH-----------QLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 569 TLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTT--IMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEEL 640
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1097-1319 |
1.24e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1097 QPVMKQLQWTALRGQTVALVGPSGSGKSTCIGML--ERFYDVTGGALRMDGQDIKNIS---------LYHLRTQMALVGQ 1165
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpedragegiFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1166 EPRLFVGTIRENVCLGLKDVPLEKINQALELANANRFLgNLPDGIDTEVGERGgqLSGGQKQRIAIARALVRDPKILLLD 1245
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL-KMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1246 EATSALDSESERAVQEALDRAREG-RTCITIAH--RLSSIQNSDLIVYIDDGRVQESGTHKELMQLKGK-YFELIKKQ 1319
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQgYGWLTEQQ 248
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
409-618 |
1.29e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.46 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 409 KIEKVVGKVTFENVHFRYPTRKeaKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvdvrdlnl 488
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLVTPNGD--VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-------- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 489 ewlRNVVGIVQQEPILFNDTIHNNLLF----------GNPDATRETMIRVCKManahDFIKKMPKGYDTqIGDGGVQLSG 558
Cdd:TIGR00954 514 ---KGKLFYVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDKDLEQILDNVQL----THILEREGGWSA-VQDWMDVLSG 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 559 GQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNAskGRTTIMIAHRLSTIR 618
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1103-1308 |
1.56e-09 |
|
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: 62.13 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1103 LQWTALRGQTVALVGPSGSGKSTC----IGMLE------------RFYDVTGGALRMDGQDIKNISLYHlrtqmalvgQE 1166
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLskiiAGVLEptsgevnvrvgdEWVDMTKPGPDGRGRAKRYIGILH---------QE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1167 PRLFV-GTIRENV--CLGLkDVPLE----KINQALELAN-----ANRFLGNLPDgidtevgerggQLSGGQKQRIAIARA 1234
Cdd:TIGR03269 374 YDLYPhRTVLDNLteAIGL-ELPDElarmKAVITLKMVGfdeekAEEILDKYPD-----------ELSEGERHRVALAQV 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 1235 LVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQL 1308
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
421-621 |
1.64e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 421 NVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIVQQ 500
Cdd:PRK13540 6 ELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 501 EPILFNDTIHNNLLF------GNPDATRetMIRVCKMANAHDFikkmPKGYdtqigdggvqLSGGQKQRVAIARTLIRDP 574
Cdd:PRK13540 83 SGINPYLTLRENCLYdihfspGAVGITE--LCRLFSLEHLIDY----PCGL----------LSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALN-NASKGRTTIMIAHRLSTIREAD 621
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQeHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1106-1300 |
1.73e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1106 TALR--------GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLrtqMALVGQ--EPRLFVGTIR 1175
Cdd:PRK15056 21 TALRdasftvpgGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQseEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCL-------GLKDVPLEKINQALELANANRflgNLPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEAT 1248
Cdd:PRK15056 98 EDVVMmgryghmGWLRRAKKRDRQIVTAALARV---DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1249 SALDSESERAVQEALDRAR-EGRTCITIAHRLSSIQN-SDLIVYIdDGRVQESG 1300
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYTVMV-KGTVLASG 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
417-614 |
2.12e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQidgvdvRDLNLEwlrnvVG 496
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 497 IVQQEpILFNDTIH---NNLLFGNPDATRETMIRVCKMANAHDFIKK-MPKgydtqigdggvqLSGGQKQRVAIARTLIR 572
Cdd:PRK09544 71 YVPQK-LYLDTTLPltvNRFLRLRPGTKKEDILPALKRVQAGHLIDApMQK------------LSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRL 614
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
430-637 |
2.22e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 430 KEAKVLNGLNLTVEPGTSVALVGHSGCGKST-SVGLLTRL-YEPEQGSVQIDGVDVRDLNLEwLRNVVGIVQ--QEPILF 505
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSPE-DRAGEGIFMafQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 506 NDTIHNNLLFGNPDATR-----ETMIRVckmaNAHDFIK------KMPKGYDTQigDGGVQLSGGQKQRVAIARTLIRDP 574
Cdd:PRK09580 91 PGVSNQFFLQTALNAVRsyrgqEPLDRF----DFQDLMEekiallKMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 575 KVLLLDEATSALDAQSESVVQSALNNASKG-RTTIMIAH--RLSTIREADKIVFFEKGVIVEAGNH 637
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
101-355 |
2.23e-09 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 60.18 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 101 VISGVSQPVLAIISGRMTNVLLvidplSKEFKTKTMENVYIFLGLGIFVSINDFCQYMCFQRVCSRMMTVMRNRYISSIL 180
Cdd:cd18589 6 VLSSLGEMAIPYYTGRMTDWIM-----NKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 181 RQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPvstICMtLLSRFL 260
Cdd:cd18589 81 RQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLP---LLL-LVPKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 261 EK---STGEELEK-VGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNsgKKHAIWGGFWSGFFGGIFFFWLMA-FMG 335
Cdd:cd18589 157 GKfqqSLAVQVQKsLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQ--KTYRLNKKEAAAYAVSMWTSSFSGlALK 234
|
250 260
....*....|....*....|.
gi 1678196980 336 CGILY-GGYLLKVGIIkSPGD 355
Cdd:cd18589 235 VGILYyGGQLVTAGTV-SSGD 254
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
440-678 |
2.25e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 440 LTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDgvdvRDLNLEWL-----RNVVGIV---------QQEPIL- 504
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLqqdppRNVEGTVydfvaegieEQAEYLk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 505 -FNDTIHnnLLFGNPdatRETMIRvcKMANA----------------HDFIKKMPKGYDTQIGDggvqLSGGQKQRVAIA 567
Cdd:PRK11147 100 rYHDISH--LVETDP---SEKNLN--ELAKLqeqldhhnlwqlenriNEVLAQLGLDPDAALSS----LSGGWLRKAALG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 568 RTLIRDPKVLLLDEATSALDAQSESVVQSALNNAsKGrTTIMIAHRLSTIRE-ADKIVFFEKGVIVE-AGNHEElvnlgg 645
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF-QG-SIIFISHDRSFIRNmATRIVDLDRGKLVSyPGNYDQ------ 240
|
250 260 270
....*....|....*....|....*....|...
gi 1678196980 646 rYFDlVKAQAFKQdpdeialekeEEDQFDEFDK 678
Cdd:PRK11147 241 -YLL-EKEEALRV----------EELQNAEFDR 261
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1115-1255 |
2.47e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1115 LVGPSGSGKSTCI----GMLERFydvTGGALRMDGqdiknislyhlrtqmALVG---QEPRLFVG-TIRENVCLGLKDVP 1186
Cdd:PRK11819 38 VLGLNGAGKSTLLrimaGVDKEF---EGEARPAPG---------------IKVGylpQEPQLDPEkTVRENVEEGVAEVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 -----LEKINQA---------------------------------LELA-NANRflgnLPDGiDTEVGerggQLSGGQKQ 1227
Cdd:PRK11819 100 aaldrFNEIYAAyaepdadfdalaaeqgelqeiidaadawdldsqLEIAmDALR----CPPW-DAKVT----KLSGGERR 170
|
170 180
....*....|....*....|....*...
gi 1678196980 1228 RIAIARALVRDPKILLLDEATSALDSES 1255
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1082-1293 |
3.50e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMlerfydVTG-------------GALRMDGQ-- 1146
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL------ITGdhpqgysndltlfGRRRGSGEti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1147 -DIK-NI----SLYHLrtqmalvgqEPRlfVGTIRENVCL-GLKDVPleKINQALELAN---ANRFLGNLpdGIDTEVGE 1216
Cdd:PRK10938 332 wDIKkHIgyvsSSLHL---------DYR--VSTSVRNVILsGFFDSI--GIYQAVSDRQqklAQQWLDIL--GIDKRTAD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1217 RGGQ-LSGGQkQRIA-IARALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRT--------------CITiaHRL 1279
Cdd:PRK10938 397 APFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaCIT--HRL 473
|
250
....*....|....
gi 1678196980 1280 SSIQNSDLIVYIDD 1293
Cdd:PRK10938 474 EFVPDGDIYRYVQT 487
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1109-1265 |
3.63e-09 |
|
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: 58.96 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLerfydvtGGALRMDGQDIKnislyhlrTQMALVGQEPRL----FVGTIRenvclglkD 1184
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIE--------IELDTVSYKPQYikadYEGTVR--------D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1185 VPLEKINQALELANANRFLGN---LPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQE 1261
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKplqIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
....
gi 1678196980 1262 ALDR 1265
Cdd:cd03237 157 VIRR 160
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1086-1286 |
3.66e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1086 NVKFSYPQrphQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI-KNISLYhlRTQMALVG 1164
Cdd:PRK13540 6 ELDFDYHD---QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTY--QKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QE----PRLfvgTIRENvCLglkdVPLEKINQALELANANRFLgNLPDGIDTEVGerggQLSGGQKQRIAIARALVRDPK 1240
Cdd:PRK13540 81 HRsginPYL---TLREN-CL----YDIHFSPGAVGITELCRLF-SLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678196980 1241 ILLLDEATSALDSESERAVQEALDRAR-EGRTCITIAHRLSSIQNSD 1286
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1109-1316 |
4.27e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.72 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLerfydvTG------GALRMDGQDIKNISLYHLRtQMALV-GQEPRLFVG-TIRENVCL 1180
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKML------TGilvptsGEVRVLGYVPFKRRKEFAR-RIGVVfGQRSQLWWDlPAIDSFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 gLK---DVPLEKINQAL-ELANanrfLGNLPDGIDTEVgeRggQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESE 1256
Cdd:COG4586 120 -LKaiyRIPDAEYKKRLdELVE----LLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1257 RAVQEALDR--AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQLKGKYFELI 1316
Cdd:COG4586 191 EAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
145-303 |
4.54e-09 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 59.33 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 145 LGIFVSIndFCQYMCfQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMV 224
Cdd:cd18548 51 LGLIAGI--LAGYFA-AKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIML 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 225 IASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEK 303
Cdd:cd18548 128 IGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDK 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
444-629 |
5.21e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 444 PGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQ-IDGVDVRDLNLEWLRNVVgivqqepilfndtihnnllfgnpdatr 522
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 523 etmirvckmanahdfikkmpkgydtqIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSAL---- 598
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678196980 599 ---NNASKGRTTIMIAHRLSTIREA------DKIVFFEKG 629
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLI 147
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
824-972 |
5.91e-09 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 59.06 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 824 TVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDnpAHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACVTIGFIN 903
Cdd:cd18573 62 VYLLRIAGERIVARLRKRLFKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYI 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 904 CWQVAILGTALIFLLGFIMAGLAFKISIVAAEHMEND-DAGKIAIEIIENVKTIQLLTRTRRFLNSYENE 972
Cdd:cd18573 140 SPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALaDATKVAEERLSNIRTVRAFAAERKEVERYAKK 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1110-1279 |
7.00e-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: 60.80 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI-KNISLYHLRtqmalVGQEPR------LFVGtiRENVCL-- 1180
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQN-----MGYCPQfdaiddLLTG--REHLYLya 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 GLKDVPLEKINQAlelanANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQ 1260
Cdd:TIGR01257 2038 RLRGVPAEEIEKV-----ANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180
....*....|....*....|
gi 1678196980 1261 EAL-DRAREGRTCITIAHRL 1279
Cdd:TIGR01257 2111 NTIvSIIREGRAVVLTSHSM 2130
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
432-632 |
7.13e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 432 AKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRdlnlewLRNVV---------------- 495
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRdairagiayvpedrkg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 496 -GIVQQEPILFN------DTIHNNLLFgnpDATRETmirvckmANAHDFIKKM---PKGYDTQIGdggvQLSGGQKQRVA 565
Cdd:COG1129 339 eGLVLDLSIRENitlaslDRLSRGGLL---DRRRER-------ALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 566 IARTLIRDPKVLLLDEATSALD--AQSEsvVQSALNN-ASKGRTTIMIAhrlSTIRE----ADKIVFFEKGVIV 632
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRElAAEGKAVIVIS---SELPEllglSDRILVMREGRIV 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1109-1306 |
7.27e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.02 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCI----GMLErfydvTGGALRMDGQDIKNISLYHLRTQMA-LVGQEPRLFVGTIRENVCLGLK 1183
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLarmaGLLP-----GSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1184 D-VPLEKINQAL-ELANANRFLGNLPDGIdtevgergGQLSGGQKQRIAIARALVR-------DPKILLLDEATSALDSe 1254
Cdd:PRK03695 96 DkTRTEAVASALnEVAEALGLDDKLGRSV--------NQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDV- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1255 serAVQEALDR-----AREGRTCITIAHRLS-SIQNSDLIVYIDDGRVQESGTHKELM 1306
Cdd:PRK03695 167 ---AQQAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
92-303 |
8.96e-09 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 58.23 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 92 LLLIGLITSVISGVSQPVLAIISGRMTNVLLvidplskefKTKTMENVYIF-LGLGIFVSINDFCQY-MCFQ--RVCSRM 167
Cdd:cd18549 3 LFFLDLFCAVLIAALDLVFPLIVRYIIDDLL---------PSKNLRLILIIgAILLALYILRTLLNYfVTYWghVMGARI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 168 MTVMRNRYISSILRQNAGWFDKNLSGTITTRL-NDNMErIQD----GVGDklgVLIRGIsMVIASVVISLIYEWRLALMM 242
Cdd:cd18549 74 ETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRItNDLFD-ISElahhGPED---LFISII-TIIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 243 LGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEK 303
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDE 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
433-629 |
1.06e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNL-EWLRNVVGIVQQE-PILFNDTIH 510
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkEALENGISMVHQElNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 511 NNLLFGN-PdaTRETMIRVCKManaHDFIKKMPKGYDTQIG--DGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:PRK10982 92 DNMWLGRyP--TKGMFVDQDKM---YRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678196980 588 AQSESVVQSALNN-ASKGRTTIMIAHRLSTIRE-ADKIVFFEKG 629
Cdd:PRK10982 167 EKEVNHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1109-1293 |
1.08e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGML---------------------ERFydvTGGALRMDGQDI--KNISLYHlRTQMalVGQ 1165
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlKRF---RGTELQDYFKKLanGEIKVAH-KPQY--VDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1166 EPRLFVGTIREnvcLgLKDVP----LEKINQALELANAnrflgnlpdgIDTEVGErggqLSGGQKQRIAIARALVRDPKI 1241
Cdd:COG1245 172 IPKVFKGTVRE---L-LEKVDergkLDELAEKLGLENI----------LDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1242 LLLDEATSALD----SESERAVQEAldrAREGRTCITIAHrlssiqnsDLIV--YIDD 1293
Cdd:COG1245 234 YFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEH--------DLAIldYLAD 280
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1109-1299 |
1.30e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDvTG---GALRMDGQ-----DIKN-----ISLYHlrTQMALVgqePRLfvgTIR 1175
Cdd:NF040905 26 EGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEvcrfkDIRDsealgIVIIH--QELALI---PYL---SIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1176 ENVCLGLKDVPLEKINQALELANANRFLG--NLPDGIDTEVGERGGqlsgGQKQRIAIARALVRDPKILLLDEATSAL-D 1252
Cdd:NF040905 97 ENIFLGNERAKRGVIDWNETNRRARELLAkvGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAALnE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678196980 1253 SESERAVQEALDRAREGRTCITIAHRLSSI-QNSDLIVYIDDGRVQES 1299
Cdd:NF040905 173 EDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIET 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
436-642 |
1.87e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.92 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 436 NGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNvVGIVQ--QEPILFND-TIHNN 512
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRtfQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 513 L---------------LFGNPD---ATREtmirvcKMANAHDFIKKM--PKGYDTQIGDggvqLSGGQKQRVAIARTLIR 572
Cdd:PRK11300 101 LlvaqhqqlktglfsgLLKTPAfrrAESE------ALDRAATWLERVglLEHANRQAGN----LAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 573 DPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELVN 642
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRN 243
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
162-301 |
1.92e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 57.50 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 162 RVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALM 241
Cdd:cd18546 65 RTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALV 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 242 MLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKY 301
Cdd:cd18546 145 ALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
387-639 |
2.20e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 387 AASIYKTIDRVpKID---PYSR--------HGKKIEKVVgkVTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSG 455
Cdd:PRK15064 282 ATSRAKQIDKI-KLEevkPSSRqnpfirfeQDKKLHRNA--LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 456 CGKSTSVGLLTRLYEPEQGSVQidgvdvrdlnleWLRNV-VGIVQQepilfnDTIHNnllFGNpDAT------------- 521
Cdd:PRK15064 356 VGKTTLLRTLVGELEPDSGTVK------------WSENAnIGYYAQ------DHAYD---FEN-DLTlfdwmsqwrqegd 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 522 RETMIR--VCKMANAHDFIKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQS-ESvvqsaL 598
Cdd:PRK15064 414 DEQAVRgtLGRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESiES-----L 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 599 NNA---SKGrTTIMIAHRlstiRE-----ADKIV-FFEKGVIVEAGNHEE 639
Cdd:PRK15064 478 NMAlekYEG-TLIFVSHD----REfvsslATRIIeITPDGVVDFSGTYEE 522
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1082-1279 |
2.35e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqpVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ-DIKNI-SLYHLRTQ 1159
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVpQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1160 MAL-VGQEPRLFVGTIRENVCLGLKDVplekinQALELANANRflgnlpdgidtevgergGQLSGGQKQRIAIARALVRD 1238
Cdd:PRK09544 82 LPLtVNRFLRLRPGTKKEDILPALKRV------QAGHLIDAPM-----------------QKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALDRAREGRTC--ITIAHRL 1279
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCavLMVSHDL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
433-639 |
2.76e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVL-NGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQI-DGVDV------RDlNLEWLRNVvgivQQEPIL 504
Cdd:TIGR03719 335 KLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLayvdqsRD-ALDPNKTV----WEEISG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 505 FNDTIhnnlLFGNpdatRETMIRV-CKMANahdFikkmpKGYDTQ--IGdggvQLSGGQKQRVAIARTLIRDPKVLLLDE 581
Cdd:TIGR03719 410 GLDII----KLGK----REIPSRAyVGRFN---F-----KGSDQQkkVG----QLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 582 ATSALDAQSESVVQSALNNAskGRTTIMIAH------RLST---IREAD-KIVFFEkgviveaGNHEE 639
Cdd:TIGR03719 470 PTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAThilAFEGDsHVEWFE-------GNFSE 528
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1110-1280 |
3.90e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.84 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLE--------------------RFYdvTGGAL-----RMDGQDIKNIslyhLRTQMalVG 1164
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAgklkpnlgkfddppdwdeilDEF--RGSELqnyftKLLEGDVKVI----VKPQY--VD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1165 QEPRLFVGTIRENvcLGLKDV--PLEKINQALELANAnrflgnlpdgIDTEVGerggQLSGGQKQRIAIARALVRDPKIL 1242
Cdd:cd03236 98 LIPKAVKGKVGEL--LKKKDErgKLDELVDQLELRHV----------LDRNID----QLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678196980 1243 LLDEATSALDS----ESERAVQEaldRAREGRTCITIAHRLS 1280
Cdd:cd03236 162 FFDEPSSYLDIkqrlNAARLIRE---LAEDDNYVLVVEHDLA 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1100-1305 |
4.77e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1100 MKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlYHLRTQM--ALVGQE----------P 1167
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQElsvideltvlE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1168 RLFVGTIRENVCLGLKDVPLEKINQalelaNANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEA 1247
Cdd:PRK09700 100 NLYIGRHLTKKVCGVNIIDWREMRV-----RAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1248 TSALDSESERAVQEALDRAR-EGRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKEL 1305
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1109-1293 |
5.14e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGML---------------------ERFydvTGGAL-----RMDGQDIKNIslyhLRTQMal 1162
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF---RGTELqnyfkKLYNGEIKVV----HKPQY-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1163 VGQEPRLFVGTIREnvcLgLKDVP----LEKINQALELANAnrflgnlpdgIDTEVGErggqLSGGQKQRIAIARALVRD 1238
Cdd:PRK13409 169 VDLIPKVFKGKVRE---L-LKKVDergkLDEVVERLGLENI----------LDRDISE----LSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1239 PKILLLDEATSALDseseraVQEALDRAR------EGRTCITIAHrlssiqnsDLIV--YIDD 1293
Cdd:PRK13409 231 ADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEH--------DLAVldYLAD 279
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-303 |
5.54e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 56.01 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 171 MRNRYISSILRQNAGWFDKNLSGTITTRL-ND--NMER-IQDGVGDklgVLIRGISMVIASVVISLIyEWRLALMMLGLI 246
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRViNDvaNVERlIADGIPQ---GITNVLTLVGVAIILFSI-NPKLALLTLIPI 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 247 PVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEK 303
Cdd:cd18778 151 PFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA 207
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
814-975 |
5.91e-08 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 56.01 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 814 LGIWFFQTLST----VMFAIVSENLGVRFRVAAFRNLLYQDAAYFDnpAHAPGSLITRLAAD----PPCVKAVVDgrmmQ 885
Cdd:cd18574 49 LGLYLLQSLLTfayiSLLSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADvqefKSSFKQCVS----Q 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 886 VVYATAAVIAC-VTIGFINCWQVAILGTAL--IFLLGFIMAGLAFKISIVAAEhmENDDAGKIAIEIIENVKTIQLLTRT 962
Cdd:cd18574 123 GLRSVTQTVGCvVSLYLISPKLTLLLLVIVpvVVLVGTLYGSFLRKLSRRAQA--QVAKATGVADEALGNIRTVRAFAME 200
|
170
....*....|...
gi 1678196980 963 RRFLNSYENESKK 975
Cdd:cd18574 201 DRELELYEEEVEK 213
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
137-313 |
8.77e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 55.21 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 137 ENVYIFLGLGIFVSindFCQYMCFQRVCSRMMTVMRNR--------YISSILRQNAGWFDKNLSGTITTRLNDNMeRIQD 208
Cdd:cd18555 38 LNLLNVLGIGILIL---FLLYGLFSFLRGYIIIKLQTKldkslmsdFFEHLLKLPYSFFENRSSGDLLFRANSNV-YIRQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 209 GVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTI 288
Cdd:cd18555 114 ILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETI 193
|
170 180
....*....|....*....|....*....
gi 1678196980 289 QAFNGQEEMVAK----YEKQLNSGKKHAI 313
Cdd:cd18555 194 KSLGSEKNIYKKwenlFKKQLKAFKKKER 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
428-612 |
8.92e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.16 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 428 TRKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWL---RNVVGIVQQEPIL 504
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 505 FND-TIHNNLLFGNPDATR--ETMIRVCKMANAHDF-----IKKMPKgydtqigdggvQLSGGQKQRVAIARTLIRDPKV 576
Cdd:PRK11831 96 FTDmNVFDNVAYPLREHTQlpAPLLHSTVMMKLEAVglrgaAKLMPS-----------ELSGGMARRAALARAIALEPDL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678196980 577 LLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAH 612
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISelNSALGVTCVVVSH 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1109-1255 |
1.04e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLerfydvTGGALRMDGQDIKNISLYHLRTQmalvgQEP-RLFVGTIRENVCLGLKDVP- 1186
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGRIIYEQDLIVARLQ-----QDPpRNVEGTVYDFVAEGIEEQAe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1187 -----------------------LEKINQALELANANRF-------LGNLPDGIDTEVGErggqLSGGQKQRIAIARALV 1236
Cdd:PRK11147 97 ylkryhdishlvetdpseknlneLAKLQEQLDHHNLWQLenrinevLAQLGLDPDAALSS----LSGGWLRKAALGRALV 172
|
170
....*....|....*....
gi 1678196980 1237 RDPKILLLDEATSALDSES 1255
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
162-303 |
1.29e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 54.82 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 162 RVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALM 241
Cdd:cd18563 69 RLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALL 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 242 MLGLIPVsticMTLLSRFLEKSTGEELEKVGEAGA----IAEECLMGVRTIQAFNGQEEMVAKYEK 303
Cdd:cd18563 149 VLIPVPL----VVWGSYFFWKKIRRLFHRQWRRWSrlnsVLNDTLPGIRVVKAFGQEKREIKRFDE 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1109-1300 |
1.31e-07 |
|
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: 53.10 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIgmLERFYdvTGGALRMdgqdIKNISLYhlrtqmalvGQEPRLFVGTIRENVCLGLKDVPLe 1188
Cdd:cd03238 20 LNVLVVVTGVSGSGKSTLV--NEGLY--ASGKARL----ISFLPKF---------SRNKLIFIDQLQFLIDVGLGYLTL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1189 kiNQALelananrflgnlpdgidtevgergGQLSGGQKQRIAIARALVRDPK--ILLLDEATSALDSESERAVQEALDRA 1266
Cdd:cd03238 82 --GQKL------------------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1678196980 1267 R-EGRTCITIAHRLSSIQNSDLIVYI------DDGRVQESG 1300
Cdd:cd03238 136 IdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1074-1307 |
1.33e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.99 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1074 TKPEIRGNILFE--NVKFSYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYD-VTGGALRMDGQ--DI 1148
Cdd:TIGR02633 248 HEPHEIGDVILEarNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1149 KNiSLYHLRTQMALVGQE-------PRLFVGtirENVCLGLKD--VPLEKINQALELANANRFLGNL------PD-GIdt 1212
Cdd:TIGR02633 328 RN-PAQAIRAGIAMVPEDrkrhgivPILGVG---KNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLkvktasPFlPI-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1213 evgergGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVY 1290
Cdd:TIGR02633 402 ------GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLV 475
|
250
....*....|....*..
gi 1678196980 1291 IDDGRVQESGTHKELMQ 1307
Cdd:TIGR02633 476 IGEGKLKGDFVNHALTQ 492
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
109-313 |
1.59e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.41 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 109 VLAIISGRMTNVLLVIDPLSKEF------KTKTMENVYIFLGL-GIFVSINDFCQYMcFQRVCSRM-MTVMRNryissiL 180
Cdd:cd18540 5 ILLIILMLLVALLDAVFPLLTKYaidhfiTPGTLDGLTGFILLyLGLILIQALSVFL-FIRLAGKIeMGVSYD------L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 181 RQNA---------GWFDKNLSGTITTRLNDNMERIQD----GVGDklgvLIRGISMVIASVVISLIYEWRLALMMLGLIP 247
Cdd:cd18540 78 RKKAfehlqtlsfSYFDKTPVGWIMARVTSDTQRLGEiiswGLVD----LVWGITYMIGILIVMLILNWKLALIVLAVVP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 248 VsticMTLLSRFLEKSTGEELEKVGEA-----GAIaEECLMGVRTIQAFNGQEEMVAKYEKQLNSGKKHAI 313
Cdd:cd18540 154 V----LAVVSIYFQKKILKAYRKVRKInsritGAF-NEGITGAKTTKTLVREEKNLREFKELTEEMRRASV 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
435-629 |
1.73e-07 |
|
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: 52.71 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVglLTRLYEPEQgsvqidgvdvrdlnlewlrnvvgivqqepilfndtihNNLL 514
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGK-------------------------------------ARLI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 515 FGNPDATRETMIRVCKMAnahdFIKKMPKGYDTqIGDGGVQLSGGQKQRVAIARTLIRDPK--VLLLDEATSALDAQSES 592
Cdd:cd03238 52 SFLPKFSRNKLIFIDQLQ----FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678196980 593 VVQSALNN-ASKGRTTIMIAHRLSTIREADKIVFFEKG 629
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
139-306 |
1.86e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 54.43 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 139 VYIFLGLGIFVSINdFCQYMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLI 218
Cdd:cd18580 43 VYAALLVLASVLLV-LLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 219 RGISMVIASVVISLIYEWRLALMmlgLIPVSTICMTLLSRFLekSTGEELEKVgeaGAIA--------EECLMGVRTIQA 290
Cdd:cd18580 122 QSLFSVLGSLIVIAIVSPYFLIV---LPPLLVVYYLLQRYYL--RTSRQLRRL---ESESrsplyshfSETLSGLSTIRA 193
|
170
....*....|....*.
gi 1678196980 291 FNGQEEMVAKYEKQLN 306
Cdd:cd18580 194 FGWQERFIEENLRLLD 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
430-638 |
2.37e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 430 KEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTR-----------LY--------EPEQGS-----------VQID 479
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdiLFkgesildlEPEERAhlgiflafqypIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 480 GVDvrdlNLEWLRNVV-------GIVQQEPILFNDTIHNNLLFGNPDATretmirvckmanahdFIKKmpkgydtQIGDG 552
Cdd:CHL00131 98 GVS----NADFLRLAYnskrkfqGLPELDPLEFLEIINEKLKLVGMDPS---------------FLSR-------NVNEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 553 gvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAH--RLSTIREADKIVFFEKG 629
Cdd:CHL00131 152 ---FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNG 228
|
....*....
gi 1678196980 630 VIVEAGNHE 638
Cdd:CHL00131 229 KIIKTGDAE 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1078-1252 |
2.98e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1078 IRG-NILFENVKFSypqrphqpvmkqlqwtALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDI-KNISLYH 1155
Cdd:PRK13538 10 ERDeRILFSGLSFT----------------LNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 lrTQMALVGQEPrlfvgtirenvclGLKDV--PLEKInqalelananRFLGNLPDGIDTE--------VGERG------G 1219
Cdd:PRK13538 74 --QDLLYLGHQP-------------GIKTEltALENL----------RFYQRLHGPGDDEalwealaqVGLAGfedvpvR 128
|
170 180 190
....*....|....*....|....*....|...
gi 1678196980 1220 QLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
93-292 |
3.93e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 53.34 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 93 LLIGLITSVISGVSQ---PVL------AIISGRMTNVLLVIDPLSkefkTKTMENVYIFLG---LGIFV--SINDFCQYM 158
Cdd:cd18565 1 LVLGLLASILNRLFDlapPLLigvaidAVFNGEASFLPLVPASLG----PADPRGQLWLLGgltVAAFLleSLFQYLSGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 159 CFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRL 238
Cdd:cd18565 77 LWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 239 ALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFN 292
Cdd:cd18565 157 ALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFT 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
417-629 |
4.09e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKEAK----------VLNGLNLTVEPGTSVALVGHSGCGKSTSVGLL----TRLYEpeQGSVQIDGVD 482
Cdd:PLN03140 868 MSFDDVNYFVDMPAEMKeqgvtedrlqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGFP 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 483 VRDlnlEWLRNVVGIVQQepilfNDtIHNnllfgnPDAT-RETMI-----RVCKMANAHD---FIKK------MPKGYDT 547
Cdd:PLN03140 946 KKQ---ETFARISGYCEQ-----ND-IHS------PQVTvRESLIysaflRLPKEVSKEEkmmFVDEvmelveLDNLKDA 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 548 QIGDGGVQ-LSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSAL-NNASKGRTTIMIAHRLST-IREA-DKI 623
Cdd:PLN03140 1011 IVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfDEL 1090
|
....*.
gi 1678196980 624 VFFEKG 629
Cdd:PLN03140 1091 LLMKRG 1096
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
818-990 |
4.81e-07 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 53.19 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 818 FFQTLSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDGRMMQVVYATAAVIACV 897
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 898 TIGFINCWQVAILGTALIFLLGFIMAGLAFKISIVAAEHME-NDDAGKIAIEIIENVKTIQLLTRTRRFLNSYENESKKR 976
Cdd:cd18552 132 GVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQEsMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERL 211
|
170
....*....|....
gi 1678196980 977 KRTELRKSVYEAVN 990
Cdd:cd18552 212 RRLSMKIARARALS 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1080-1264 |
5.05e-07 |
|
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: 54.17 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1080 GNILFENVKFSYPqrphqpvmkqlqwtalRGQTVALVGPSGSGKSTCIGMLerfydvTG------GALRMdGQDIKnisl 1153
Cdd:TIGR03719 334 DKLLIDDLSFKLP----------------PGGIVGVIGPNGAGKSTLFRMI------TGqeqpdsGTIEI-GETVK---- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1154 yhlrtqMALVGQ-----EPRlfvGTIRENVCLGLKDVPLEK--INQAlelANANRFlgNLpDGIDTEvgERGGQLSGGQK 1226
Cdd:TIGR03719 387 ------LAYVDQsrdalDPN---KTVWEEISGGLDIIKLGKreIPSR---AYVGRF--NF-KGSDQQ--KKVGQLSGGER 449
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678196980 1227 QRIAIARALVRDPKILLLDEATSALDSESERAVQEALD 1264
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1109-1288 |
7.17e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLerfydvtGGALRMDGQDIK---NISlYhlRTQMALVGQEprlfvGTIRENvclglkdv 1185
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEVDpelKIS-Y--KPQYIKPDYD-----GTVEDL-------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1186 pLEKINQAL-------ELANanRFlgNLPDGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERA 1258
Cdd:PRK13409 421 -LRSITDDLgssyyksEIIK--PL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|..
gi 1678196980 1259 VQEALDRAREGR--TCITIAHRLSSIqnsDLI 1288
Cdd:PRK13409 492 VAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1110-1255 |
8.79e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.11 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCI----GMLERFYDVTGgALRMDGQDIKNISLYHlRTQMALVGQE----PRLfvgTIRENVCLG 1181
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLkalaNRTEGNVSVEG-DIHYNGIPYKEFAEKY-PGEIIYVSEEdvhfPTL---TVRETLDFA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1182 LKdvplekinqalelANANRFLgnlpdgidtevgeRGgqLSGGQKQRIAIARALVRDPKILLLDEATSALDSES 1255
Cdd:cd03233 108 LR-------------CKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1219-1307 |
1.22e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1219 GQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGRTCITI---------AHRLssiqnsDLIV 1289
Cdd:NF033858 135 GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVlvataymeeAERF------DWLV 208
|
90
....*....|....*...
gi 1678196980 1290 YIDDGRVQESGTHKELMQ 1307
Cdd:NF033858 209 AMDAGRVLATGTPAELLA 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
439-639 |
1.32e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 439 NLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVR-----------------DlnlewlRNVVGIVQQE 501
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairagimlcpeD------RKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 502 PILFNDTI----HNNLLFGNPDATRETmirvckmANAHDFIKKM----PKGyDTQIGdggvQLSGGQKQRVAIARTLIRD 573
Cdd:PRK11288 347 SVADNINIsarrHHLRAGCLINNRWEA-------ENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 574 PKVLLLDEATSALD--AQSEsVVQSALNNASKGRTTIMIAHRL-STIREADKIVFFEKGVIVEAGNHEE 639
Cdd:PRK11288 415 MKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
536-587 |
1.45e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 1.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678196980 536 DFIK----KMPkGYDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:PRK10762 377 DFIRlfniKTP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
797-1008 |
1.54e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 51.39 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 797 KMMHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDnpAHAPGSLITRLAADppcvk 876
Cdd:cd18572 30 GSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSD----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 877 avvdgrmmqvvyaTAAVIACVTIGFINCWQVAILGT-ALIFLLG---------FIMAGLAFKISIVAAEHMEN------- 939
Cdd:cd18572 103 -------------CQKVSDPLSTNLNVFLRNLVQLVgGLAFMFSlswrltllaFITVPVIALITKVYGRYYRKlskeiqd 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678196980 940 --DDAGKIAIEIIENVKTIQlltrtrrflnSYENESKKRKRTE------LRKSVYEAVNYCISQ--NFMYYMSCFCFAL 1008
Cdd:cd18572 170 alAEANQVAEEALSNIRTVR----------SFATEEREARRYEraldkaLKLSVRQALAYAGYVavNTLLQNGTQVLVL 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1110-1277 |
1.56e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCI----GMLERFYDVTGGALRMDG---QDIKNislyHLRTQMALVGQE----PRLFVGtirenv 1178
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLktiaSNTDGFHIGVEGVITYDGitpEEIKK----HYRGDVVYNAETdvhfPHLTVG------ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1179 clglkdvplekinQALELANANRFLGNLPDGI-----------------------DTEVGE---RGgqLSGGQKQRIAIA 1232
Cdd:TIGR00956 157 -------------ETLDFAARCKTPQNRPDGVsreeyakhiadvymatyglshtrNTKVGNdfvRG--VSGGERKRVSIA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1678196980 1233 RALVRDPKILLLDEATSALDSESeravqeALDRAREGRTCITIAH 1277
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILD 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
433-587 |
2.75e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 433 KVL-NGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIdGVDVRdlnlewlrnvVGIVQQepilFNDTIhn 511
Cdd:PRK11819 337 RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVDQ----SRDAL-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 512 nllfgNPDATRETMIrvckmANAHDFIK----KMP----------KGYDTQ--IGdggvQLSGGQKQRVAIARTLIRDPK 575
Cdd:PRK11819 400 -----DPNKTVWEEI-----SGGLDIIKvgnrEIPsrayvgrfnfKGGDQQkkVG----VLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|..
gi 1678196980 576 VLLLDEATSALD 587
Cdd:PRK11819 466 VLLLDEPTNDLD 477
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1084-1280 |
3.70e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFsYPQRPhqPVMKQ-------LQwtALRGQT--------VALVGPSGSGKSTCIGMLERfyDVTGGAL----RMD 1144
Cdd:PLN03140 870 FDDVNY-FVDMP--AEMKEqgvtedrLQ--LLREVTgafrpgvlTALMGVSGAGKTTLMDVLAG--RKTGGYIegdiRIS 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1145 G-----QDIKNISLYHLRTQMalvgQEPRLfvgTIRENVC----LGL-KDVPLEK----INQALELANanrfLGNLPDGI 1210
Cdd:PLN03140 943 GfpkkqETFARISGYCEQNDI----HSPQV---TVRESLIysafLRLpKEVSKEEkmmfVDEVMELVE----LDNLKDAI 1011
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1211 DTEVGERGgqLSGGQKQRIAIARALVRDPKILLLDEATSALDSESE----RAVQEALDrarEGRTCITIAHRLS 1280
Cdd:PLN03140 1012 VGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAaivmRTVRNTVD---TGRTVVCTIHQPS 1080
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1084-1246 |
3.73e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.34 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1084 FENVKFSYPQRPHQ------PVMKQLQwtalRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLR 1157
Cdd:COG4615 330 LRGVTYRYPGEDGDegftlgPIDLTIR----RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1158 TQMALVGQEPRLFvgtirENVcLGLKDVPL-EKINQALElananRFlgnlpdGIDTEVGERGG-----QLSGGQKQRIAI 1231
Cdd:COG4615 406 QLFSAVFSDFHLF-----DRL-LGLDGEADpARARELLE-----RL------ELDHKVSVEDGrfsttDLSQGQRKRLAL 468
|
170
....*....|....*
gi 1678196980 1232 ARALVRDPKILLLDE 1246
Cdd:COG4615 469 LVALLEDRPILVFDE 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
452-587 |
4.09e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 452 GHSGCGKSTSVGLLTRLYEPEQGSVQIDG--VDVRDLNLewlRNVVGIVQQEPILFND-TIHNNL-----LFGNPDATRE 523
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAT---RRRVGYMSQAFSLYGElTVRQNLelharLFHLPAAEIA 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 524 TmiRVCKMANAHDFIKKMpkgyDTQIGDggvqLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:NF033858 376 A--RVAEMLERFDLADVA----DALPDS----LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
417-637 |
4.21e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvdvrDLNLEW------ 490
Cdd:PRK10636 2 IVFSSLQIRRGVRV---LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQLAWvnqetp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 491 ------LRNVVG----IVQQEPILFNDTIHNN-----LLFGNPDATRETMIRvckmANAHDFIKKMpkGY-DTQIGDGGV 554
Cdd:PRK10636 75 alpqpaLEYVIDgdreYRQLEAQLHDANERNDghaiaTIHGKLDAIDAWTIR----SRAASLLHGL--GFsNEQLERPVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKgrTTIMIAHR---LSTIreADKIVFFEKGVI 631
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISHDrdfLDPI--VDKIIHIEQQSL 224
|
....*..
gi 1678196980 632 VE-AGNH 637
Cdd:PRK10636 225 FEyTGNY 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
415-587 |
4.86e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 415 GKVTF--ENVHFRYPTRKeakVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIdGVdvrdlNLEwlr 492
Cdd:PRK11147 316 GKIVFemENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GT-----KLE--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 493 nVVGIVQQEPILFND-TIHNNLlfgnPDATRETMIRVCK---MANAHDFIKKmPKGYDTQIGdggvQLSGGQKQRVAIAR 568
Cdd:PRK11147 384 -VAYFDQHRAELDPEkTVMDNL----AEGKQEVMVNGRPrhvLGYLQDFLFH-PKRAMTPVK----ALSGGERNRLLLAR 453
|
170
....*....|....*....
gi 1678196980 569 TLIRDPKVLLLDEATSALD 587
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLD 472
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1109-1273 |
6.01e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKS----TCIGMLErfydVTGGALRMDGQDIKNIS--------LYHL---RTQMALVGQEprlfvgT 1173
Cdd:COG3845 283 AGEILGIAGVAGNGQSelaeALAGLRP----PASGSIRLDGEDITGLSprerrrlgVAYIpedRLGRGLVPDM------S 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1174 IRENVCLG-LKDVPLEK---INQALELANANRFLGNL---PDGIDTEVGerggQLSGGQKQRIAIARALVRDPKILLLDE 1246
Cdd:COG3845 353 VAENLILGrYRRPPFSRggfLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180
....*....|....*....|....*..
gi 1678196980 1247 ATSALDSESERAVQEALDRAREGRTCI 1273
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAGAAV 455
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1219-1312 |
6.32e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1219 GQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAV-QEALDRAREGRTCITIAHRLSSIQN-SDLIVYIDDGRV 1296
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
90 100
....*....|....*....|.
gi 1678196980 1297 -----QESGTHKELMQLKGKY 1312
Cdd:PRK10982 470 agivdTKTTTQNEILRLASLH 490
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
540-647 |
6.94e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 540 KMPkGYDTQIGdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD--AQSEsVVQSALNNASKGRTTIMIAhrlSTI 617
Cdd:PRK10982 381 KTP-GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIIS---SEM 451
|
90 100 110
....*....|....*....|....*....|....*....
gi 1678196980 618 RE----ADKIVFFEKGV---IVEAG--NHEELVNLGGRY 647
Cdd:PRK10982 452 PEllgiTDRILVMSNGLvagIVDTKttTQNEILRLASLH 490
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
802-989 |
7.98e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 49.43 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 802 LAMSVIAHCAAGLGIWffqtlSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDG 881
Cdd:cd18564 58 AALVGIALLRGLASYA-----GTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 882 RMMQVVYATAAVIACVTIGF-INcWQVAILGTALIFLLGFIMAGLAFKISIVAAEHMENDdaGKIAI---EIIENVKTIQ 957
Cdd:cd18564 131 GVLPLLTNLLTLVGMLGVMFwLD-WQLALIALAVAPLLLLAARRFSRRIKEASREQRRRE--GALASvaqESLSAIRVVQ 207
|
170 180 190
....*....|....*....|....*....|..
gi 1678196980 958 LLTRTRRFLNSYENESKKRKRTELRKSVYEAV 989
Cdd:cd18564 208 AFGREEHEERRFARENRKSLRAGLRAARLQAL 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1114-1295 |
8.39e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1114 ALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYH-LRTQMALVGQEPRLFVG-TIRENVCLGLKDVPLEKIN 1191
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQrSVMDNMWLGRYPTKGMFVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1192 QALELANANRFLGNLpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALdseSERAVQEALD--RAREG 1269
Cdd:PRK10982 108 QDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNHLFTiiRKLKE 182
|
170 180
....*....|....*....|....*....
gi 1678196980 1270 RTC--ITIAHRLSSI-QNSDLIVYIDDGR 1295
Cdd:PRK10982 183 RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
550-659 |
9.05e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 550 GDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIRE--ADKIVFFE 627
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218
|
90 100 110
....*....|....*....|....*....|...
gi 1678196980 628 KGVIVEAGNHEEL-VNLGGRYFDLVKAQAFKQD 659
Cdd:NF000106 219 RGRVIADGKVDELkTKVGGRTLQIRPAHAAELD 251
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
162-304 |
1.06e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 49.02 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 162 RVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGdKLGVLIRGISMVIASVVISLIYEWRLALM 241
Cdd:cd18543 65 RLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALV 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 242 MLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFnGQEE-MVAKYEKQ 304
Cdd:cd18543 144 ALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAF-GRERrELDRFEAA 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1221-1279 |
1.06e-05 |
|
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: 47.57 E-value: 1.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1221 LSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRL 1279
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDL 132
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1110-1282 |
1.20e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGML-ERfydVTGGAL----RMDG-----------------QDIknislyHLRTqmaLVGQEP 1167
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLaER---VTTGVItggdRLVNgrpldssfqrsigyvqqQDL------HLPT---STVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1168 RLFVGTIRE--NVCLGLKDVPLEKINQALELAnanrflgnlpDGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILL-L 1244
Cdd:TIGR00956 857 LRFSAYLRQpkSVSKSEKMEYVEEVIKLLEME----------SYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|....*....
gi 1678196980 1245 DEATSALDSESERAVQEALDR-AREGRTCITIAHRLSSI 1282
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
438-631 |
1.32e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 438 LNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLN--------LEWL---RNVVGIVQQEPILFN 506
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlargLVYLpedRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 507 D---TIHNNLLFGNPDATRETMIRVCKMANahdfIKKmpkgydTQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEAT 583
Cdd:PRK15439 362 VcalTHNRRGFWIKPARENAVLERYRRALN----IKF------NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678196980 584 SALDAQSES-VVQSALNNASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:PRK15439 432 RGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1221-1288 |
1.41e-05 |
|
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: 49.40 E-value: 1.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1221 LSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGR--TCITIAHRLSSIqnsDLI 1288
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYI 522
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
435-641 |
1.49e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 435 LNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDG-VDVRDLNLEWLRNVVGIvqqEPILFndtihNNL 513
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAGLSGQLTGI---ENIEF-----KML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 514 LFG-NPDATRETMIRVCKMANAHDFIKKMPKGYdtqigdggvqlSGGQKQRVAIARTLIRDPKVLLLDEATSALDaqsES 592
Cdd:PRK13546 112 CMGfKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---QT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 593 VVQSALNN----ASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVIVEAGNHEELV 641
Cdd:PRK13546 178 FAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1221-1289 |
1.78e-05 |
|
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: 47.99 E-value: 1.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1221 LSGGQKQRIAIARALVR---DPKILLLDEATSALDSESERAVQEALDRARE-GRTCITIAHRLSSIQNSDLIV 1289
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWII 242
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
382-595 |
1.79e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 382 NARVAA--ASIYKTIDRVPKID--------------PYSRHGKKIekvvgkVTFENVHFRYPtrKEAKVLNGLNLTVEPG 445
Cdd:PLN03073 464 NAKRASlvQSRIKALDRLGHVDavvndpdykfefptPDDRPGPPI------ISFSDASFGYP--GGPLLFKNLNFGIDLD 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 446 TSVALVGHSGCGKSTSVGLLTRLYEPEQGSVqIDGVDVRdlnlewlrnvVGIVQQEPILFNDTIHNNLLF------GNPd 519
Cdd:PLN03073 536 SRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVR----------MAVFSQHHVDGLDLSSNPLLYmmrcfpGVP- 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 520 atrETMIRvckmanAHdfikkmpkgydtqIGDGGVQ----------LSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQ 589
Cdd:PLN03073 604 ---EQKLR------AH-------------LGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
....*..
gi 1678196980 590 S-ESVVQ 595
Cdd:PLN03073 662 AvEALIQ 668
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
141-306 |
2.15e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 47.94 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 141 IFLGLGIFVSINDFC-QYMCFQrVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNmERIQDG-VGDKLGVLI 218
Cdd:cd18568 47 GLLIVGIFQILLSAVrQYLLDY-FANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFlTRSALTTIL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 219 RGIsMVIASVVISLIYEWRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMV 298
Cdd:cd18568 125 DLL-MVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIR 203
|
....*...
gi 1678196980 299 AKYEKQLN 306
Cdd:cd18568 204 WRWENKFA 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
555-642 |
2.56e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALN--NASKGRTTIMIAHRLSTIRE-ADKIVFFEKGVI 631
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|.
gi 1678196980 632 VEAGNHEELVN 642
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1207-1265 |
2.74e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 43.76 E-value: 2.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 1207 PDGIDTEVGERGGQLSGGQKQR---IAIARALV----------RDPKILLLDEATSALDSESERAVQEALDR 1265
Cdd:pfam13558 19 EDGSEVETYRRSGGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
441-615 |
2.80e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.36 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 441 TVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGvdvrdlnlEW---LRNVVGIVQQEPI--LFNDTI------ 509
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPP--------DWdeiLDEFRGSELQNYFtkLLEGDVkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 510 -HNNLLfgnPDATRETMIRVCKMANAHDFIKKMPKGYD-TQIGDGGV-QLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:cd03236 94 qYVDLI---PKAVKGKVGELLKKKDERGKLDELVDQLElRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 1678196980 587 D-AQSESVVQSALNNASKGRTTIMIAHRLS 615
Cdd:cd03236 171 DiKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
795-929 |
2.95e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 47.43 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 795 GGKMMHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNpAHApGSLITRLAADPPC 874
Cdd:cd18542 31 GGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK-ART-GDLMSRCTSDVDT 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 875 VKAVVDGRMMQVVYATAAVIACVTIGFINCWQVAILGTALIFLLGFIMAGLAFKI 929
Cdd:cd18542 109 IRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKV 163
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1220-1291 |
3.01e-05 |
|
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: 45.81 E-value: 3.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1220 QLSGGQKQRIAIA-----RALVRDPkILLLDEATSALDSESERAVQEAL-DRAREGRTCITIAHRLSSIQNSDLIVYI 1291
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
555-614 |
3.05e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRL 614
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
534-640 |
3.38e-05 |
|
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: 48.47 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 534 AHDFIKKMPK-------------GYdTQIGDGGVQLSGGQKQRVAIARTLIRD---PKVLLLDEATSALD----AQSESV 593
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHfddiKKLLEV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 594 VQSAlnnASKGRTTIMIAHRLSTIREADKIVFF------EKGVIVEAGNHEEL 640
Cdd:TIGR00630 875 LQRL---VDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
554-627 |
3.45e-05 |
|
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: 46.03 E-value: 3.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 554 VQLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASK--GRTTIMIAHRLSTIRE-ADKIVFFE 627
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
450-612 |
4.33e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 450 LVGHSGCGKSTSVGLLTRLYEPEQGSVQIDgVDVRdlnlewlrnvVGIVQQEPILFN-----DTI---HNNL-------- 513
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-PNER----------LGKLRQDQFAFEeftvlDTVimgHTELwevkqerd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 514 -LFGNPDATRETMIRVckmANAHDFIKKMpKGYDTQIGDG----GV------------QLSGGQKQRVAIARTLIRDPKV 576
Cdd:PRK15064 101 rIYALPEMSEEDGMKV---ADLEVKFAEM-DGYTAEARAGelllGVgipeeqhyglmsEVAPGWKLRVLLAQALFSNPDI 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678196980 577 LLLDEATSALDAQSESVVQSALNNasKGRTTIMIAH 612
Cdd:PRK15064 177 LLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
431-598 |
4.47e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 431 EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQI-DGVDV---RDLNLEWLRnvvgiVQQEPIlfn 506
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLgyfAQHQLEFLR-----ADESPL--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 507 dtihNNLLFGNPDATrETMIRvckmanahDFIKKMPKGYDtQIGDGGVQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:PRK10636 396 ----QHLARLAPQEL-EQKLR--------DYLGGFGFQGD-KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170
....*....|..
gi 1678196980 587 DAQSESVVQSAL 598
Cdd:PRK10636 462 DLDMRQALTEAL 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
417-587 |
5.12e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 417 VTFENVHFRYptrKEAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRD----------- 485
Cdd:NF033858 2 ARLEGVSHRY---GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarhrravcpri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 486 ------L--NLewlrnvvgivqqEPILfndTIHNNL-----LFGNPDATRETMI-RVCKMANAHDFIKKmPKGydtqigd 551
Cdd:NF033858 79 aympqgLgkNL------------YPTL---SVFENLdffgrLFGQDAAERRRRIdELLRATGLAPFADR-PAG------- 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678196980 552 ggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:NF033858 136 ---KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
91-306 |
5.15e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 46.70 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 91 ILLLIGLITSVISGVsqpvlaiisgrMTNVLLVIdPLSKEFKTKTMENVYIFLGLGIFVSINDFCQYMCFQRVCSRMMTV 170
Cdd:cd18606 2 PLLLLLLILSQFAQV-----------FTNLWLSF-WTEDFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 171 MRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYEWRLALMMLGLIpvst 250
Cdd:cd18606 70 LHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLL---- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 251 ICMTLLSRFLEKSTGE--ELEKVGEAGAIAE--ECLMGVRTIQAFNGQEEMVAKYEKQLN 306
Cdd:cd18606 146 VLYYFIANYYRASSRElkRLESILRSFVYANfsESLSGLSTIRAYGAQDRFIKKNEKLID 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
555-633 |
5.37e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTIREA-DKIVFFEKGVIV 632
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
.
gi 1678196980 633 E 633
Cdd:PRK09700 489 Q 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1219-1252 |
5.43e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 5.43e-05
10 20 30
....*....|....*....|....*....|....
gi 1678196980 1219 GQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1082-1304 |
5.45e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1082 ILFENVKFSYPQRPhqPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGAL------RM--------DGQD 1147
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvRMavfsqhhvDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1148 IK-NISLYHLRTQMALVGQEPRLFVGTirenvcLGLKDvplekiNQALELANAnrflgnlpdgidtevgerggqLSGGQK 1226
Cdd:PLN03073 587 LSsNPLLYMMRCFPGVPEQKLRAHLGS------FGVTG------NLALQPMYT---------------------LSGGQK 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1227 QRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRAREGrtCITIAHRLSSIQNS-DLIVYIDDGRVQE-SGTHKE 1304
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFHD 711
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
555-616 |
5.95e-05 |
|
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: 47.47 E-value: 5.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLST 616
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRElAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
802-986 |
7.80e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 46.32 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 802 LAMSVIAHCAAGLGIWffQTLstvMFAIVSENLGVRFRVAAFRNLLYQDAAYFDNpaHAPGSLITRLAADPPCVKAVVDG 881
Cdd:cd18550 43 LGMVAVAVASALLGVV--QTY---LSARIGQGVMYDLRVQLYAHLQRMSLAFFTR--TRTGEIQSRLNNDVGGAQSVVTG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 882 RMMQVVYATAAVIACVTIGFINCWQVAILGTALIFLLGFIMAGLAFKISIVAAEHME-NDDAGKIAIEI--IENVKTIQL 958
Cdd:cd18550 116 TLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEkLAELNSIMQETlsVSGALLVKL 195
|
170 180
....*....|....*....|....*...
gi 1678196980 959 LTRTRRFLNSYENESKKRKRTELRKSVY 986
Cdd:cd18550 196 FGREDDEAARFARRSRELRDLGVRQALA 223
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
156-306 |
7.84e-05 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 46.26 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 156 QYmCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGVGDKLGVLIRGISMVIASVVISLIYE 235
Cdd:cd18554 67 QY-FAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLN 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 236 WRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLN 306
Cdd:cd18554 146 PKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNG 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
77-307 |
8.63e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 46.05 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 77 SLLQLFRFATTFDYILLLIGLITSVIsgvsqpVLAIISGRMTNVLLVIdplskefktktmenVYIFLGLGIFVSINDFCQ 156
Cdd:cd18782 3 ALIEVLALSFVVQLLGLANPLLFQVI------IDKVLVQQDLATLYVI--------------GVVMLVAALLEAVLTALR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 157 YMCFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDnMERIQD-GVGDKLGVLIRGISMVIASVVIsLIYE 235
Cdd:cd18782 63 TYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISE-LDTIRGfLTGTALTTLLDVLFSVIYIAVL-FSYS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678196980 236 WRLALMMLGLIPVSTICMTLLSRFLEKSTGEELEKVGEAGAIAEECLMGVRTIQAFNGQEEMVAKYEKQLNS 307
Cdd:cd18782 141 PLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYAR 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1094-1254 |
8.70e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1094 RPHQPVMKQLQWTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISlyhlRTQ-MALVGQEPrlfvg 1172
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1173 tirenvclGLK-DVP-LEKIN--QALELANANRFLGN------LPDGIDTEVGerggQLSGGQKQRIAIARALVRDPKIL 1242
Cdd:PRK13543 92 --------GLKaDLStLENLHflCGLHGRRAKQMPGSalaivgLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|..
gi 1678196980 1243 LLDEATSALDSE 1254
Cdd:PRK13543 160 LLDEPYANLDLE 171
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1190-1252 |
9.45e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 9.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1190 INQALELANANRFLGNLPdgIDTEVGE-RGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PRK13549 376 IDDAAELKTILESIQRLK--VKTASPElAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
554-624 |
1.03e-04 |
|
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: 44.27 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678196980 554 VQLSGGQKQRVAIA-----RTLIRDPkVLLLDEATSALDAQS-ESVVQSALNNASKGRTTIMIAHRLSTIREADKIV 624
Cdd:cd03227 76 LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1215-1305 |
1.28e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1215 GERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAV-QEALDRAREGRTC-ITIAHRLSSIQNSDLIVYID 1292
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVlLTTQYMEEAEQLAHELTVID 218
|
90
....*....|...
gi 1678196980 1293 DGRVQESGTHKEL 1305
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1187-1252 |
1.84e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1187 LEKINQALEL-------ANANRFLGNLPDGIDTEVgERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PLN03073 305 LEEIYKRLELidaytaeARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1219-1264 |
1.93e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1678196980 1219 GQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALD 1264
Cdd:PRK11819 444 GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1109-1298 |
1.94e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYH-LRTQMALVGQEPRL--FVG--TIRENVCLG-- 1181
Cdd:PRK09700 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITESRRDngFFPnfSIAQNMAISrs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1182 LKDVPLEK----INQALE--LANANRFLGNLP-DGIDTEVGErggqLSGGQKQRIAIARALVRDPKILLLDEATSALDSE 1254
Cdd:PRK09700 368 LKDGGYKGamglFHEVDEqrTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVG 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678196980 1255 SERAVQEALDR-AREGRTCITIAHRLSSIQN-SDLIVYIDDGRVQE 1298
Cdd:PRK09700 444 AKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1089-1296 |
2.49e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1089 FSYPQRPHQPVMKQLQ------------WTALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYH- 1155
Cdd:PRK11288 246 YGYRPRPLGEVRLRLDglkgpglrepisFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDa 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1156 LRTQMALVgQEPRLFVG-----TIRENV------------CLglkdvplekINQALELANANRFLGNLpdGIDTEVGERG 1218
Cdd:PRK11288 326 IRAGIMLC-PEDRKAEGiipvhSVADNInisarrhhlragCL---------INNRWEAENADRFIRSL--NIKTPSREQL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1219 -GQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEAL-DRAREGRTCITIAHRLSSIQN-SDLIVYIDDGR 1295
Cdd:PRK11288 394 iMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGR 473
|
.
gi 1678196980 1296 V 1296
Cdd:PRK11288 474 I 474
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1110-1306 |
2.51e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKS-----TCiGMLERFYDVTGGALRMDGQDIKNISLYHLRT----QMALVGQEPRlfvgtirenVCL 1180
Cdd:PRK15093 33 GEIRGLVGESGSGKSliakaIC-GVTKDNWRVTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEPQ---------SCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1181 GlkdvPLEKINQALELANA---------NRFLGNLPDGIdtEVGERGG-------------QLSGGQKQRIAIARALVRD 1238
Cdd:PRK15093 103 D----PSERVGRQLMQNIPgwtykgrwwQRFGWRKRRAI--ELLHRVGikdhkdamrsfpyELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1239 PKILLLDEATSALDSESERAVQEALDRARE--GRTCITIAHRLSSI-QNSDLIVYIDDGRVQESGTHKELM 1306
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
133-306 |
2.88e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 44.44 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 133 TKTMENVYIFLGLG--IFVSINDFCqymcFQRVCSRMMTVMRNRYISSILRQNAGWFDKNLSGTITTRLNDNMERIQDGV 210
Cdd:cd18605 41 FNFFLTVYGFLAGLnsLFTLLRAFL----FAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 211 GDKLGVLIRGISMVIASVVIsLIYEwrLALMMLGLIPVStICMTLLSRFLEKSTGE--ELEKVGEAGAIA--EECLMGVR 286
Cdd:cd18605 117 PFILNILLAQLFGLLGYLVV-ICYQ--LPWLLLLLLPLA-FIYYRIQRYYRATSRElkRLNSVNLSPLYThfSETLKGLV 192
|
170 180
....*....|....*....|
gi 1678196980 287 TIQAFNGQEEMVAKYEKQLN 306
Cdd:cd18605 193 TIRAFRKQERFLKEYLEKLE 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1110-1307 |
3.60e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQDIKNISLYHLR-----------TQMALVGQEPrlFVGTIRENV 1178
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQklvsdewqrnnTDMLSPGEDD--TGRTTAEII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1179 CLGLKDVPLekinqALELANanRFlgnlpdGIDTEVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERA 1258
Cdd:PRK10938 107 QDEVKDPAR-----CEQLAQ--QF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1259 VQEALDR-AREGRTCITIAHRLSSIqnSDLIVYI---DDGRVQESGTHKELMQ 1307
Cdd:PRK10938 174 LAELLASlHQSGITLVLVLNRFDEI--PDFVQFAgvlADCTLAETGEREEILQ 224
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
430-624 |
3.65e-04 |
|
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: 43.76 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 430 KEAKVLNGLNLTVE-P-GTSVALVGHSGCGKSTSVG--LLTRLYEPEQGSVQIDGVDVRDLNLEWLRNVVGIvQQEPI-- 503
Cdd:cd03271 4 KGARENNLKNIDVDiPlGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVI-DQSPIgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 504 -----------LFnDTIHNnlLF----GNPDATRETM-IR--------VCKM--ANAHDFIKKMPK-------------G 544
Cdd:cd03271 83 tprsnpatytgVF-DEIRE--LFcevcKGKRYNRETLeVRykgksiadVLDMtvEEALEFFENIPKiarklqtlcdvglG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 545 YdTQIGDGGVQLSGGQKQRVAIARTLIR---DPKVLLLDEATSAL---DAQSESVVQSALnnASKGRTTIMIAHRLSTIR 618
Cdd:cd03271 160 Y-IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLhfhDVKKLLEVLQRL--VDKGNTVVVIEHNLDVIK 236
|
....*.
gi 1678196980 619 EADKIV 624
Cdd:cd03271 237 CADWII 242
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
431-620 |
4.80e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 431 EAKVLNGLNLTVEPGTSVALVGHSGCGKSTSVGLLTRLYEPEQGSVQIDGVDVRDLNLEWLRNvvgIVQQEPILFNDTIH 510
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY---IGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 511 NNLLFG----NPDATRETMIRVCKManaHDFIKKmpKGYdtqigdggvQLSGGQKQRVAIARTLIRDPKVLLLDEATSAL 586
Cdd:PRK13541 89 ENLKFWseiyNSAETLYAAIHYFKL---HDLLDE--KCY---------SLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1678196980 587 DAQSESVvqsaLNN-----ASKGRTTIMIAHRLSTIREA 620
Cdd:PRK13541 155 SKENRDL----LNNlivmkANSGGIVLLSSHLESSIKSA 189
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1106-1322 |
6.27e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1106 TALRGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGqDIKNISLYH-LRTQmaLVGQEPRLFvgtirENVCLGLKD 1184
Cdd:PRK13546 46 KAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAgLSGQ--LTGIENIEF-----KMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1185 VPLEKInqalelananrflgnLPDGID-TEVGERGGQ----LSGGQKQRIAIARALVRDPKILLLDEATSALDsesERAV 1259
Cdd:PRK13546 118 KEIKAM---------------TPKIIEfSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 1260 QEALDRARE----GRTCITIAHRLSSIQN-SDLIVYIDDGRVQESGTHKELMQLKGKYFELIKKQDLA 1322
Cdd:PRK13546 180 QKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKA 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
395-610 |
7.43e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 395 DRVPKIDPYsrhgkkiekvVGKVTFE----NVHfrYPTRKEAKVLNGLNLTVEPGTSVALVGHSGCGKS-TSVGLLTRLY 469
Cdd:NF040905 244 DRYPERTPK----------IGEVVFEvknwTVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSY 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 470 -EPEQGSVQIDGVDVRdlnlewLRNV-----------------VGIVQQEPILFNDTIHNnlL-----FGNPDATRETMI 526
Cdd:NF040905 312 gRNISGTVFKDGKEVD------VSTVsdaidaglayvtedrkgYGLNLIDDIKRNITLAN--LgkvsrRGVIDENEEIKV 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 527 rvckmanAHDFIKKMpkgydtQIGDGGV-----QLSGGQKQRVAIARTLIRDPKVLLLDEATSALD--AQSE--SVVQSA 597
Cdd:NF040905 384 -------AEEYRKKM------NIKTPSVfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYEiyTIINEL 450
|
250
....*....|...
gi 1678196980 598 lnnASKGRTTIMI 610
Cdd:NF040905 451 ---AAEGKGVIVI 460
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
555-630 |
7.88e-04 |
|
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: 42.63 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIArtLIR-----DPK-VLLLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKI--VFF 626
Cdd:cd03272 158 QLSGGQKSLVALA--LIFaiqkcDPApFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFygVKF 235
|
....
gi 1678196980 627 EKGV 630
Cdd:cd03272 236 RNKV 239
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1221-1310 |
7.96e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1221 LSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALDRArEGrTCITIAH-R--LSSIQNSdlIVYI-DDGRV 1296
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSLATR--IIEItPDGVV 514
|
90
....*....|....
gi 1678196980 1297 QESGTHKELMQLKG 1310
Cdd:PRK15064 515 DFSGTYEEYLRSQG 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1213-1263 |
8.39e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 8.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1678196980 1213 EVGERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEAL 1263
Cdd:PRK10636 423 KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
556-617 |
9.36e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.27 E-value: 9.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 556 LSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNN-ASKGRTTIMIAHRLSTI 617
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV 466
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1221-1289 |
1.00e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 1221 LSGGQKQRIAIARALVRD---PKILLLDEATSALDSESERAVQEALDRARE-GRTCITIAHRLSSIQNSDLIV 1289
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYII 902
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
555-587 |
1.01e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|...
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALD 587
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1110-1252 |
1.04e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1110 GQTVALVGPSGSGKSTcigMLERFY---DVTGGALRMDGQDIKNISLYHlRTQMALV-----GQEPRLFV-GTIRENVCL 1180
Cdd:PRK15439 289 GEILGLAGVVGAGRTE---LAETLYglrPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYLdAPLAWNVCA 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678196980 1181 GLKDVPLEKINQALELANANRF---LGNLPDGIDTEVGerggQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:PRK15439 365 LTHNRRGFWIKPARENAVLERYrraLNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
537-624 |
1.11e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 537 FIKKMPKGYDTQIGDGGVQLSGGQ---------KQRVAIARTLIRDPK---VLLLDEATSALDAQSESVVQSALNN-ASK 603
Cdd:PRK00635 1672 FLKKIQKPLQALIDNGLGYLPLGQnlsslslseKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSL 1751
|
90 100
....*....|....*....|.
gi 1678196980 604 GRTTIMIAHRLSTIREADKIV 624
Cdd:PRK00635 1752 GHSVIYIDHDPALLKQADYLI 1772
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
799-1009 |
1.18e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 42.62 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 799 MHRLAMSVIAHCAAGLGIWFFQTLSTVMFAIVSENLGVRFRVAAFRNLLYQDAAYFDnpAHAPGSLITRLAADPPCVKAV 878
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 879 VDGRMMQVVYATAAVIACVTIGFINCWQVAILGTALIFLLGFIMAGLAFKISIVAAEHMEN-DDAGKIAIEIIENVKTIQ 957
Cdd:cd18780 116 VTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDAlAAASTVAEESISNIRTVR 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678196980 958 lltrtrrflnSYENESKKRKRTElrKSVYEAVNYCISQNFMY-YMSCFCFALA 1009
Cdd:cd18780 196 ----------SFAKETKEVSRYS--EKINESYLLGKKLARASgGFNGFMGAAA 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1109-1310 |
1.48e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1109 RGQTVALVGPSGSGKSTCIGMLERFYDVTGGALRMDGQ--DIKNIslyhlrtqmalvgqEPRLFVG------------TI 1174
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDI--------------ATRRRVGymsqafslygelTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1175 RENVCLG--LKDVPLEKINQALELAnANRFlgNLPDGIDtevgERGGQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:NF033858 357 RQNLELHarLFHLPAAEIAARVAEM-LERF--DLADVAD----ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1253 SESERAVQEAL-DRAREGRTCITIA-HRLSSIQNSDLIVYIDDGRVQESGTHKELMQLKG 1310
Cdd:NF033858 430 PVARDMFWRLLiELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
555-612 |
1.79e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678196980 555 QLSGGQKQRVAIARTLIRDPKVLLLDEATSALDAQSESVVQSALNNASKgrTTIMIAH 612
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSH 399
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
555-631 |
2.01e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 555 QLSGGQKQRVAIArtLI-----RDPKVL-LLDEATSALDAQSESVVQSALNNASKGRTTIMIAHRLSTIREADKIV---F 625
Cdd:pfam02463 1077 LLSGGEKTLVALA--LIfaiqkYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVgvtM 1154
|
....*.
gi 1678196980 626 FEKGVI 631
Cdd:pfam02463 1155 VENGVS 1160
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
545-588 |
2.45e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 2.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1678196980 545 YDTQIGDGGVQ-LSGGQKQRVAIARTLIRDPKVLLLDEATSALDA 588
Cdd:TIGR00956 198 RNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1076-1252 |
5.19e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1076 PEIrGNILFE----NVKfsYPQRPHQPVMKQLQWTALRGQTVALVGPSGSGKsTCIGM--LERFYDV-TGGALRMDGQDI 1148
Cdd:NF040905 251 PKI-GEVVFEvknwTVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELAMsvFGRSYGRnISGTVFKDGKEV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 1149 knislyHLRTQMALVGQ------EPRLFVG-----TIRENVCL-GLKDV-PLEKINQALELANANRFLGNL----PdGID 1211
Cdd:NF040905 327 ------DVSTVSDAIDAglayvtEDRKGYGlnlidDIKRNITLaNLGKVsRRGVIDENEEIKVAEEYRKKMniktP-SVF 399
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1678196980 1212 TEVGerggQLSGGQKQRIAIARALVRDPKILLLDEATSALD 1252
Cdd:NF040905 400 QKVG----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1224-1277 |
5.64e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 5.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1678196980 1224 GQKQRIAIARALVRDPKILLLDEATSALDSESERAVQEALdRAREGrTCITIAH 1277
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL-NERNS-TMIIISH 210
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
541-621 |
6.79e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678196980 541 MPKGYDTqigdggvqLSGGQKQ------RVAIARTLIRDPKVLLLDEATSALDAQSES----VVQSALNNASKGRTTIMI 610
Cdd:PRK01156 795 MVEGIDS--------LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQVIMI 866
|
90
....*....|.
gi 1678196980 611 AHRLSTIREAD 621
Cdd:PRK01156 867 SHHRELLSVAD 877
|
|
| |
